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Volumn 73, Issue 14, 2016, Pages 2619-2641

Structure and function of α-glucan debranching enzymes

Author keywords

Carbohydrate binding modules; Domain architecture; Glycoside hydrolase family 13 subfamilies; Multi domain three dimensional structure; Phylogeny; Sequence motifs and determinants; Structure function relationship; Substrate specificity

Indexed keywords

ALPHA GLUCAN DEBRANCHING ENZYME; CARBOHYDRATE BINDING MODULE 20; CARBOHYDRATE BINDING MODULE 34; CARBOHYDRATE BINDING MODULE 41; CARBOHYDRATE BINDING MODULE 48; CARBOHYDRATE BINDING MODULE 68; CARBOHYDRATE BINDING PROTEIN; GLUCAN ALPHA GLUCOSIDASE; GLYCOGEN DEBRANCHING ENZYME; GLYCOSIDASE; GLYCOSYLTRANSFERASE; ISOAMYLASE; MALTOGENIC ALPHA AMYLASE; OLIGO 1,6 GLUCOSIDASE; OLIGO ALPHA GLUCOSIDASE; PULLULAN HYDROLASE; PULLULANASE; PULLULANASE TYPE I; PULLULANASE TYPE II; PULLULANASE TYPE II WITH ONE CATALYTIC DOMAIN; PULLULANASE TYPE II WITH TWO CATALYTIC DOMAIN; UNCLASSIFIED DRUG; GLUCAN; GLYCOGEN;

EID: 84965052610     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-016-2241-y     Document Type: Review
Times cited : (79)

References (162)
  • 1
    • 62949176124 scopus 로고    scopus 로고
    • Bioproducts from Aureobasidium pullulans, a biotechnologically important yeast
    • COI: 1:CAS:528:DC%2BD1MXjsVWgu7w%3D, PID: 19198830
    • Chi Z, Wang F, Chi Z, Yue L, Liu G, Zhang T (2009) Bioproducts from Aureobasidium pullulans, a biotechnologically important yeast. Appl Microbiol Biotechnol 82(5):793–804
    • (2009) Appl Microbiol Biotechnol , vol.82 , Issue.5 , pp. 793-804
    • Chi, Z.1    Wang, F.2    Chi, Z.3    Yue, L.4    Liu, G.5    Zhang, T.6
  • 2
    • 84922718832 scopus 로고    scopus 로고
    • Structure-function relationships of starch components
    • COI: 1:CAS:528:DC%2BC2cXitVChsrnI
    • Vamadevan V, Bertoft E (2015) Structure-function relationships of starch components. Starch Stärke 67(1–2):55–68
    • (2015) Starch Stärke , vol.67 , Issue.1-2 , pp. 55-68
    • Vamadevan, V.1    Bertoft, E.2
  • 3
    • 84855929671 scopus 로고    scopus 로고
    • Glycogen and its metabolism: some new developments and old themes
    • COI: 1:CAS:528:DC%2BC38XovFKktg%3D%3D, PID: 22248338
    • Roach PJ, Depaoli-Roach AA, Hurley TD, Tagliabracci VS (2012) Glycogen and its metabolism: some new developments and old themes. Biochem J 441:763–787
    • (2012) Biochem J , vol.441 , pp. 763-787
    • Roach, P.J.1    Depaoli-Roach, A.A.2    Hurley, T.D.3    Tagliabracci, V.S.4
  • 4
    • 84891763855 scopus 로고    scopus 로고
    • The carbohydrate-active enzymes database (CAZy) in 2013
    • COI: 1:CAS:528:DC%2BC2cXoslWn, PID: 24270786
    • Lombard V, Ramulu HG, Drula E, Coutinho PM, Henrissat B (2014) The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res 42(D1):D490–D495
    • (2014) Nucleic Acids Res , vol.42 , Issue.D1 , pp. D490-D495
    • Lombard, V.1    Ramulu, H.G.2    Drula, E.3    Coutinho, P.M.4    Henrissat, B.5
  • 5
    • 33845665889 scopus 로고    scopus 로고
    • Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins
    • COI: 1:CAS:528:DC%2BD28Xht1Ohu7rJ, PID: 17085431
    • Stam MR, Danchin EGJ, Rancurel C, Coutinho PM, Henrissat B (2006) Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins. Protein Eng Des Sel 19(12):555–562
    • (2006) Protein Eng Des Sel , vol.19 , Issue.12 , pp. 555-562
    • Stam, M.R.1    Danchin, E.G.J.2    Rancurel, C.3    Coutinho, P.M.4    Henrissat, B.5
  • 6
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the α-amylase family of enzymes
    • COI: 1:CAS:528:DC%2BD3MXhvVagtLk%3D
    • MacGregor EA, Janeček S, Svensson B (2001) Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochim Biophys Acta Protein Struct Mol Enzymol 1546(1):1–20
    • (2001) Biochim Biophys Acta Protein Struct Mol Enzymol , vol.1546 , Issue.1 , pp. 1-20
    • MacGregor, E.A.1    Janeček, S.2    Svensson, B.3
  • 7
    • 0032976301 scopus 로고    scopus 로고
    • The concept of the α-amylase family: structural similarity and common catalytic mechanism
    • COI: 1:CAS:528:DyaK1MXltFCmu74%3D, PID: 16232518
    • Kuriki T, Imanaka T (1999) The concept of the α-amylase family: structural similarity and common catalytic mechanism. J Biosci Bioeng 87(5):557–565
    • (1999) J Biosci Bioeng , vol.87 , Issue.5 , pp. 557-565
    • Kuriki, T.1    Imanaka, T.2
  • 8
    • 84899863334 scopus 로고    scopus 로고
    • α-Amylase: an enzyme specificity found in various families of glycoside hydrolases
    • COI: 1:CAS:528:DC%2BC3sXhtVGjsrvE, PID: 23807207
    • Janecek S, Svensson B, MacGregor EA (2014) α-Amylase: an enzyme specificity found in various families of glycoside hydrolases. Cell Mol Life Sci 71(7):1149–1170
    • (2014) Cell Mol Life Sci , vol.71 , Issue.7 , pp. 1149-1170
    • Janecek, S.1    Svensson, B.2    MacGregor, E.A.3
  • 9
    • 81055147824 scopus 로고    scopus 로고
    • Sequence-structural features and evolutionary relationships of family GH57 α-amylases and their putative α-amylase-like homologues
    • COI: 1:CAS:528:DC%2BC3MXpt1aqtLo%3D, PID: 21786160
    • Janecek S, Blesak K (2011) Sequence-structural features and evolutionary relationships of family GH57 α-amylases and their putative α-amylase-like homologues. Protein J 30(6):429–435
    • (2011) Protein J , vol.30 , Issue.6 , pp. 429-435
    • Janecek, S.1    Blesak, K.2
  • 10
    • 84902470011 scopus 로고    scopus 로고
    • Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04
    • COI: 1:CAS:528:DC%2BC2cXpsVGnsrw%3D
    • Park K, Jung J, Park S, Lee M, Holden JF, Park C, Woo E (2014) Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04. Acta Crystallogr Sect D Biol Crystallogr 70(6):1659–1668
    • (2014) Acta Crystallogr Sect D Biol Crystallogr , vol.70 , Issue.6 , pp. 1659-1668
    • Park, K.1    Jung, J.2    Park, S.3    Lee, M.4    Holden, J.F.5    Park, C.6    Woo, E.7
  • 11
    • 3242816124 scopus 로고    scopus 로고
    • Bioinformatics of the glycoside hydrolase family 57 and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis
    • COI: 1:CAS:528:DC%2BD2cXmtVyrtLw%3D, PID: 15233783
    • Zona R, Chang-Pi-Hin F, O’Donohue M, Janecek S (2004) Bioinformatics of the glycoside hydrolase family 57 and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis. Eur J Biochem 271(14):2863–2872
    • (2004) Eur J Biochem , vol.271 , Issue.14 , pp. 2863-2872
    • Zona, R.1    Chang-Pi-Hin, F.2    O’Donohue, M.3    Janecek, S.4
  • 12
    • 12144255190 scopus 로고    scopus 로고
    • Identification of Pyrococcus furiosus amylopullulanase catalytic residues
    • COI: 1:CAS:528:DC%2BD2cXhtVKrur%2FK, PID: 15599521
    • Kang S, Vieille C, Zeikus J (2005) Identification of Pyrococcus furiosus amylopullulanase catalytic residues. Appl Microbiol Biotechnol 66(4):408–413
    • (2005) Appl Microbiol Biotechnol , vol.66 , Issue.4 , pp. 408-413
    • Kang, S.1    Vieille, C.2    Zeikus, J.3
  • 13
    • 33748670795 scopus 로고    scopus 로고
    • Amylolytic families of glycoside hydrolases: focus on the family GH-57
    • Janeček S (2005) Amylolytic families of glycoside hydrolases: focus on the family GH-57. Biologia 60:177–184
    • (2005) Biologia , vol.60 , pp. 177-184
    • Janeček, S.1
  • 14
    • 84860839630 scopus 로고    scopus 로고
    • Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57
    • COI: 1:CAS:528:DC%2BC38XmvVKgsr8%3D, PID: 22527043
    • Blesak K, Janecek S (2012) Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57. Extremophiles 16(3):497–506
    • (2012) Extremophiles , vol.16 , Issue.3 , pp. 497-506
    • Blesak, K.1    Janecek, S.2
  • 16
    • 84905991993 scopus 로고    scopus 로고
    • Crystal structure of the Chlamydomonas starch debranching enzyme isoamylase ISA1 reveals insights into the mechanism of branch trimming and complex assembly
    • COI: 1:CAS:528:DC%2BC2cXhtlGmtbjP, PID: 24993830
    • Sim L, Beeren SR, Findinier J, Dauvillee D, Ball SG, Henriksen A, Palcic MM (2014) Crystal structure of the Chlamydomonas starch debranching enzyme isoamylase ISA1 reveals insights into the mechanism of branch trimming and complex assembly. J Biol Chem 289(33):22991–23003
    • (2014) J Biol Chem , vol.289 , Issue.33 , pp. 22991-23003
    • Sim, L.1    Beeren, S.R.2    Findinier, J.3    Dauvillee, D.4    Ball, S.G.5    Henriksen, A.6    Palcic, M.M.7
  • 18
    • 79952814469 scopus 로고    scopus 로고
    • Starch biosynthesis in developing seeds
    • COI: 1:CAS:528:DC%2BC3MXhtlCisA%3D%3D
    • Tetlow IJ (2011) Starch biosynthesis in developing seeds. Seed Sci Res 21(1):5–32
    • (2011) Seed Sci Res , vol.21 , Issue.1 , pp. 5-32
    • Tetlow, I.J.1
  • 19
    • 77953494275 scopus 로고    scopus 로고
    • Structural rationale for the short branched substrate specificity of the glycogen debranching enzyme GlgX
    • COI: 1:CAS:528:DC%2BC3cXkvFegt70%3D
    • Song H, Jung T, Park J, Park B, Myung PK, Boos W, Woo E, Park K (2010) Structural rationale for the short branched substrate specificity of the glycogen debranching enzyme GlgX. Proteins: Struct Funct Bioinf 78(8):1847–1855
    • (2010) Proteins: Struct Funct Bioinf , vol.78 , Issue.8 , pp. 1847-1855
    • Song, H.1    Jung, T.2    Park, J.3    Park, B.4    Myung, P.K.5    Boos, W.6    Woo, E.7    Park, K.8
  • 20
    • 0032863715 scopus 로고    scopus 로고
    • Expression of the isoamylase gene of Flavobacterium odoratum KU in Escherichia coli and identification of essential residues of the enzyme by site-directed mutagenesis
    • COI: 1:CAS:528:DyaK1MXlvFCjsr4%3D, PID: 10473430
    • Abe J, Ushijima C, Hizukuri S (1999) Expression of the isoamylase gene of Flavobacterium odoratum KU in Escherichia coli and identification of essential residues of the enzyme by site-directed mutagenesis. Appl Environ Microbiol 65(9):4163–4170
    • (1999) Appl Environ Microbiol , vol.65 , Issue.9 , pp. 4163-4170
    • Abe, J.1    Ushijima, C.2    Hizukuri, S.3
  • 21
    • 0030573162 scopus 로고    scopus 로고
    • Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius
    • COI: 1:CAS:528:DyaK28XmslyhsL0%3D, PID: 8980629
    • Maruta K, Mitsuzumi H, Nakada T, Kubota M, Chaen H, Fukuda S, Sugimoto T, Kurimoto M (1996) Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius. Biochim Biophys Acta 1291(3):177–181
    • (1996) Biochim Biophys Acta , vol.1291 , Issue.3 , pp. 177-181
    • Maruta, K.1    Mitsuzumi, H.2    Nakada, T.3    Kubota, M.4    Chaen, H.5    Fukuda, S.6    Sugimoto, T.7    Kurimoto, M.8
  • 22
    • 34250184680 scopus 로고    scopus 로고
    • Cloning and characterization of glycogen-debranching enzyme from hyperthermophilic archaeon Sulfolobus shibatae
    • Van TTK, Ryu S, Lee K, Kim E, Lee S (2007) Cloning and characterization of glycogen-debranching enzyme from hyperthermophilic archaeon Sulfolobus shibatae. J Microbiol Biotechn 17(5):792–799
    • (2007) J Microbiol Biotechn , vol.17 , Issue.5 , pp. 792-799
    • Van, T.T.K.1    Ryu, S.2    Lee, K.3    Kim, E.4    Lee, S.5
  • 23
    • 34447544538 scopus 로고    scopus 로고
    • The glgX gene product of Corynebacterium glutamicum is required for glycogen degradation and for fast adaptation to hyperosmotic stress
    • COI: 1:CAS:528:DC%2BD2sXot1Wltbo%3D
    • Seibold GM, Eikmanns BJ (2007) The glgX gene product of Corynebacterium glutamicum is required for glycogen degradation and for fast adaptation to hyperosmotic stress. Microbiol SGM 153:2212–2220
    • (2007) Microbiol SGM , vol.153 , pp. 2212-2220
    • Seibold, G.M.1    Eikmanns, B.J.2
  • 24
    • 0030926237 scopus 로고    scopus 로고
    • An isoamylase with neutral pH optimum from a Flavobacterium species: cloning, characterization and expression of the iam gene
    • COI: 1:CAS:528:DyaK2sXjvFWjtrY%3D, PID: 9197405
    • Krohn B, Barry G, Kishore G (1997) An isoamylase with neutral pH optimum from a Flavobacterium species: cloning, characterization and expression of the iam gene. Mol Gen Genet 254(5):469–478
    • (1997) Mol Gen Genet , vol.254 , Issue.5 , pp. 469-478
    • Krohn, B.1    Barry, G.2    Kishore, G.3
  • 25
    • 0033118441 scopus 로고    scopus 로고
    • Purification, characterization, and cDNA structure of isoamylase from developing endosperm of rice
    • COI: 1:CAS:528:DyaK1MXjtFejtb8%3D, PID: 10333591
    • Fujita N, Kubo A, Francisco P, Nakakita M, Harada K, Minaka N, Nakamura Y (1999) Purification, characterization, and cDNA structure of isoamylase from developing endosperm of rice. Planta 208(2):283–293
    • (1999) Planta , vol.208 , Issue.2 , pp. 283-293
    • Fujita, N.1    Kubo, A.2    Francisco, P.3    Nakakita, M.4    Harada, K.5    Minaka, N.6    Nakamura, Y.7
  • 26
    • 0034659896 scopus 로고    scopus 로고
    • Localization of C-terminal domains required for the maximal activity or for determination of substrate preference of maize branching enzymes
    • COI: 1:CAS:528:DC%2BD3cXktVGqurY%3D, PID: 10860552
    • Hong S, Preiss J (2000) Localization of C-terminal domains required for the maximal activity or for determination of substrate preference of maize branching enzymes. Arch Biochem Biophys 378(2):349–355
    • (2000) Arch Biochem Biophys , vol.378 , Issue.2 , pp. 349-355
    • Hong, S.1    Preiss, J.2
  • 27
    • 1842788556 scopus 로고    scopus 로고
    • Functional characteristics of C-terminal regions of starch-branching enzymes from developing seeds of kidney bean (Phaseolus vulgaris L.)
    • COI: 1:CAS:528:DC%2BD2cXivVWmu70%3D
    • Ito H, Hamada S, Isono N, Yoshizaki T, Ueno H, Yoshimoto Y, Takeda Y, Matsui H (2004) Functional characteristics of C-terminal regions of starch-branching enzymes from developing seeds of kidney bean (Phaseolus vulgaris L.). Plant Sci 166(5):1149–1158
    • (2004) Plant Sci , vol.166 , Issue.5 , pp. 1149-1158
    • Ito, H.1    Hamada, S.2    Isono, N.3    Yoshizaki, T.4    Ueno, H.5    Yoshimoto, Y.6    Takeda, Y.7    Matsui, H.8
  • 28
    • 61649113784 scopus 로고    scopus 로고
    • The unique branching patterns of Deinococcus glycogen branching enzymes are determined by their N-terminal domains
    • COI: 1:CAS:528:DC%2BD1MXjtVyqs7k%3D
    • Palomo M, Kralj S, van der Maarel MJEC, Dijkhuizen L (2009) The unique branching patterns of Deinococcus glycogen branching enzymes are determined by their N-terminal domains. Apple Environ Microbiol 75(5):1355–1362
    • (2009) Apple Environ Microbiol , vol.75 , Issue.5 , pp. 1355-1362
    • Palomo, M.1    Kralj, S.2    van der Maarel, M.J.E.C.3    Dijkhuizen, L.4
  • 29
    • 0032483304 scopus 로고    scopus 로고
    • Three-dimensional structure of Pseudomonas isoamylase at 2.2 angstrom resolution
    • COI: 1:CAS:528:DyaK1cXmtVygsrc%3D, PID: 9719642
    • Katsuya Y, Mezaki Y, Kubota M, Matsuura Y (1998) Three-dimensional structure of Pseudomonas isoamylase at 2.2 angstrom resolution. J Mol Biol 281(5):885–897
    • (1998) J Mol Biol , vol.281 , Issue.5 , pp. 885-897
    • Katsuya, Y.1    Mezaki, Y.2    Kubota, M.3    Matsuura, Y.4
  • 30
    • 57649133949 scopus 로고    scopus 로고
    • Structural insight into the bifunctional mechanism of the glycogen-debranching enzyme TreX from the archaeon Sulfolobus solfataricus
    • COI: 1:CAS:528:DC%2BD1cXht1ans7jF, PID: 18703518
    • Woo E, Lee S, Cha H, Park J, Yoon S, Song H, Park K (2008) Structural insight into the bifunctional mechanism of the glycogen-debranching enzyme TreX from the archaeon Sulfolobus solfataricus. J Biol Chem 283(42):28641–28648
    • (2008) J Biol Chem , vol.283 , Issue.42 , pp. 28641-28648
    • Woo, E.1    Lee, S.2    Cha, H.3    Park, J.4    Yoon, S.5    Song, H.6    Park, K.7
  • 31
    • 80054923047 scopus 로고    scopus 로고
    • Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases
    • COI: 1:CAS:528:DC%2BC38XmsFOjur4%3D, PID: 21711082
    • Cuyvers S, Dornez E, Delcour JA, Courtin CM (2012) Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases. Crit Rev Biotechnol 32(2):93–107
    • (2012) Crit Rev Biotechnol , vol.32 , Issue.2 , pp. 93-107
    • Cuyvers, S.1    Dornez, E.2    Delcour, J.A.3    Courtin, C.M.4
  • 32
    • 84896731376 scopus 로고    scopus 로고
    • Association of bi-functional activity in the N-terminal domain of glycogen debranching enzyme
    • COI: 1:CAS:528:DC%2BC2cXislGrtbw%3D, PID: 24491554
    • Min-ho L, Hyung-Nam S, Ji-Eun C, Lan TP, Sunghoon P, Jong-Tae P, Eui-Jeon W (2014) Association of bi-functional activity in the N-terminal domain of glycogen debranching enzyme. Biochem Biophys Res Commun 445(1):107–112
    • (2014) Biochem Biophys Res Commun , vol.445 , Issue.1 , pp. 107-112
    • Min-ho, L.1    Hyung-Nam, S.2    Ji-Eun, C.3    Lan, T.P.4    Sunghoon, P.5    Jong-Tae, P.6    Eui-Jeon, W.7
  • 33
    • 0025778569 scopus 로고
    • Reassessment of the catalytic mechanism of glycogen debranching enzyme
    • COI: 1:CAS:528:DyaK3MXlvVSmtw%3D%3D, PID: 1991122
    • Liu W, Madsen N, Braun C, Withers S (1991) Reassessment of the catalytic mechanism of glycogen debranching enzyme. Biochemistry 30(5):1419–1424
    • (1991) Biochemistry , vol.30 , Issue.5 , pp. 1419-1424
    • Liu, W.1    Madsen, N.2    Braun, C.3    Withers, S.4
  • 34
    • 0035800737 scopus 로고    scopus 로고
    • Identification of the catalytic residues of bifunctional glycogen debranching enzyme
    • COI: 1:CAS:528:DC%2BD3MXlvFSru7w%3D, PID: 11375985
    • Nakayama A, Yamamoto K, Tabata S (2001) Identification of the catalytic residues of bifunctional glycogen debranching enzyme. J Biol Chem 276(31):28824–28828
    • (2001) J Biol Chem , vol.276 , Issue.31 , pp. 28824-28828
    • Nakayama, A.1    Yamamoto, K.2    Tabata, S.3
  • 35
    • 85007778637 scopus 로고
    • An alkaline amylopullulanase from alkalophilic Bacillus sp KSM-1378; kinetic evidence for 2 independent active-sites for the α-1,4 and α-1,6 hydrolytic reactions
    • COI: 1:CAS:528:DyaK2MXlsVSmtLY%3D
    • Ara K, Igarashi K, Saeki K, Ito S (1995) An alkaline amylopullulanase from alkalophilic Bacillus sp KSM-1378; kinetic evidence for 2 independent active-sites for the α-1,4 and α-1,6 hydrolytic reactions. Biosci Biotechnol Biochem 59(4):662–666
    • (1995) Biosci Biotechnol Biochem , vol.59 , Issue.4 , pp. 662-666
    • Ara, K.1    Igarashi, K.2    Saeki, K.3    Ito, S.4
  • 37
    • 84887560848 scopus 로고    scopus 로고
    • Recombinant bacterial amylopullulanases. Developments and perspectives
    • COI: 1:STN:280:DC%2BC3sngvVKksA%3D%3D, PID: 23645215
    • Nisha M, Satyanarayana T (2013) Recombinant bacterial amylopullulanases. Developments and perspectives. Bioengineered 4(6):388–400
    • (2013) Bioengineered , vol.4 , Issue.6 , pp. 388-400
    • Nisha, M.1    Satyanarayana, T.2
  • 38
    • 57849098719 scopus 로고    scopus 로고
    • Characterization of gene encoding amylopullulanase from plant-originated lactic acid bacterium, Lactobacillus plantarum L137
    • COI: 1:CAS:528:DC%2BD1MXhvVymsrg%3D, PID: 19111640
    • Kim J, Sunako M, Ono H, Murooka Y, Fukusaki E, Yamashita M (2008) Characterization of gene encoding amylopullulanase from plant-originated lactic acid bacterium, Lactobacillus plantarum L137. J Biosci Bioeng 106(5):449–459
    • (2008) J Biosci Bioeng , vol.106 , Issue.5 , pp. 449-459
    • Kim, J.1    Sunako, M.2    Ono, H.3    Murooka, Y.4    Fukusaki, E.5    Yamashita, M.6
  • 39
    • 60949105812 scopus 로고    scopus 로고
    • Characterization of the C-terminal truncated form of amylopullulanase from Lactobacillus plantarum L137
    • COI: 1:CAS:528:DC%2BD1MXkvFGltrc%3D, PID: 19217549
    • Kim J, Sunako M, Ono H, Murooka Y, Fukusaki E, Yamashita M (2009) Characterization of the C-terminal truncated form of amylopullulanase from Lactobacillus plantarum L137. J Biosci Bioeng 107(2):124–129
    • (2009) J Biosci Bioeng , vol.107 , Issue.2 , pp. 124-129
    • Kim, J.1    Sunako, M.2    Ono, H.3    Murooka, Y.4    Fukusaki, E.5    Yamashita, M.6
  • 40
    • 77956362798 scopus 로고    scopus 로고
    • ApuA, a multifunctional α-glucan-degrading enzyme of Streptococcus suis, mediates adhesion to porcine epithelium and mucus
    • COI: 1:CAS:528:DC%2BC3cXht12is7fK, PID: 20522493
    • Ferrando ML, Fuentes S, de Greeff A, Smith H, Wells JM (2010) ApuA, a multifunctional α-glucan-degrading enzyme of Streptococcus suis, mediates adhesion to porcine epithelium and mucus. Microbiology 156:2818–2828
    • (2010) Microbiology , vol.156 , pp. 2818-2828
    • Ferrando, M.L.1    Fuentes, S.2    de Greeff, A.3    Smith, H.4    Wells, J.M.5
  • 41
    • 0029661443 scopus 로고    scopus 로고
    • Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes α-1,4 and α-1,6 linkages in polysaccharides at different active sites
    • COI: 1:CAS:528:DyaK28XlvFSqt7g%3D, PID: 8798645
    • Hatada Y, Igarashi K, Ozaki K, Ara K, Hitomi J, Kobayashi T, Kawai S, Watabe T, Ito S (1996) Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes α-1,4 and α-1,6 linkages in polysaccharides at different active sites. J Biol Chem 271(39):24075–24083
    • (1996) J Biol Chem , vol.271 , Issue.39 , pp. 24075-24083
    • Hatada, Y.1    Igarashi, K.2    Ozaki, K.3    Ara, K.4    Hitomi, J.5    Kobayashi, T.6    Kawai, S.7    Watabe, T.8    Ito, S.9
  • 43
    • 84951285680 scopus 로고    scopus 로고
    • Identification of a novel alkaline amylopullulanase from a gut metagenome of Hermetia illucens
    • COI: 1:CAS:528:DC%2BC2MXhvVCht73J, PID: 26526170
    • Lee YS, Seo SH, Yoon SH, Kim SY, Hahn BS, Sim JS, Koo BS, Lee CM (2016) Identification of a novel alkaline amylopullulanase from a gut metagenome of Hermetia illucens. Int J Biol Macromol 82:514–522
    • (2016) Int J Biol Macromol , vol.82 , pp. 514-522
    • Lee, Y.S.1    Seo, S.H.2    Yoon, S.H.3    Kim, S.Y.4    Hahn, B.S.5    Sim, J.S.6    Koo, B.S.7    Lee, C.M.8
  • 45
    • 84878679186 scopus 로고    scopus 로고
    • Cloning, purification and biochemical characterisation of an organic solvent-, detergent-, and thermo-stable amylopullulanase from Thermococcus kodakarensis KOD1
    • COI: 1:CAS:528:DC%2BC3sXnsVyhsrk%3D
    • Guan Q, Guo X, Han T, Wei M, Jin M, Zeng F, Liu L, Li Z, Wang Y, Cheong G, Zhang S, Jia B (2013) Cloning, purification and biochemical characterisation of an organic solvent-, detergent-, and thermo-stable amylopullulanase from Thermococcus kodakarensis KOD1. Process Biochem 48(5–6):878–884
    • (2013) Process Biochem , vol.48 , Issue.5-6 , pp. 878-884
    • Guan, Q.1    Guo, X.2    Han, T.3    Wei, M.4    Jin, M.5    Zeng, F.6    Liu, L.7    Li, Z.8    Wang, Y.9    Cheong, G.10    Zhang, S.11    Jia, B.12
  • 46
    • 0027385006 scopus 로고
    • Cloning and sequencing of a gene encoding acidophilic amylase from Bacillus acidocaldarius
    • COI: 1:CAS:528:DyaK2cXntVGntQ%3D%3D, PID: 8254309
    • Koivula T, Hemila H, Pakkanen R, Sibakov M, Palva I (1993) Cloning and sequencing of a gene encoding acidophilic amylase from Bacillus acidocaldarius. J Gen Microbiol 139:2399–2407
    • (1993) J Gen Microbiol , vol.139 , pp. 2399-2407
    • Koivula, T.1    Hemila, H.2    Pakkanen, R.3    Sibakov, M.4    Palva, I.5
  • 47
    • 81855201858 scopus 로고    scopus 로고
    • Identification of an acidic α-amylase from Alicyclobacillus sp A4 and assessment of its application in the starch industry
    • COI: 1:CAS:528:DC%2BC3MXhsVyktrrF
    • Bai Y, Huang H, Meng K, Shi P, Yang P, Luo H, Luo C, Feng Y, Zhang W, Yao B (2012) Identification of an acidic α-amylase from Alicyclobacillus sp A4 and assessment of its application in the starch industry. Food Chem 131(4):1473–1478
    • (2012) Food Chem , vol.131 , Issue.4 , pp. 1473-1478
    • Bai, Y.1    Huang, H.2    Meng, K.3    Shi, P.4    Yang, P.5    Luo, H.6    Luo, C.7    Feng, Y.8    Zhang, W.9    Yao, B.10
  • 48
    • 0028146782 scopus 로고
    • Cloning of the aapT gene and characterization of its product, α-amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601
    • COI: 1:CAS:528:DyaK2MXhtFahu74%3D, PID: 7986049
    • Lee S, Morikawa M, Takagi M, Imanaka T (1994) Cloning of the aapT gene and characterization of its product, α-amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601. Appl Environ Microbiol 60(10):3764–3773
    • (1994) Appl Environ Microbiol , vol.60 , Issue.10 , pp. 3764-3773
    • Lee, S.1    Morikawa, M.2    Takagi, M.3    Imanaka, T.4
  • 49
    • 67049158420 scopus 로고    scopus 로고
    • The high-molecular-mass amylase (HMMA) of Geobacillus stearothermophilus ATCC 12980 interacts with the cell wall components by virtue of three specific binding regions
    • COI: 1:CAS:528:DC%2BD1MXotFagt74%3D, PID: 19460092
    • Ferner-Ortner-Bleckmann J, Huber-Gries C, Pavkov T, Keller W, Mader C, Ilk N, Sleytr UB, Egelseer EM (2009) The high-molecular-mass amylase (HMMA) of Geobacillus stearothermophilus ATCC 12980 interacts with the cell wall components by virtue of three specific binding regions. Mol Microbiol 72(6):1448–1461
    • (2009) Mol Microbiol , vol.72 , Issue.6 , pp. 1448-1461
    • Ferner-Ortner-Bleckmann, J.1    Huber-Gries, C.2    Pavkov, T.3    Keller, W.4    Mader, C.5    Ilk, N.6    Sleytr, U.B.7    Egelseer, E.M.8
  • 50
    • 0034979496 scopus 로고    scopus 로고
    • Structure and expression of an amylopullulanase gene from Bacillus stearothermophilus TS-23
    • COI: 1:CAS:528:DC%2BD3MXkslWkurc%3D, PID: 11389673
    • Chen J, Chen M, Chen L, Chu W (2001) Structure and expression of an amylopullulanase gene from Bacillus stearothermophilus TS-23. Biotechnol Appl Biochem 33:189–199
    • (2001) Biotechnol Appl Biochem , vol.33 , pp. 189-199
    • Chen, J.1    Chen, M.2    Chen, L.3    Chu, W.4
  • 51
    • 84879842967 scopus 로고    scopus 로고
    • Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification
    • COI: 1:CAS:528:DC%2BC3sXhtVCrt73J, PID: 23132347
    • Nisha M, Satyanarayana T (2013) Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification. Appl Microbiol Biotechnol 97(14):6279–6292
    • (2013) Appl Microbiol Biotechnol , vol.97 , Issue.14 , pp. 6279-6292
    • Nisha, M.1    Satyanarayana, T.2
  • 52
    • 84930766492 scopus 로고    scopus 로고
    • The role of N1 domain on the activity, stability, substrate specificity and raw starch binding of amylopullulanase of the extreme thermophile Geobacillus thermoleovorans
    • COI: 1:CAS:528:DC%2BC2MXmtVaktw%3D%3D, PID: 25573470
    • Nisha M, Satyanarayana T (2015) The role of N1 domain on the activity, stability, substrate specificity and raw starch binding of amylopullulanase of the extreme thermophile Geobacillus thermoleovorans. Appl Microbiol Biotechnol 99(13):5461–5474
    • (2015) Appl Microbiol Biotechnol , vol.99 , Issue.13 , pp. 5461-5474
    • Nisha, M.1    Satyanarayana, T.2
  • 53
    • 0025012804 scopus 로고
    • Substrate competition and specificity at the active site of amylopullulanase from Clostridium thermohydrosulfuricum
    • COI: 1:CAS:528:DyaK3cXhtFCksr0%3D, PID: 2302196
    • Mathupala S, Saha B, Zeikus J (1990) Substrate competition and specificity at the active site of amylopullulanase from Clostridium thermohydrosulfuricum. Biochem Biophys Res Commun 166(1):126–132
    • (1990) Biochem Biophys Res Commun , vol.166 , Issue.1 , pp. 126-132
    • Mathupala, S.1    Saha, B.2    Zeikus, J.3
  • 54
    • 0027257462 scopus 로고
    • Sequencing of the amylopullulanase (apu) gene of Thermoanaerobacter ethanolicus 39E, and identification of the active site by site-directed mutagenesis
    • COI: 1:CAS:528:DyaK3sXmt1Sguro%3D, PID: 8344920
    • Mathupala S, Lowe S, Podkovyrov S, Zeikus J (1993) Sequencing of the amylopullulanase (apu) gene of Thermoanaerobacter ethanolicus 39E, and identification of the active site by site-directed mutagenesis. J Biol Chem 268(22):16332–16344
    • (1993) J Biol Chem , vol.268 , Issue.22 , pp. 16332-16344
    • Mathupala, S.1    Lowe, S.2    Podkovyrov, S.3    Zeikus, J.4
  • 55
    • 0028038927 scopus 로고
    • Cloning and sequencing of the Thermoanaerobacterium saccharolyticum B6A-RI apu gene and purification and characterization of the amylopullulanase from Escherichia coli
    • COI: 1:CAS:528:DyaK2cXht1KmsL0%3D, PID: 8117096
    • Ramesh M, Podkovyrov S, Lowe S, Zeikus J (1994) Cloning and sequencing of the Thermoanaerobacterium saccharolyticum B6A-RI apu gene and purification and characterization of the amylopullulanase from Escherichia coli. Appl Environ Microbiol 60(1):94–101
    • (1994) Appl Environ Microbiol , vol.60 , Issue.1 , pp. 94-101
    • Ramesh, M.1    Podkovyrov, S.2    Lowe, S.3    Zeikus, J.4
  • 56
    • 0024287178 scopus 로고
    • Purification and some properties of the extracellular α-amylase-pullulanase produced by Clostridium thermohydrosulfuricum
    • COI: 1:CAS:528:DyaL1cXhs1ekurs%3D, PID: 3260488
    • Melasniemi H (1988) Purification and some properties of the extracellular α-amylase-pullulanase produced by Clostridium thermohydrosulfuricum. Biochem J 250(3):813–818
    • (1988) Biochem J , vol.250 , Issue.3 , pp. 813-818
    • Melasniemi, H.1
  • 57
    • 84989051900 scopus 로고
    • Analysis of the amylolytic enzyme-system of Clostridium thermosulfurogenes EM1: purification and synergistic action of pullulanases and maltohexaose forming α-amylase
    • COI: 1:CAS:528:DyaK38XlvVOjtr4%3D
    • Spreinat A, Antranikian G (1992) Analysis of the amylolytic enzyme-system of Clostridium thermosulfurogenes EM1: purification and synergistic action of pullulanases and maltohexaose forming α-amylase. Starch-Stärke 44(8):305–312
    • (1992) Starch-Stärke , vol.44 , Issue.8 , pp. 305-312
    • Spreinat, A.1    Antranikian, G.2
  • 58
    • 0028321448 scopus 로고
    • Pullulanase of Thermoanaerobacterium thermosulfurigenes EM1 (Clostridium thermosulfurogenes): molecular analysis of the gene, composite structure of the enzyme, and a common model for its attachment to the cell surface
    • COI: 1:CAS:528:DyaK2cXlt1Kmsr8%3D, PID: 8195085
    • Matuschek M, Burchhardt G, Sahm K, Bahl H (1994) Pullulanase of Thermoanaerobacterium thermosulfurigenes EM1 (Clostridium thermosulfurogenes): molecular analysis of the gene, composite structure of the enzyme, and a common model for its attachment to the cell surface. J Bacteriol 176(11):3295–3302
    • (1994) J Bacteriol , vol.176 , Issue.11 , pp. 3295-3302
    • Matuschek, M.1    Burchhardt, G.2    Sahm, K.3    Bahl, H.4
  • 59
    • 84878425381 scopus 로고    scopus 로고
    • A high molecular-mass Anoxybacillus sp SK3-4 amylopullulanase: characterization and its relationship in carbohydrate utilization
    • PID: 23759984
    • Kahar UM, Chan K, Salleh MM, Hii SM, Goh KM (2013) A high molecular-mass Anoxybacillus sp SK3-4 amylopullulanase: characterization and its relationship in carbohydrate utilization. Int J Mol Sci 14(6):11302–11318
    • (2013) Int J Mol Sci , vol.14 , Issue.6 , pp. 11302-11318
    • Kahar, U.M.1    Chan, K.2    Salleh, M.M.3    Hii, S.M.4    Goh, K.M.5
  • 60
    • 84917726222 scopus 로고    scopus 로고
    • Preparation of linear maltodextrins using a hyperthermophilic amylopullulanase with cyclodextrin- and starch-hydrolysing activities
    • COI: 1:CAS:528:DC%2BC2cXitValsLfF, PID: 25563953
    • Li X, Li D (2015) Preparation of linear maltodextrins using a hyperthermophilic amylopullulanase with cyclodextrin- and starch-hydrolysing activities. Carbohydr Polym 119:134–141
    • (2015) Carbohydr Polym , vol.119 , pp. 134-141
    • Li, X.1    Li, D.2
  • 61
    • 84907371588 scopus 로고    scopus 로고
    • Gene cloning and characterization of a type II pullulanase hydrolase from a hyperthermophilic archaeon, Pyrobaculum calidifontis
    • COI: 1:CAS:528:DC%2BC2cXitFSgurvK
    • Siddiqui MA, Rehman HU, Rashid N (2014) Gene cloning and characterization of a type II pullulanase hydrolase from a hyperthermophilic archaeon, Pyrobaculum calidifontis. Pak J Zool 46(4):1077–1084
    • (2014) Pak J Zool , vol.46 , Issue.4 , pp. 1077-1084
    • Siddiqui, M.A.1    Rehman, H.U.2    Rashid, N.3
  • 62
    • 0030803307 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme
    • COI: 1:CAS:528:DyaK2sXmtVKhtbw%3D, PID: 9293009
    • Dong G, Vieille C, Zeikus J (1997) Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme. Appl Environ Microbiol 63(9):3577–3584
    • (1997) Appl Environ Microbiol , vol.63 , Issue.9 , pp. 3577-3584
    • Dong, G.1    Vieille, C.2    Zeikus, J.3
  • 63
    • 84940436546 scopus 로고    scopus 로고
    • Membrane-bound amylopullulanase is essential for starch metabolism of Sulfolobus acidocaldarius DSM639
    • COI: 1:CAS:528:DC%2BC2MXhtFCjsr7F, PID: 26104674
    • Choi K, Cha J (2015) Membrane-bound amylopullulanase is essential for starch metabolism of Sulfolobus acidocaldarius DSM639. Extremophiles 19(5):909–920
    • (2015) Extremophiles , vol.19 , Issue.5 , pp. 909-920
    • Choi, K.1    Cha, J.2
  • 64
    • 84878680257 scopus 로고    scopus 로고
    • An extremely thermostable amylopullulanase from Staphylothermus marinus displays both pullulan- and cyclodextrin-degrading activities
    • COI: 1:CAS:528:DC%2BC3sXosVejurk%3D, PID: 23001056
    • Li X, Li D, Park K (2013) An extremely thermostable amylopullulanase from Staphylothermus marinus displays both pullulan- and cyclodextrin-degrading activities. Appl Microbiol Biotechnol 97(12):5359–5369
    • (2013) Appl Microbiol Biotechnol , vol.97 , Issue.12 , pp. 5359-5369
    • Li, X.1    Li, D.2    Park, K.3
  • 65
    • 0032908691 scopus 로고    scopus 로고
    • The type II pullulanase of Thermococcus hydrothermalis: molecular characterization of the gene and expression of the catalytic domain
    • COI: 1:CAS:528:DyaK1MXjt1yrtr8%3D, PID: 10322035
    • Erra-Pujada M, Debeire P, Duchiron F, O’Donohue M (1999) The type II pullulanase of Thermococcus hydrothermalis: molecular characterization of the gene and expression of the catalytic domain. J Bacteriol 181(10):3284–3287
    • (1999) J Bacteriol , vol.181 , Issue.10 , pp. 3284-3287
    • Erra-Pujada, M.1    Debeire, P.2    Duchiron, F.3    O’Donohue, M.4
  • 66
    • 0027179678 scopus 로고
    • Characterization of amylolytic enzymes, having both α-1,4 and α-1,6 hydrolytic activity, from the thermophilic archaea Pyrococcus furiosus and Thermococcus litoralis
    • COI: 1:CAS:528:DyaK3sXms1Gjurg%3D, PID: 16349019
    • Brown S, Kelly R (1993) Characterization of amylolytic enzymes, having both α-1,4 and α-1,6 hydrolytic activity, from the thermophilic archaea Pyrococcus furiosus and Thermococcus litoralis. Appl Environ Microbiol 59(8):2614–2621
    • (1993) Appl Environ Microbiol , vol.59 , Issue.8 , pp. 2614-2621
    • Brown, S.1    Kelly, R.2
  • 67
    • 79151480736 scopus 로고    scopus 로고
    • A GH57 family amylopullulanase from deep-sea Thermococcus siculi: expression of the gene and characterization of the recombinant enzyme
    • COI: 1:CAS:528:DC%2BC3cXhsF2gtrrO, PID: 20593184
    • Jiao Y, Wang S, Lv M, Xu J, Fang Y, Liu S (2011) A GH57 family amylopullulanase from deep-sea Thermococcus siculi: expression of the gene and characterization of the recombinant enzyme. Curr Microbiol 62(1):222–228
    • (2011) Curr Microbiol , vol.62 , Issue.1 , pp. 222-228
    • Jiao, Y.1    Wang, S.2    Lv, M.3    Xu, J.4    Fang, Y.5    Liu, S.6
  • 68
    • 0034705064 scopus 로고    scopus 로고
    • Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family
    • COI: 1:CAS:528:DC%2BD3cXjsVGhsbc%3D
    • Park KH, Kim TJ, Cheong TK, Kim JW, Oh BH, Svensson B (2000) Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family. Biochim Biophys Acta Protein Struct Mol Enzymol 1478(2):165–185
    • (2000) Biochim Biophys Acta Protein Struct Mol Enzymol , vol.1478 , Issue.2 , pp. 165-185
    • Park, K.H.1    Kim, T.J.2    Cheong, T.K.3    Kim, J.W.4    Oh, B.H.5    Svensson, B.6
  • 69
    • 0037077228 scopus 로고    scopus 로고
    • Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other
    • COI: 1:CAS:528:DC%2BD38Xksl2jsLY%3D, PID: 11923309
    • Lee HS, Kim MS, Cho HS, Kim JI, Kim TJ, Choi JH, Park C, Lee HS, Oh BH, Park KH (2002) Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other. J Biol Chem 277(24):21891–21897
    • (2002) J Biol Chem , vol.277 , Issue.24 , pp. 21891-21897
    • Lee, H.S.1    Kim, M.S.2    Cho, H.S.3    Kim, J.I.4    Kim, T.J.5    Choi, J.H.6    Park, C.7    Lee, H.S.8    Oh, B.H.9    Park, K.H.10
  • 70
    • 0032942009 scopus 로고    scopus 로고
    • Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain
    • COI: 1:CAS:528:DyaK1MXitlartLY%3D, PID: 10103262
    • Kim T, Kim M, Kim B, Kim J, Cheong T, Kim J, Park K (1999) Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain. Appl Environ Microbiol 65(4):1644–1651
    • (1999) Appl Environ Microbiol , vol.65 , Issue.4 , pp. 1644-1651
    • Kim, T.1    Kim, M.2    Kim, B.3    Kim, J.4    Cheong, T.5    Kim, J.6    Park, K.7
  • 72
    • 77449094593 scopus 로고    scopus 로고
    • Structural features of the Nostoc punctiforme debranching enzyme reveal the basis of its mechanism and substrate specificity
    • COI: 1:CAS:528:DC%2BD1MXhsFGjsr%2FE
    • Dumbrepatil AB, Choi J, Park JT, Kim M, Kim TJ, Woo E, Park KH (2010) Structural features of the Nostoc punctiforme debranching enzyme reveal the basis of its mechanism and substrate specificity. Proteins Struct Funct Bioinf 78(2):348–356
    • (2010) Proteins Struct Funct Bioinf , vol.78 , Issue.2 , pp. 348-356
    • Dumbrepatil, A.B.1    Choi, J.2    Park, J.T.3    Kim, M.4    Kim, T.J.5    Woo, E.6    Park, K.H.7
  • 73
    • 33646158199 scopus 로고    scopus 로고
    • Structure of a complex of Thermoactinomyces vulgaris R-47 α-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft
    • COI: 1:CAS:528:DC%2BD28XksFeqsbY%3D, PID: 16564038
    • Ohtaki A, Mizuno M, Yoshida H, Tonozuka T, Sakano Y, Kamitori S (2006) Structure of a complex of Thermoactinomyces vulgaris R-47 α-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft. Carbohydr Res 341(8):1041–1046
    • (2006) Carbohydr Res , vol.341 , Issue.8 , pp. 1041-1046
    • Ohtaki, A.1    Mizuno, M.2    Yoshida, H.3    Tonozuka, T.4    Sakano, Y.5    Kamitori, S.6
  • 74
    • 0034704981 scopus 로고    scopus 로고
    • Molecular characterization of a dimeric intracellular maltogenic amylase of Bacillus subtilis SUH4-2
    • COI: 1:CAS:528:DC%2BD3cXjsVGht7s%3D, PID: 10825545
    • Cho H, Kim Y, Kim T, Lee H, Kim D, Kim J, Lee Y, Lee S, Park K (2000) Molecular characterization of a dimeric intracellular maltogenic amylase of Bacillus subtilis SUH4-2. Biochim Biophys Acta 1478(2):333–340
    • (2000) Biochim Biophys Acta , vol.1478 , Issue.2 , pp. 333-340
    • Cho, H.1    Kim, Y.2    Kim, T.3    Lee, H.4    Kim, D.5    Kim, J.6    Lee, Y.7    Lee, S.8    Park, K.9
  • 75
    • 84884373635 scopus 로고    scopus 로고
    • Dimerization mediates thermo-adaptation, substrate affinity and transglycosylation in a highly thermostable maltogenic amylase of Geobacillus thermoleovorans
    • Mehta D, Satyanarayana T (2013) Dimerization mediates thermo-adaptation, substrate affinity and transglycosylation in a highly thermostable maltogenic amylase of Geobacillus thermoleovorans. PLoS One 8(9):1–13
    • (2013) PLoS One , vol.8 , Issue.9 , pp. 1-13
    • Mehta, D.1    Satyanarayana, T.2
  • 76
    • 84893023329 scopus 로고    scopus 로고
    • Novel maltotriose-hydrolyzing thermoacidophilic type III pullulan hydrolase from Thermococcus kodakarensis
    • PID: 24296501
    • Ahmad N, Rashid N, Haider MS, Akram M, Akhtar M (2014) Novel maltotriose-hydrolyzing thermoacidophilic type III pullulan hydrolase from Thermococcus kodakarensis. Appl Environ Microbiol 80(3):1108–1115
    • (2014) Appl Environ Microbiol , vol.80 , Issue.3 , pp. 1108-1115
    • Ahmad, N.1    Rashid, N.2    Haider, M.S.3    Akram, M.4    Akhtar, M.5
  • 77
    • 84866321639 scopus 로고    scopus 로고
    • Enzymology and structure of the GH13_31 glucan 1,6-α-glucosidase that confers isomaltooligosaccharide utilization in the probiotic Lactobacillus acidophilus NCFM
    • PID: 22685275
    • Møller MS, Fredslund F, Majumder A, Nakai H, Poulsen JN, Lo Leggio L, Svensson B, Abou Hachem M (2012) Enzymology and structure of the GH13_31 glucan 1,6-α-glucosidase that confers isomaltooligosaccharide utilization in the probiotic Lactobacillus acidophilus NCFM. J Bacteriol 194(16):4249–4259
    • (2012) J Bacteriol , vol.194 , Issue.16 , pp. 4249-4259
    • Møller, M.S.1    Fredslund, F.2    Majumder, A.3    Nakai, H.4    Poulsen, J.N.5    Lo Leggio, L.6    Svensson, B.7    Abou Hachem, M.8
  • 79
    • 84865724994 scopus 로고    scopus 로고
    • Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21
    • Møller MS, Abou Hachem M, Svensson B, Henriksen A (2012) Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21. Acta Crystallogr F Struct Biol Cryst Commun 68(Pt 9):1008–1012
    • (2012) Acta Crystallogr F Struct Biol Cryst Commun , vol.68 , pp. 1008-1012
    • Møller, M.S.1    Abou Hachem, M.2    Svensson, B.3    Henriksen, A.4
  • 80
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: fine-tuning polysaccharide recognition
    • COI: 1:CAS:528:DC%2BD2cXntlOrsL8%3D, PID: 15214846
    • Boraston AB, Bolam DN, Gilbert HJ, Davies GJ (2004) Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J 382:769–781
    • (2004) Biochem J , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 81
    • 76649087970 scopus 로고    scopus 로고
    • Carbohydrate-binding domains: multiplicity of biological roles
    • PID: 19908036
    • Guillén D, Sánchez S, Rodríguez-Sanoja R (2010) Carbohydrate-binding domains: multiplicity of biological roles. Appl Microbiol Biotechnol 85(5):1241–1249
    • (2010) Appl Microbiol Biotechnol , vol.85 , Issue.5 , pp. 1241-1249
    • Guillén, D.1    Sánchez, S.2    Rodríguez-Sanoja, R.3
  • 85
    • 80054683038 scopus 로고    scopus 로고
    • Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals
    • PID: 22112614
    • Janeček S, Svensson B, MacGregor EA (2011) Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals. Enzyme Microb Technol 49(5):429–440
    • (2011) Enzyme Microb Technol , vol.49 , Issue.5 , pp. 429-440
    • Janeček, S.1    Svensson, B.2    MacGregor, E.A.3
  • 86
    • 69449083006 scopus 로고    scopus 로고
    • The carbohydrate-binding module family 20-diversity, structure, and function
    • COI: 1:CAS:528:DC%2BD1MXhtFChtrjN, PID: 19682075
    • Christiansen C, Abou Hachem M, Janecek S, Vikso-Nielsen A, Blennow A, Svensson B (2009) The carbohydrate-binding module family 20-diversity, structure, and function. FEBS J 276(18):5006–5029
    • (2009) FEBS J , vol.276 , Issue.18 , pp. 5006-5029
    • Christiansen, C.1    Abou Hachem, M.2    Janecek, S.3    Vikso-Nielsen, A.4    Blennow, A.5    Svensson, B.6
  • 88
    • 12644258001 scopus 로고    scopus 로고
    • The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251
    • COI: 1:CAS:528:DyaK2sXntVWj, PID: 8955113
    • Penninga D, vander Veen B, Knegtel R, van Hijum S, Rozeboom H, Kalk K, Dijkstra B, Dijkhuizen L (1996) The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251. J Biol Chem 271(51):32777–32784
    • (1996) J Biol Chem , vol.271 , Issue.51 , pp. 32777-32784
    • Penninga, D.1    vander Veen, B.2    Knegtel, R.3    van Hijum, S.4    Rozeboom, H.5    Kalk, K.6    Dijkstra, B.7    Dijkhuizen, L.8
  • 89
    • 0031570348 scopus 로고    scopus 로고
    • Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to β-cyclodextrin
    • COI: 1:CAS:528:DyaK2sXjvFamt7Y%3D, PID: 9195884
    • Sorimachi K, Le Gal-Coëffet M, Williamson G, Archer D, Williamson M (1997) Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to β-cyclodextrin. Structure 5(5):647–661
    • (1997) Structure , vol.5 , Issue.5 , pp. 647-661
    • Sorimachi, K.1    Le Gal-Coëffet, M.2    Williamson, G.3    Archer, D.4    Williamson, M.5
  • 90
    • 84906833059 scopus 로고    scopus 로고
    • The carbohydrate-binding domain of overexpressed STBD1 is important for its stability and protein-protein interactions
    • COI: 1:CAS:528:DC%2BC2cXhsVeksbjP
    • Zhu Y, Zhang M, Kelly AR, Cheng A (2014) The carbohydrate-binding domain of overexpressed STBD1 is important for its stability and protein-protein interactions. Biosci Rep 34:311–320
    • (2014) Biosci Rep , vol.34 , pp. 311-320
    • Zhu, Y.1    Zhang, M.2    Kelly, A.R.3    Cheng, A.4
  • 91
    • 84871714045 scopus 로고
    • Woo E and Park K (2013) A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus
    • Park J, Song H, Jung T, Lee M, Park S (1834) Woo E and Park K (2013) A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus. Biochim Biophys Acta Proteins Proteomics 1:380–386
    • (1834) Biochim Biophys Acta Proteins Proteomics , vol.1 , pp. 380-386
    • Park, J.1    Song, H.2    Jung, T.3    Lee, M.4    Park, S.5
  • 92
    • 84976333044 scopus 로고    scopus 로고
    • Solution structure of family 21 carbohydrate-binding module from Rhizopus oryzae glucoamylase
    • Liu Y, Lai Y, Chou W, Chang MD, Lyu P (2007) Solution structure of family 21 carbohydrate-binding module from Rhizopus oryzae glucoamylase. Biochem J 40:321–330
    • (2007) Biochem J , vol.40 , pp. 321-330
    • Liu, Y.1    Lai, Y.2    Chou, W.3    Chang, M.D.4    Lyu, P.5
  • 93
    • 28244442802 scopus 로고    scopus 로고
    • Complexes of Thermoactinomyces vulgaris R-47 α-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages
    • COI: 1:CAS:528:DC%2BD2MXhtlSqsbfI, PID: 16302977
    • Abe A, Yoshida H, Tonozuka T, Sakano Y, Kamitori S (2005) Complexes of Thermoactinomyces vulgaris R-47 α-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages. FEBS J 272(23):6145–6153
    • (2005) FEBS J , vol.272 , Issue.23 , pp. 6145-6153
    • Abe, A.1    Yoshida, H.2    Tonozuka, T.3    Sakano, Y.4    Kamitori, S.5
  • 94
    • 33846096051 scopus 로고    scopus 로고
    • Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors
    • PID: 17187076
    • van Bueren AL, Higgins M, Wang D, Burke RD, Boraston AB (2007) Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors. Nat Struct Mol Biol 14(1):76–84
    • (2007) Nat Struct Mol Biol , vol.14 , Issue.1 , pp. 76-84
    • van Bueren, A.L.1    Higgins, M.2    Wang, D.3    Burke, R.D.4    Boraston, A.B.5
  • 95
    • 84867745280 scopus 로고    scopus 로고
    • Insights into the recognition of the human glycome by microbial carbohydrate-binding modules
    • COI: 1:CAS:528:DC%2BC38XhtFeitL3J, PID: 22858095
    • Ficko-Blean E, Boraston AB (2012) Insights into the recognition of the human glycome by microbial carbohydrate-binding modules. Curr Opin Struct Biol 22(5):570–577
    • (2012) Curr Opin Struct Biol , vol.22 , Issue.5 , pp. 570-577
    • Ficko-Blean, E.1    Boraston, A.B.2
  • 96
    • 66149096253 scopus 로고    scopus 로고
    • Group B Streptococcus pullulanase crystal structures in the context of a novel strategy for vaccine development
    • COI: 1:CAS:528:DC%2BD1MXms1eisbo%3D, PID: 19329633
    • Gourlay LJ, Santi I, Pezzicoli A, Grandi G, Soriani M, Bolognesi M (2009) Group B Streptococcus pullulanase crystal structures in the context of a novel strategy for vaccine development. J Bacteriol 191(11):3544–3552
    • (2009) J Bacteriol , vol.191 , Issue.11 , pp. 3544-3552
    • Gourlay, L.J.1    Santi, I.2    Pezzicoli, A.3    Grandi, G.4    Soriani, M.5    Bolognesi, M.6
  • 97
    • 33845683489 scopus 로고    scopus 로고
    • The structural basis of α-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima
    • Lammerts van Bueren A, Boraston AB (2007) The structural basis of α-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima. J Mol Biol 365(3):555–560
    • (2007) J Mol Biol , vol.365 , Issue.3 , pp. 555-560
    • Lammerts van Bueren, A.1    Boraston, A.B.2
  • 98
    • 10644283902 scopus 로고    scopus 로고
    • α-Glucan recognition by a new family of carbohydrate-binding modules found primarily in bacterial pathogens
    • van Bueren A, Finn R, Ausio J, Boraston A (2004) α-Glucan recognition by a new family of carbohydrate-binding modules found primarily in bacterial pathogens. Biochemistry 43(49):15633–15642
    • (2004) Biochemistry , vol.43 , Issue.49 , pp. 15633-15642
    • van Bueren, A.1    Finn, R.2    Ausio, J.3    Boraston, A.4
  • 99
    • 57349180133 scopus 로고    scopus 로고
    • Domain evolution in the GH13 pullulanase subfamily with focus on the carbohydrate-binding module family 48
    • COI: 1:CAS:528:DC%2BD1MXjvVWiurg%3D
    • Machovic M, Janeček S (2008) Domain evolution in the GH13 pullulanase subfamily with focus on the carbohydrate-binding module family 48. Biologia 63(6):1057–1068
    • (2008) Biologia , vol.63 , Issue.6 , pp. 1057-1068
    • Machovic, M.1    Janeček, S.2
  • 100
    • 26444608572 scopus 로고    scopus 로고
    • Structural basis for glycogen recognition by AMP-activated protein kinase
    • COI: 1:CAS:528:DC%2BD2MXhtFWhtrzJ, PID: 16216577
    • Polekhina G, Gupta A, van Denderen B, Fell S, Kemp B, Stapleton D, Parker M (2005) Structural basis for glycogen recognition by AMP-activated protein kinase. Structure 13(10):1453–1462
    • (2005) Structure , vol.13 , Issue.10 , pp. 1453-1462
    • Polekhina, G.1    Gupta, A.2    van Denderen, B.3    Fell, S.4    Kemp, B.5    Stapleton, D.6    Parker, M.7
  • 102
    • 77955478357 scopus 로고    scopus 로고
    • Biochemical and functional studies on the regulation of the Saccharomyces cerevisiae AMPK homolog SNF1
    • COI: 1:CAS:528:DC%2BC3cXotVChu74%3D, PID: 20529674
    • Amodeo GA, Momcilovic M, Carlson M, Tong L (2010) Biochemical and functional studies on the regulation of the Saccharomyces cerevisiae AMPK homolog SNF1. Biochem Biophys Res Commun 397(2):197–201
    • (2010) Biochem Biophys Res Commun , vol.397 , Issue.2 , pp. 197-201
    • Amodeo, G.A.1    Momcilovic, M.2    Carlson, M.3    Tong, L.4
  • 103
  • 104
    • 84924081191 scopus 로고    scopus 로고
    • PROTEIN TARGETING TO STARCH is required for localising GRANULE-BOUND STARCH SYNTHASE to starch granules and for normal amylose synthesis in Arabidopsis
    • Seung D, Soyk S, Coiro M, Maier BA, Eicke S, Zeeman SC (2015) PROTEIN TARGETING TO STARCH is required for localising GRANULE-BOUND STARCH SYNTHASE to starch granules and for normal amylose synthesis in Arabidopsis. PLoS Biol 13(2):1–29
    • (2015) PLoS Biol , vol.13 , Issue.2 , pp. 1-29
    • Seung, D.1    Soyk, S.2    Coiro, M.3    Maier, B.A.4    Eicke, S.5    Zeeman, S.C.6
  • 105
    • 84864758794 scopus 로고    scopus 로고
    • Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose
    • COI: 1:CAS:528:DC%2BC38XhtVOqu7vL, PID: 22771800
    • Chaen K, Noguchi J, Omori T, Kakuta Y, Kimura M (2012) Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose. Biochem Biophys Res Commun 424(3):508–511
    • (2012) Biochem Biophys Res Commun , vol.424 , Issue.3 , pp. 508-511
    • Chaen, K.1    Noguchi, J.2    Omori, T.3    Kakuta, Y.4    Kimura, M.5
  • 106
    • 84944096734 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli branching enzyme in complex with linear oligosaccharides
    • COI: 1:CAS:528:DC%2BC2MXhtlCltb%2FN, PID: 26280198
    • Feng L, Fawaz R, Hovde S, Gilbert L, Chiou J, Geiger JH (2015) Crystal structures of Escherichia coli branching enzyme in complex with linear oligosaccharides. Biochemistry 54(40):6207–6218
    • (2015) Biochemistry , vol.54 , Issue.40 , pp. 6207-6218
    • Feng, L.1    Fawaz, R.2    Hovde, S.3    Gilbert, L.4    Chiou, J.5    Geiger, J.H.6
  • 107
    • 33646770359 scopus 로고    scopus 로고
    • Crystal structure of pullulanase: evidence for parallel binding of oligosaccharides in the active site
    • COI: 1:CAS:528:DC%2BD28XltFGjur4%3D, PID: 16650854
    • Mikami B, Iwamoto H, Malle D, Yoon HJ, Demirkan-Sarikaya E, Mezaki Y, Katsuya Y (2006) Crystal structure of pullulanase: evidence for parallel binding of oligosaccharides in the active site. J Mol Biol 359(3):690–707
    • (2006) J Mol Biol , vol.359 , Issue.3 , pp. 690-707
    • Mikami, B.1    Iwamoto, H.2    Malle, D.3    Yoon, H.J.4    Demirkan-Sarikaya, E.5    Mezaki, Y.6    Katsuya, Y.7
  • 108
    • 0031471066 scopus 로고    scopus 로고
    • Amino acid residues specific for the catalytic action towards α-1,6-glucosidic linkages in Klebsiella pullulanase
    • COI: 1:CAS:528:DyaK2sXntlyjt78%3D
    • Yamashita M, Matsumoto D, Murooka Y (1997) Amino acid residues specific for the catalytic action towards α-1,6-glucosidic linkages in Klebsiella pullulanase. J Ferment Bioeng 84(4):283–290
    • (1997) J Ferment Bioeng , vol.84 , Issue.4 , pp. 283-290
    • Yamashita, M.1    Matsumoto, D.2    Murooka, Y.3
  • 109
    • 84924362759 scopus 로고    scopus 로고
    • Structural elements responsible for the glucosidic linkage-selectivity of a glycoside hydrolase family 13 exo-glucosidase
    • COI: 1:CAS:528:DC%2BC2MXjslChu7k%3D, PID: 25728274
    • Saburi W, Rachi-Otsuka H, Hondoh H, Okuyama M, Mori H, Kimura A (2015) Structural elements responsible for the glucosidic linkage-selectivity of a glycoside hydrolase family 13 exo-glucosidase. FEBS Lett 589(7):865–869
    • (2015) FEBS Lett , vol.589 , Issue.7 , pp. 865-869
    • Saburi, W.1    Rachi-Otsuka, H.2    Hondoh, H.3    Okuyama, M.4    Mori, H.5    Kimura, A.6
  • 110
    • 33947646402 scopus 로고    scopus 로고
    • Val326 of Thermoactinomyces vulgaris R-47 amylase II modulates the preference for α-(1,4)- and α-(1,6)-glycosidic linkages
    • COI: 1:CAS:528:DC%2BD2sXjslemtbk%3D, PID: 17400040
    • Ito K, Ito S, Ishino K, Shimizu-Ibuka A, Sakai H (2007) Val326 of Thermoactinomyces vulgaris R-47 amylase II modulates the preference for α-(1,4)- and α-(1,6)-glycosidic linkages. Biochim Biophys Acta 1774(4):443–449
    • (2007) Biochim Biophys Acta , vol.1774 , Issue.4 , pp. 443-449
    • Ito, K.1    Ito, S.2    Ishino, K.3    Shimizu-Ibuka, A.4    Sakai, H.5
  • 111
    • 0030016344 scopus 로고    scopus 로고
    • Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center
    • COI: 1:CAS:528:DyaK28XksFamtLw%3D, PID: 8663322
    • Kuriki T, Kaneko H, Yanase M, Takata H, Shimada J, Handa S, Takada T, Umeyama H, Okada S (1996) Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center. J Biol Chem 271(29):17321–17329
    • (1996) J Biol Chem , vol.271 , Issue.29 , pp. 17321-17329
    • Kuriki, T.1    Kaneko, H.2    Yanase, M.3    Takata, H.4    Shimada, J.5    Handa, S.6    Takada, T.7    Umeyama, H.8    Okada, S.9
  • 112
    • 33745119485 scopus 로고    scopus 로고
    • Structural elements in dextran glucosidase responsible for high specificity to long chain substrate
    • COI: 1:CAS:528:DC%2BD28XjvFSjs7o%3D, PID: 16503208
    • Saburi W, Mori H, Saito S, Okuyama M, Kimura A (2006) Structural elements in dextran glucosidase responsible for high specificity to long chain substrate. Biochim Biophys Acta 1764(4):688–698
    • (2006) Biochim Biophys Acta , vol.1764 , Issue.4 , pp. 688-698
    • Saburi, W.1    Mori, H.2    Saito, S.3    Okuyama, M.4    Kimura, A.5
  • 113
    • 0036866921 scopus 로고    scopus 로고
    • Oligo-1,6-glucosidase and neopullulanase enzyme subfamilies from the α-amylase family defined by the fifth conserved sequence region
    • PID: 12530525
    • Oslancová A, Janecek S (2002) Oligo-1,6-glucosidase and neopullulanase enzyme subfamilies from the α-amylase family defined by the fifth conserved sequence region. Cell Mol Life Sci 59(11):1945–1959
    • (2002) Cell Mol Life Sci , vol.59 , Issue.11 , pp. 1945-1959
    • Oslancová, A.1    Janecek, S.2
  • 114
    • 0032866910 scopus 로고    scopus 로고
    • Purification and molecular genetic characterization of ZPU1, a pullulanase-type starch-debranching enzyme from maize
    • COI: 1:CAS:528:DyaK1MXmt1Grsg%3D%3D, PID: 9880368
    • Beatty MK, Rahman A, Cao HP, Woodman W, Lee M, Myers AM, James MG (1999) Purification and molecular genetic characterization of ZPU1, a pullulanase-type starch-debranching enzyme from maize. Plant Physiol 119(1):255–266
    • (1999) Plant Physiol , vol.119 , Issue.1 , pp. 255-266
    • Beatty, M.K.1    Rahman, A.2    Cao, H.P.3    Woodman, W.4    Lee, M.5    Myers, A.M.6    James, M.G.7
  • 115
    • 45849123454 scopus 로고    scopus 로고
    • Isolation and characterization of a novel thermostable neopullulanase-like enzyme from a hot spring in Thailand
    • COI: 1:CAS:528:DC%2BD1cXotlyksro%3D, PID: 18540099
    • Tang K, Kobayashi RS, Champreda V, Eurwilaichitr L, Tanapongpipat S (2008) Isolation and characterization of a novel thermostable neopullulanase-like enzyme from a hot spring in Thailand. Biosci Biotechnol Biochem 72(6):1448–1456
    • (2008) Biosci Biotechnol Biochem , vol.72 , Issue.6 , pp. 1448-1456
    • Tang, K.1    Kobayashi, R.S.2    Champreda, V.3    Eurwilaichitr, L.4    Tanapongpipat, S.5
  • 116
    • 84976307991 scopus 로고    scopus 로고
    • Cloning, expression and characterization of the recombinant cold-active type-I pullulanase from Shewanella arctica
    • Elleuche S, Qoura FM, Lorenz U, Rehn T, Brueck T, Antranikian G (2015) Cloning, expression and characterization of the recombinant cold-active type-I pullulanase from Shewanella arctica. J Mol Catal B Enzym 11:670–677
    • (2015) J Mol Catal B Enzym , vol.11 , pp. 670-677
    • Elleuche, S.1    Qoura, F.M.2    Lorenz, U.3    Rehn, T.4    Brueck, T.5    Antranikian, G.6
  • 117
    • 79551472575 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of a heat-stable type I pullulanase from Thermotoga neapolitana
    • COI: 1:CAS:528:DC%2BC3MXhs1agurs%3D, PID: 22112909
    • Kang J, Park K, Choi K, Park C, Kim G, Kim D, Cha J (2011) Molecular cloning and biochemical characterization of a heat-stable type I pullulanase from Thermotoga neapolitana. Enzyme Microb Technol 48(3):260–266
    • (2011) Enzyme Microb Technol , vol.48 , Issue.3 , pp. 260-266
    • Kang, J.1    Park, K.2    Choi, K.3    Park, C.4    Kim, G.5    Kim, D.6    Cha, J.7
  • 118
    • 0027957981 scopus 로고
    • Molecular genetic analysis of the pullulanase B gene of Bacillus acidopullulyticus
    • COI: 1:CAS:528:DyaK2cXhvVCgu70%3D
    • Kelly A, Diderichsen B, Jorgensen S, Mcconnell D (1994) Molecular genetic analysis of the pullulanase B gene of Bacillus acidopullulyticus. FEMS Microbial Lett 115(1):97–105
    • (1994) FEMS Microbial Lett , vol.115 , Issue.1 , pp. 97-105
    • Kelly, A.1    Diderichsen, B.2    Jorgensen, S.3    Mcconnell, D.4
  • 119
    • 0030715627 scopus 로고    scopus 로고
    • Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus
    • COI: 1:CAS:528:DyaK2sXmtVWhurk%3D, PID: 9375788
    • Albertson G, McHale R, Gibbs M, Bergquist P (1997) Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus. Biochim Biophys Acta 1354(1):35–39
    • (1997) Biochim Biophys Acta , vol.1354 , Issue.1 , pp. 35-39
    • Albertson, G.1    McHale, R.2    Gibbs, M.3    Bergquist, P.4
  • 120
    • 77952466937 scopus 로고    scopus 로고
    • Starch: its metabolism, evolution, and biotechnological modification in plants
    • COI: 1:CAS:528:DC%2BC3cXnslSjsL4%3D, PID: 20192737
    • Zeeman SC, Kossmann J, Smith AM (2010) Starch: its metabolism, evolution, and biotechnological modification in plants. Annu Rev Plant Biol 61:209–234
    • (2010) Annu Rev Plant Biol , vol.61 , pp. 209-234
    • Zeeman, S.C.1    Kossmann, J.2    Smith, A.M.3
  • 121
    • 0037341209 scopus 로고    scopus 로고
    • Mutational analysis of the pullulanase-type debranching enzyme of maize indicates multiple functions in starch metabolism
    • COI: 1:CAS:528:DC%2BD3sXisVektLg%3D, PID: 12615940
    • Dinges J, Colleoni C, James M, Myers A (2003) Mutational analysis of the pullulanase-type debranching enzyme of maize indicates multiple functions in starch metabolism. Plant Cell 15(3):666–680
    • (2003) Plant Cell , vol.15 , Issue.3 , pp. 666-680
    • Dinges, J.1    Colleoni, C.2    James, M.3    Myers, A.4
  • 124
    • 57749084358 scopus 로고    scopus 로고
    • Further evidence for the mandatory nature of polysaccharide debranching for the aggregation of semicrystalline starch and for overlapping functions of debranching enzymes in Arabidopsis leaves
    • COI: 1:CAS:528:DC%2BD1cXhsVSnurvE, PID: 18815382
    • Wattebled F, Planchot V, Dong Y, Szydlowski N, Pontoire B, Devin A, Ball S, D’Hulst C (2008) Further evidence for the mandatory nature of polysaccharide debranching for the aggregation of semicrystalline starch and for overlapping functions of debranching enzymes in Arabidopsis leaves. Plant Physiol 148(3):1309–1323
    • (2008) Plant Physiol , vol.148 , Issue.3 , pp. 1309-1323
    • Wattebled, F.1    Planchot, V.2    Dong, Y.3    Szydlowski, N.4    Pontoire, B.5    Devin, A.6    Ball, S.7    D’Hulst, C.8
  • 125
    • 62549154915 scopus 로고    scopus 로고
    • Starch granule biosynthesis in arabidopsis is abolished by removal of all debranching enzymes but restored by the subsequent removal of an endoamylase
    • COI: 1:CAS:528:DC%2BD1MXitVaru7w%3D, PID: 19074683
    • Streb S, Delatte T, Umhang M, Eicke S, Schorderet M, Reinhardt D, Zeeman SC (2008) Starch granule biosynthesis in arabidopsis is abolished by removal of all debranching enzymes but restored by the subsequent removal of an endoamylase. Plant Cell 20(12):3448–3466
    • (2008) Plant Cell , vol.20 , Issue.12 , pp. 3448-3466
    • Streb, S.1    Delatte, T.2    Umhang, M.3    Eicke, S.4    Schorderet, M.5    Reinhardt, D.6    Zeeman, S.C.7
  • 126
    • 0029278930 scopus 로고
    • Characterization of the maize gene sugary1, a determinant of starch composition in kernels
    • COI: 1:CAS:528:DyaK2MXlt1yhsrg%3D, PID: 7773016
    • James M, Robertson D, Myers A (1995) Characterization of the maize gene sugary1, a determinant of starch composition in kernels. Plant Cell 7(4):417–429
    • (1995) Plant Cell , vol.7 , Issue.4 , pp. 417-429
    • James, M.1    Robertson, D.2    Myers, A.3
  • 127
    • 0000095135 scopus 로고
    • Carbohydrate-metabolism in the developing endosperm of rice grains
    • COI: 1:CAS:528:DyaK3cXhtFGrsb8%3D
    • Nakamura Y, Yuki K, Park S, Ohya T (1989) Carbohydrate-metabolism in the developing endosperm of rice grains. Plant Cell Physiol 30(6):833–839
    • (1989) Plant Cell Physiol , vol.30 , Issue.6 , pp. 833-839
    • Nakamura, Y.1    Yuki, K.2    Park, S.3    Ohya, T.4
  • 128
    • 0038303343 scopus 로고    scopus 로고
    • Antisense inhibition of isoamylase alters the structure of amylopectin and the physicochemical properties of starch in rice endosperm
    • COI: 1:CAS:528:DC%2BD3sXkvFSjsLg%3D, PID: 12826626
    • Fujita N, Kubo A, Suh DS, Wong KS, Jane JL, Ozawa K, Takaiwa F, Inaba Y, Nakamura Y (2003) Antisense inhibition of isoamylase alters the structure of amylopectin and the physicochemical properties of starch in rice endosperm. Plant Cell Physiol 44(6):607–618
    • (2003) Plant Cell Physiol , vol.44 , Issue.6 , pp. 607-618
    • Fujita, N.1    Kubo, A.2    Suh, D.S.3    Wong, K.S.4    Jane, J.L.5    Ozawa, K.6    Takaiwa, F.7    Inaba, Y.8    Nakamura, Y.9
  • 130
    • 63649158522 scopus 로고    scopus 로고
    • Characterization of expression of the OsPUL gene encoding a pullulanase-type debranching enzyme during seed development and germination in rice
    • COI: 1:CAS:528:DC%2BD1MXktF2ltb8%3D, PID: 19251430
    • Li Q, Zhang G, Dong Z, Yu H, Gu M, Sun SSM, Liu Q (2009) Characterization of expression of the OsPUL gene encoding a pullulanase-type debranching enzyme during seed development and germination in rice. Plant Physiol Biochem 47(5):351–358
    • (2009) Plant Physiol Biochem , vol.47 , Issue.5 , pp. 351-358
    • Li, Q.1    Zhang, G.2    Dong, Z.3    Yu, H.4    Gu, M.5    Sun, S.S.M.6    Liu, Q.7
  • 132
    • 77958165867 scopus 로고    scopus 로고
    • Starch biosynthesis in cereal endosperm
    • COI: 1:CAS:528:DC%2BC3cXlvVeju7Y%3D, PID: 20400324
    • Jeon J, Ryoo N, Hahn T, Walia H, Nakamura Y (2010) Starch biosynthesis in cereal endosperm. Plant Physiol Biochem 48(6):383–392
    • (2010) Plant Physiol Biochem , vol.48 , Issue.6 , pp. 383-392
    • Jeon, J.1    Ryoo, N.2    Hahn, T.3    Walia, H.4    Nakamura, Y.5
  • 133
    • 0036348660 scopus 로고    scopus 로고
    • Towards a better understanding of the metabolic system for amylopectin biosynthesis in plants: rice endosperm as a model tissue
    • COI: 1:CAS:528:DC%2BD38XlsFOisb8%3D, PID: 12154134
    • Nakamura Y (2002) Towards a better understanding of the metabolic system for amylopectin biosynthesis in plants: rice endosperm as a model tissue. Plant Cell Physiol 43(7):718–725
    • (2002) Plant Cell Physiol , vol.43 , Issue.7 , pp. 718-725
    • Nakamura, Y.1
  • 134
    • 0002056409 scopus 로고    scopus 로고
    • Some properties of starch debranching enzymes and their possible role in amylopectin biosynthesis
    • COI: 1:CAS:528:DyaK28Xnt1Whsbs%3D
    • Nakamura Y (1996) Some properties of starch debranching enzymes and their possible role in amylopectin biosynthesis. Plant Sci 121(1):1–18
    • (1996) Plant Sci , vol.121 , Issue.1 , pp. 1-18
    • Nakamura, Y.1
  • 135
    • 0033102225 scopus 로고    scopus 로고
    • A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley
    • COI: 1:CAS:528:DyaK1MXhvFymtb8%3D, PID: 10069825
    • Burton RA, Zhang XQ, Hrmova M, Fincher GB (1999) A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley. Plant Physiol 119(3):859–871
    • (1999) Plant Physiol , vol.119 , Issue.3 , pp. 859-871
    • Burton, R.A.1    Zhang, X.Q.2    Hrmova, M.3    Fincher, G.B.4
  • 136
    • 0035010116 scopus 로고    scopus 로고
    • Improved pattern for genome-based screening identifies novel cell wall-attached proteins in gram-positive bacteria
    • COI: 1:CAS:528:DC%2BD3MXjvFyqs78%3D, PID: 11349071
    • Janulczyk R, Rasmussen M (2001) Improved pattern for genome-based screening identifies novel cell wall-attached proteins in gram-positive bacteria. Infect Immun 69(6):4019–4026
    • (2001) Infect Immun , vol.69 , Issue.6 , pp. 4019-4026
    • Janulczyk, R.1    Rasmussen, M.2
  • 137
    • 77952243181 scopus 로고    scopus 로고
    • Construction of a direct starch-fermenting industrial strain of Saccharomyces cerevisiae producing glucoamylase, α-amylase and debranching enzyme
    • COI: 1:CAS:528:DC%2BC3cXksVeisLk%3D, PID: 20131079
    • Kim J, Kim H, Lim M, Ko H, Chin J, Lee HB, Kim I, Bai S (2010) Construction of a direct starch-fermenting industrial strain of Saccharomyces cerevisiae producing glucoamylase, α-amylase and debranching enzyme. Biotechnol Lett 32(5):713–719
    • (2010) Biotechnol Lett , vol.32 , Issue.5 , pp. 713-719
    • Kim, J.1    Kim, H.2    Lim, M.3    Ko, H.4    Chin, J.5    Lee, H.B.6    Kim, I.7    Bai, S.8
  • 138
    • 17344380706 scopus 로고    scopus 로고
    • Pullulan degrading enzymes of bacterial origin
    • COI: 1:CAS:528:DC%2BD2cXlt1ajsL8%3D, PID: 15239382
    • Doman-Pytka M, Bardowski J (2004) Pullulan degrading enzymes of bacterial origin. Crit Rev Microbiol 30(2):107–121
    • (2004) Crit Rev Microbiol , vol.30 , Issue.2 , pp. 107-121
    • Doman-Pytka, M.1    Bardowski, J.2
  • 139
    • 84868259379 scopus 로고    scopus 로고
    • Pullulanase: role in starch hydrolysis and potential industrial applications
    • Hii SL, Tan JS, Ling TC, Ariff AB (2012) Pullulanase: role in starch hydrolysis and potential industrial applications. Enzyme Res 2012:1–14
    • (2012) Enzyme Res , vol.2012 , pp. 1-14
    • Hii, S.L.1    Tan, J.S.2    Ling, T.C.3    Ariff, A.B.4
  • 140
    • 62849102004 scopus 로고    scopus 로고
    • Starch and α-glucan acting enzymes, modulating their properties by directed evolution
    • COI: 1:CAS:528:DC%2BD1MXjvVWjsbY%3D, PID: 19428713
    • Kelly RM, Dijkhuizen L, Leemhuis H (2009) Starch and α-glucan acting enzymes, modulating their properties by directed evolution. J Biotechnol 140(3–4):184–193
    • (2009) J Biotechnol , vol.140 , Issue.3-4 , pp. 184-193
    • Kelly, R.M.1    Dijkhuizen, L.2    Leemhuis, H.3
  • 141
    • 0037187437 scopus 로고    scopus 로고
    • Properties and applications of starch-converting enzymes of the α-amylase family
    • PID: 11796168
    • van der Maarel M, van der Veen B, Uitdehaag J, Leemhuis H, Dijkhuizen L (2002) Properties and applications of starch-converting enzymes of the α-amylase family. J Biotechnol 94(2):137–155
    • (2002) J Biotechnol , vol.94 , Issue.2 , pp. 137-155
    • van der Maarel, M.1    van der Veen, B.2    Uitdehaag, J.3    Leemhuis, H.4    Dijkhuizen, L.5
  • 142
    • 0037411739 scopus 로고    scopus 로고
    • Developments in industrially important thermostable enzymes: a review
    • COI: 1:CAS:528:DC%2BD3sXis1aqu7s%3D, PID: 12676497
    • Haki G, Rakshit S (2003) Developments in industrially important thermostable enzymes: a review. Bioresour Technol 89(1):17–34
    • (2003) Bioresour Technol , vol.89 , Issue.1 , pp. 17-34
    • Haki, G.1    Rakshit, S.2
  • 143
    • 79956099930 scopus 로고    scopus 로고
    • Will isomalto-oligosaccharides, a well-established functional food in Asia, break through the European and American market? The status of knowledge on these prebiotics
    • PID: 21491266
    • Goffin D, Delzenne N, Blecker C, Hanon E, Deroanne C, Paquot M (2011) Will isomalto-oligosaccharides, a well-established functional food in Asia, break through the European and American market? The status of knowledge on these prebiotics. Crit Rev Food Sci Nutr 51(5):394–409
    • (2011) Crit Rev Food Sci Nutr , vol.51 , Issue.5 , pp. 394-409
    • Goffin, D.1    Delzenne, N.2    Blecker, C.3    Hanon, E.4    Deroanne, C.5    Paquot, M.6
  • 144
    • 33847690260 scopus 로고    scopus 로고
    • Non-digestible oligosaccharides: a review
    • COI: 1:CAS:528:DC%2BD2sXislWgsL8%3D
    • Mussatto SI, Mancilha IM (2007) Non-digestible oligosaccharides: a review. Carbohydr Polym 68(3):587–597
    • (2007) Carbohydr Polym , vol.68 , Issue.3 , pp. 587-597
    • Mussatto, S.I.1    Mancilha, I.M.2
  • 145
    • 77958500768 scopus 로고    scopus 로고
    • Crystal structure of an essential enzyme in seed starch degradation: barley limit dextrinase in complex with cyclodextrins
    • COI: 1:CAS:528:DC%2BC3cXhtlKhs7jJ, PID: 20863834
    • Vester-Christensen MB, Abou Hachem M, Svensson B, Henriksen A (2010) Crystal structure of an essential enzyme in seed starch degradation: barley limit dextrinase in complex with cyclodextrins. J Mol Biol 403(5):739–750
    • (2010) J Mol Biol , vol.403 , Issue.5 , pp. 739-750
    • Vester-Christensen, M.B.1    Abou Hachem, M.2    Svensson, B.3    Henriksen, A.4
  • 146
    • 84929347435 scopus 로고    scopus 로고
    • Crystal structure of barley limit dextrinase-limit dextrinase inhibitor (LD-LDI) complex reveals insights into mechanism and diversity of cereal type inhibitors
    • PID: 25792743
    • Møller MS, Vester-Christensen MB, Jensen JM, Abou Hachem M, Henriksen A, Svensson B (2015) Crystal structure of barley limit dextrinase-limit dextrinase inhibitor (LD-LDI) complex reveals insights into mechanism and diversity of cereal type inhibitors. J Biol Chem 290(20):12614–12629
    • (2015) J Biol Chem , vol.290 , Issue.20 , pp. 12614-12629
    • Møller, M.S.1    Vester-Christensen, M.B.2    Jensen, J.M.3    Abou Hachem, M.4    Henriksen, A.5    Svensson, B.6
  • 148
    • 33645795717 scopus 로고    scopus 로고
    • Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168
    • COI: 1:CAS:528:DC%2BD28XjtVWjt78%3D, PID: 16582490
    • Malle D, Itoh T, Hashimoto W, Murata K, Utsumi S, Mikami B (2006) Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168. Acta Crystallogr Sect F Struct Biol Cryst Commun 62:381–384
    • (2006) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.62 , pp. 381-384
    • Malle, D.1    Itoh, T.2    Hashimoto, W.3    Murata, K.4    Utsumi, S.5    Mikami, B.6
  • 149
    • 0037423706 scopus 로고    scopus 로고
    • Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase
    • COI: 1:CAS:528:DC%2BD3sXlt12gtg%3D%3D, PID: 12547200
    • Hondoh H, Kuriki T, Matsuura Y (2003) Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase. J Mol Biol 326(1):177–188
    • (2003) J Mol Biol , vol.326 , Issue.1 , pp. 177-188
    • Hondoh, H.1    Kuriki, T.2    Matsuura, Y.3
  • 150
    • 0033574502 scopus 로고    scopus 로고
    • Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolution
    • COI: 1:CAS:528:DyaK1MXis1Kksbc%3D, PID: 10222200
    • Kamitori S, Kondo S, Okuyama K, Yokota T, Shimura Y, Tonozuka T, Sakano Y (1999) Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolution. J Mol Biol 287(5):907–921
    • (1999) J Mol Biol , vol.287 , Issue.5 , pp. 907-921
    • Kamitori, S.1    Kondo, S.2    Okuyama, K.3    Yokota, T.4    Shimura, Y.5    Tonozuka, T.6    Sakano, Y.7
  • 151
    • 0035045976 scopus 로고    scopus 로고
    • Studies on the hydrolyzing mechanism for cyclodextrins of Thermoactinomyces vulgaris R-47 α-amylase 2 (TVAII). X-ray structure of the mutant E354A complexed with β-cyclodextrin, and kinetic analyses on cyclodextrins
    • COI: 1:CAS:528:DC%2BD3MXjtlSju7Y%3D, PID: 11226882
    • Kondo S, Ohtaki A, Tonozuka T, Sakano Y, Kamitori S (2001) Studies on the hydrolyzing mechanism for cyclodextrins of Thermoactinomyces vulgaris R-47 α-amylase 2 (TVAII). X-ray structure of the mutant E354A complexed with β-cyclodextrin, and kinetic analyses on cyclodextrins. J Biochem 129(3):423–428
    • (2001) J Biochem , vol.129 , Issue.3 , pp. 423-428
    • Kondo, S.1    Ohtaki, A.2    Tonozuka, T.3    Sakano, Y.4    Kamitori, S.5
  • 152
    • 0035823414 scopus 로고    scopus 로고
    • Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 α-amylase 2 (TVAII). X-ray structures of the mutant TVA11 s, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs
    • COI: 1:CAS:528:DC%2BD3MXmt12hsr0%3D, PID: 11527532
    • Ohtaki A, Kondo S, Shimura Y, Tonozuka T, Sakano Y, Kamitori S (2001) Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 α-amylase 2 (TVAII). X-ray structures of the mutant TVA11 s, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs. Carbohydr Res 334(4):309–313
    • (2001) Carbohydr Res , vol.334 , Issue.4 , pp. 309-313
    • Ohtaki, A.1    Kondo, S.2    Shimura, Y.3    Tonozuka, T.4    Sakano, Y.5    Kamitori, S.6
  • 153
    • 0036304348 scopus 로고    scopus 로고
    • Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 α-amylase 1 (TVAI) at 1.6 Å resolution and α-amylase 2 (TVAII) at 2.3 Å resolution
    • COI: 1:CAS:528:DC%2BD38XktlCksLo%3D, PID: 12051850
    • Kamitori S, Abe A, Ohtaki A, Kaji A, Tonozuka T, Sakano Y (2002) Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 α-amylase 1 (TVAI) at 1.6 Å resolution and α-amylase 2 (TVAII) at 2.3 Å resolution. J Mol Biol 318(2):443–453
    • (2002) J Mol Biol , vol.318 , Issue.2 , pp. 443-453
    • Kamitori, S.1    Abe, A.2    Ohtaki, A.3    Kaji, A.4    Tonozuka, T.5    Sakano, Y.6
  • 154
    • 0035291410 scopus 로고    scopus 로고
    • Structures of Thermoactinomyces vulgaris R-47 α-amylase II complexed with substrate analogues
    • COI: 1:CAS:528:DC%2BD3MXisFKqurs%3D, PID: 11330677
    • Yokota T, Tonozuka T, Shimura Y, Ichikawa K, Kamitori S, Sakano Y (2001) Structures of Thermoactinomyces vulgaris R-47 α-amylase II complexed with substrate analogues. Biosci Biotechnol Biochem 65(3):619–626
    • (2001) Biosci Biotechnol Biochem , vol.65 , Issue.3 , pp. 619-626
    • Yokota, T.1    Tonozuka, T.2    Shimura, Y.3    Ichikawa, K.4    Kamitori, S.5    Sakano, Y.6
  • 155
    • 3042588260 scopus 로고    scopus 로고
    • The crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVA II) complexed with transglycosylated product
    • COI: 1:CAS:528:DC%2BD2cXltlKksr8%3D, PID: 15182368
    • Mizuno M, Tonozuka T, Uechi A, Ohtaki A, Ichikawa K, Kamitori S, Nishikawa A, Sakano Y (2004) The crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVA II) complexed with transglycosylated product. Eur J Biochem 271(12):2530–2538
    • (2004) Eur J Biochem , vol.271 , Issue.12 , pp. 2530-2538
    • Mizuno, M.1    Tonozuka, T.2    Uechi, A.3    Ohtaki, A.4    Ichikawa, K.5    Kamitori, S.6    Nishikawa, A.7    Sakano, Y.8
  • 156
    • 3843112354 scopus 로고    scopus 로고
    • Complex structures of Thermoactinomyces vulgaris R-47 α-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism
    • COI: 1:CAS:528:DC%2BD2cXlslOktbs%3D, PID: 15138257
    • Ohtaki A, Mizuno M, Tonozuka T, Sakano Y, Kamitori S (2004) Complex structures of Thermoactinomyces vulgaris R-47 α-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism. J Biol Chem 279(30):31033–31040
    • (2004) J Biol Chem , vol.279 , Issue.30 , pp. 31033-31040
    • Ohtaki, A.1    Mizuno, M.2    Tonozuka, T.3    Sakano, Y.4    Kamitori, S.5
  • 157
    • 0031591389 scopus 로고    scopus 로고
    • The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: structural characterization of proline-substitution sites for protein thermostabilization
    • COI: 1:CAS:528:DyaK2sXktVKmtr4%3D, PID: 9193006
    • Watanabe K, Hata Y, Kizaki H, Katsube Y, Suzuki Y (1997) The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: structural characterization of proline-substitution sites for protein thermostabilization. J Mol Biol 269(1):142–153
    • (1997) J Mol Biol , vol.269 , Issue.1 , pp. 142-153
    • Watanabe, K.1    Hata, Y.2    Kizaki, H.3    Katsube, Y.4    Suzuki, Y.5
  • 158
    • 41949139216 scopus 로고    scopus 로고
    • Substrate recognition mechanism of α-1,6-glucosidic linkage hydrolyzing enzyme, dextran glucosidase from Streptococcus mutans
    • PID: 18395742
    • Hondoh H, Saburi W, Mori H, Okuyama M, Nakada T, Matsuura Y, Kimura A (2008) Substrate recognition mechanism of α-1,6-glucosidic linkage hydrolyzing enzyme, dextran glucosidase from Streptococcus mutans. J Mol Biol 378(4):913–922
    • (2008) J Mol Biol , vol.378 , Issue.4 , pp. 913-922
    • Hondoh, H.1    Saburi, W.2    Mori, H.3    Okuyama, M.4    Nakada, T.5    Matsuura, Y.6    Kimura, A.7
  • 159
    • 84890330527 scopus 로고    scopus 로고
    • MEGA6: molecular Evolutionary Genetics Analysis version 6.0
    • COI: 1:CAS:528:DC%2BC3sXhvVKhurzP, PID: 24132122
    • Tamura K, Stecher G, Peterson D, Filipski A, Kumar S (2013) MEGA6: molecular Evolutionary Genetics Analysis version 6.0. Mol Biol Evol 30(12):2725–2729
    • (2013) Mol Biol Evol , vol.30 , Issue.12 , pp. 2725-2729
    • Tamura, K.1    Stecher, G.2    Peterson, D.3    Filipski, A.4    Kumar, S.5
  • 160
    • 77649142047 scopus 로고    scopus 로고
    • Multiple structure alignment and consensus identification for proteins
    • Ilinkin I, Ye J, Janardan R (2010) Multiple structure alignment and consensus identification for proteins. BMC Bioinf 11:1–8
    • (2010) BMC Bioinf , vol.11 , pp. 1-8
    • Ilinkin, I.1    Ye, J.2    Janardan, R.3
  • 161
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: a tool for multiple protein sequence and structure alignments
    • COI: 1:CAS:528:DC%2BD1cXkvFGgtrs%3D, PID: 18287115
    • Pei J, Kim B, Grishin NV (2008) PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res 36(7):2295–2300
    • (2008) Nucleic Acids Res , vol.36 , Issue.7 , pp. 2295-2300
    • Pei, J.1    Kim, B.2    Grishin, N.V.3
  • 162
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • COI: 1:CAS:528:DC%2BC2cXhtFCqs7vK, PID: 24753421
    • Robert X, Gouet P (2014) Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res 42(W1):W320–W324
    • (2014) Nucleic Acids Res , vol.42 , Issue.W1 , pp. W320-W324
    • Robert, X.1    Gouet, P.2


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