메뉴 건너뛰기




Volumn 8, Issue 10, 2013, Pages

Identification and Characterization of a Novel Trehalose Synthase Gene Derived from Saline-Alkali Soil Metagenomes

Author keywords

[No Author keywords available]

Indexed keywords

GENOMIC DNA; MALTOSE; MERCURY; SYNTHETASE; TREHALOSE; TREHALOSE SYNTHETASE; UNCLASSIFIED DRUG; ZINC ION; BACTERIAL PROTEIN; GLUCOSYLTRANSFERASE; ION; METAL; RECOMBINANT PROTEIN; SOIL; TREHALOSE SYNTHASE;

EID: 84885770536     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0077437     Document Type: Article
Times cited : (42)

References (46)
  • 1
    • 0036772879 scopus 로고    scopus 로고
    • Trehalose production: exploiting novel approaches
    • 10.1016/S0167-7799(02)02041-3
    • Schiraldi C, Di Lernia I, De Rosa M, (2002) Trehalose production: exploiting novel approaches. Trends Biotechnol 20: 420-425. doi:10.1016/S0167-7799(02)02041-3. PubMed: 12220904.
    • (2002) Trends Biotechnol , vol.20 , pp. 420-425
    • Schiraldi, C.1    Di Lernia, I.2    De Rosa, M.3
  • 2
    • 0038056150 scopus 로고    scopus 로고
    • New insights on trehalose: a multifunctional molecule
    • 10.1093/glycob/cwg047
    • Elbein AD, Pan YT, Pastuszak I, Carroll D, (2003) New insights on trehalose: a multifunctional molecule. Glycobiology 13: 17R-27R. doi:10.1093/glycob/cwg047. PubMed: 12626396.
    • (2003) Glycobiology , vol.13
    • Elbein, A.D.1    Pan, Y.T.2    Pastuszak, I.3    Carroll, D.4
  • 3
    • 80053907355 scopus 로고    scopus 로고
    • Mechanistic analysis of trehalose synthase from Mycobacterium smegmatis
    • 21840994
    • Zhang R, Pan YT, He SM, Lam M, Brayer GD, et al. (2001) Mechanistic analysis of trehalose synthase from Mycobacterium smegmatis. J Biol Chem 286: 35601-35609. PubMed: 21840994.
    • (2001) J Biol Chem , vol.286 , pp. 35601-35609
    • Zhang, R.1    Pan, Y.T.2    He, S.M.3    Lam, M.4    Brayer, G.D.5
  • 4
    • 0037162460 scopus 로고    scopus 로고
    • Trehalose synthesis is induced upon exposure of Escherichia coli to cold and is essential for viability at low temperatures
    • 10.1073/pnas.142314099
    • Kandror O, DeLeon A, Goldberg AL, (2002) Trehalose synthesis is induced upon exposure of Escherichia coli to cold and is essential for viability at low temperatures. Proc Natl Acad Sci U S A 99: 9727-9732. doi:10.1073/pnas.142314099. PubMed: 12105274.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 9727-9732
    • Kandror, O.1    DeLeon, A.2    Goldberg, A.L.3
  • 5
    • 22144455041 scopus 로고    scopus 로고
    • Enhanced trehalose production improves growth of Escherichia coli under osmotic stress
    • 10.1128/AEM.71.7.3761-3769.2005
    • Purvis JE, Yomano LP, Ingram LO, (2005) Enhanced trehalose production improves growth of Escherichia coli under osmotic stress. Appl Environ Microbiol 71: 3761-3769. doi:10.1128/AEM.71.7.3761-3769.2005. PubMed: 16000787.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 3761-3769
    • Purvis, J.E.1    Yomano, L.P.2    Ingram, L.O.3
  • 6
    • 0742304300 scopus 로고    scopus 로고
    • The importance of a functional trehalose biosynthetic pathway for the life of yeasts and fungi
    • 10.1016/S1567-1356(03)00222-8
    • Gancedo C, Flores CL, (2004) The importance of a functional trehalose biosynthetic pathway for the life of yeasts and fungi. FEMS Yeast Res 4: 351-359. doi:10.1016/S1567-1356(03)00222-8. PubMed: 14734015.
    • (2004) FEMS Yeast Res , vol.4 , pp. 351-359
    • Gancedo, C.1    Flores, C.L.2
  • 7
    • 0024454522 scopus 로고
    • Effect of growth-conditions and trehalose content on cryotolerance of bakers' yeast in frozen doughs
    • 16348024
    • Gélinas P, Fiset G, Leduy A, Goulet J, (1989) Effect of growth-conditions and trehalose content on cryotolerance of bakers' yeast in frozen doughs. Appl Environ Microbiol 55: 2453-2459. PubMed: 16348024.
    • (1989) Appl Environ Microbiol , vol.55 , pp. 2453-2459
    • Gélinas, P.1    Fiset, G.2    Leduy, A.3    Goulet, J.4
  • 8
    • 0026562056 scopus 로고
    • Anhydrobiosis
    • 10.1146/annurev.ph.54.030192.003051
    • Crowe JH, Hoekstra FA, Crowe LM, (1992) Anhydrobiosis. Annu Rev Physiol 54: 579-599. doi:10.1146/annurev.ph.54.030192.003051. PubMed: 1562184.
    • (1992) Annu Rev Physiol , vol.54 , pp. 579-599
    • Crowe, J.H.1    Hoekstra, F.A.2    Crowe, L.M.3
  • 9
    • 0016689944 scopus 로고
    • On the formation of glycogen and trehalose in baker's yeast
    • 10.1007/BF01385443
    • Grba S, Oura E, Suomalainen H, (1975) On the formation of glycogen and trehalose in baker's yeast. Eur J Appl Microbiol 2: 29-31. doi:10.1007/BF01385443.
    • (1975) Eur J Appl Microbiol , vol.2 , pp. 29-31
    • Grba, S.1    Oura, E.2    Suomalainen, H.3
  • 10
    • 0028054926 scopus 로고
    • The role of trehalose synthesis for the acquisition of thermotolerance in yeast
    • Hottiger T, Devirgilio C, Hall MN, Boller T, Wiemken A, (1994) The role of trehalose synthesis for the acquisition of thermotolerance in yeast. Eur J Biochem 19: 187-193.
    • (1994) Eur J Biochem , vol.19 , pp. 187-193
    • Hottiger, T.1    Devirgilio, C.2    Hall, M.N.3    Boller, T.4    Wiemken, A.5
  • 11
    • 33846909430 scopus 로고    scopus 로고
    • The natural osmolyte trehalose is a positive regulator of the heat-induced activity of yeast heat shock transcription factor
    • 10.1128/MCB.01158-06
    • Conlin LK, Nelson HCM, (2007) The natural osmolyte trehalose is a positive regulator of the heat-induced activity of yeast heat shock transcription factor. Mol Cell Biol 27: 1505-1515. doi:10.1128/MCB.01158-06. PubMed: 17145780.
    • (2007) Mol Cell Biol , vol.27 , pp. 1505-1515
    • Conlin, L.K.1    Nelson, H.C.M.2
  • 12
    • 58149477054 scopus 로고    scopus 로고
    • Effect of trehalose on protein structure
    • 19177348
    • Jain NK, Roy I, (2009) Effect of trehalose on protein structure. Protein Sci 18: 24-36. PubMed: 19177348.
    • (2009) Protein Sci , vol.18 , pp. 24-36
    • Jain, N.K.1    Roy, I.2
  • 13
    • 0035968318 scopus 로고    scopus 로고
    • Trehalose accumulation during cellular stress protects cells and cellular proteins from damage by oxygen radicals
    • 10.1074/jbc.M101487200
    • Benaroudj N, Lee DH, Goldberg AL, (2001) Trehalose accumulation during cellular stress protects cells and cellular proteins from damage by oxygen radicals. J Biol Chem 276: 24261-24267. doi:10.1074/jbc.M101487200. PubMed: 11301331.
    • (2001) J Biol Chem , vol.276 , pp. 24261-24267
    • Benaroudj, N.1    Lee, D.H.2    Goldberg, A.L.3
  • 14
    • 79954514686 scopus 로고    scopus 로고
    • Trehalose: current use and future applications
    • 10.1002/jps.22458
    • Ohtake S, Wang YJ, (2011) Trehalose: current use and future applications. J Pharm Sci 100: 2020-2053. doi:10.1002/jps.22458. PubMed: 21337544.
    • (2011) J Pharm Sci , vol.100 , pp. 2020-2053
    • Ohtake, S.1    Wang, Y.J.2
  • 15
    • 72049083976 scopus 로고    scopus 로고
    • TB Research at UT-Houston-A review of cord factor: new approaches to drugs, vaccines and the pathogenesis of tuberculosis
    • 10.1016/S1472-9792(09)70007-1
    • Hunter RL, Armitige L, Jagannath C, Actor JK, (2009) TB Research at UT-Houston-A review of cord factor: new approaches to drugs, vaccines and the pathogenesis of tuberculosis. Tuberculosis 89: S18-S25. doi:10.1016/S1472-9792(09)70007-1. PubMed: 20006299.
    • (2009) Tuberculosis , vol.89
    • Hunter, R.L.1    Armitige, L.2    Jagannath, C.3    Actor, J.K.4
  • 16
    • 33751256585 scopus 로고    scopus 로고
    • Multiple roles of cord factor in the pathogenesis of primary, secondary, and cavitary tuberculosis, including a revised description of the pathology of secondary disease
    • 17127724
    • Hunter RL, Olsen MR, Jagannath C, Actor JK, (2006) Multiple roles of cord factor in the pathogenesis of primary, secondary, and cavitary tuberculosis, including a revised description of the pathology of secondary disease. Ann Clin Lab Sci 36: 371-386. PubMed: 17127724.
    • (2006) Ann Clin Lab Sci , vol.36 , pp. 371-386
    • Hunter, R.L.1    Olsen, M.R.2    Jagannath, C.3    Actor, J.K.4
  • 17
    • 0030309476 scopus 로고    scopus 로고
    • Biotechnological applications of the disaccharide trehalose
    • 10.1016/S1387-2656(08)70015-2
    • Paiva CL, Panek AD, (1996) Biotechnological applications of the disaccharide trehalose. Biotechnol Annu Rev 2: 293-314. doi:10.1016/S1387-2656(08)70015-2. PubMed: 9704101.
    • (1996) Biotechnol Annu Rev , vol.2 , pp. 293-314
    • Paiva, C.L.1    Panek, A.D.2
  • 18
    • 0029391228 scopus 로고
    • Formation of trehalose from maltooligosaccharides by a novel enzymatic system
    • 10.1271/bbb.59.1829
    • Maruta K, Nakada T, Kubota M, Chaen H, Sugimoto T, et al. (1995) Formation of trehalose from maltooligosaccharides by a novel enzymatic system. Biosci Biotechnol Biochem 59: 1829-1834. doi:10.1271/bbb.59.1829. PubMed: 8534970.
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 1829-1834
    • Maruta, K.1    Nakada, T.2    Kubota, M.3    Chaen, H.4    Sugimoto, T.5
  • 19
    • 84861580150 scopus 로고    scopus 로고
    • Integrated biocatalytic process for trehalose production and separation from rice hydrolysate using a bioreactor system
    • 10.1016/j.foodchem.2012.03.065
    • Chang SW, Liu PT, Hsu LC, Chen CS, Shaw JF, (2012) Integrated biocatalytic process for trehalose production and separation from rice hydrolysate using a bioreactor system. Food Chem 134: 1745-1753. doi:10.1016/j.foodchem.2012.03.065. PubMed: 23442616.
    • (2012) Food Chem , vol.134 , pp. 1745-1753
    • Chang, S.W.1    Liu, P.T.2    Hsu, L.C.3    Chen, C.S.4    Shaw, J.F.5
  • 20
    • 0001642923 scopus 로고
    • Existence of a novel enzyme converting maltose into trehalose
    • 10.1271/bbb.59.2189
    • Nishimoto T, Nakano M, Ikegami S, Chaen H, Fukuda S, et al. (1995) Existence of a novel enzyme converting maltose into trehalose. Biosci Biotechnol Biochem 59: 2189-2190. doi:10.1271/bbb.59.2189.
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 2189-2190
    • Nishimoto, T.1    Nakano, M.2    Ikegami, S.3    Chaen, H.4    Fukuda, S.5
  • 21
    • 23944495106 scopus 로고    scopus 로고
    • Metagenomics for studying unculturable microorganisms: cutting the Gordian knot
    • 10.1186/gb-2005-6-8-229
    • Schloss PD, Handelsman J, (2005) Metagenomics for studying unculturable microorganisms: cutting the Gordian knot. Genome Biol 6: 229. doi:10.1186/gb-2005-6-8-229. PubMed: 16086859.
    • (2005) Genome Biol , vol.6 , pp. 229
    • Schloss, P.D.1    Handelsman, J.2
  • 22
    • 77949917038 scopus 로고    scopus 로고
    • Expression of a Glucose-tolerant beta-glucosidase from Humicola grisea var. thermoidea in Saccharomyces cerevisiae
    • 10.1007/s12010-009-8732-7
    • Benoliel B, Poças-Fonseca MJ, Torres FAG, de Moraes LMP, (2010) Expression of a Glucose-tolerant beta-glucosidase from Humicola grisea var. thermoidea in Saccharomyces cerevisiae. Appl Biochem Biotechnol 160: 2036-2044. doi:10.1007/s12010-009-8732-7. PubMed: 19669941.
    • (2010) Appl Biochem Biotechnol , vol.160 , pp. 2036-2044
    • Benoliel, B.1    Poças-Fonseca, M.J.2    Torres, F.A.G.3    de Moraes, L.M.P.4
  • 23
    • 71349088748 scopus 로고    scopus 로고
    • Achievements and new knowledge unraveled by metagenomic approaches
    • 10.1007/s00253-009-2233-z
    • Simon C, Daniel R, (2009) Achievements and new knowledge unraveled by metagenomic approaches. Appl Microbiol Biotechnol 85: 265-276. doi:10.1007/s00253-009-2233-z. PubMed: 19760178.
    • (2009) Appl Microbiol Biotechnol , vol.85 , pp. 265-276
    • Simon, C.1    Daniel, R.2
  • 24
    • 79955002051 scopus 로고    scopus 로고
    • Isolation and characterization of a novel tannase from a metagenomic library
    • 10.1021/jf104394m
    • Yao J, Fan XJ, Lu Y, Liu YH, (2011) Isolation and characterization of a novel tannase from a metagenomic library. J Agric Food Chem 59: 3812-3818. doi:10.1021/jf104394m. PubMed: 21388130.
    • (2011) J Agric Food Chem , vol.59 , pp. 3812-3818
    • Yao, J.1    Fan, X.J.2    Lu, Y.3    Liu, Y.H.4
  • 25
    • 0030070838 scopus 로고    scopus 로고
    • DNA recovery from soils of diverse composition
    • 8593035
    • Zhou JZ, Bruns MA, Tiedje JM, (1996) DNA recovery from soils of diverse composition. Appl Environ Microbiol 62: 316-322. PubMed: 8593035.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 316-322
    • Zhou, J.Z.1    Bruns, M.A.2    Tiedje, J.M.3
  • 26
    • 84873702019 scopus 로고    scopus 로고
    • Cloning, expression, properties, and functional amino acid residues of new trehalose synthase from Thermomonospora curvata DSM 43183
    • 10.1016/j.molcatb.2013.01.014
    • Liang JY, Huang RB, Huang Y, Wang XB, Du LQ, et al. (2013) Cloning, expression, properties, and functional amino acid residues of new trehalose synthase from Thermomonospora curvata DSM 43183. J Mol Catal Benzym 90: 26-32. doi:10.1016/j.molcatb.2013.01.014.
    • (2013) J Mol Catal Benzym , vol.90 , pp. 26-32
    • Liang, J.Y.1    Huang, R.B.2    Huang, Y.3    Wang, X.B.4    Du, L.Q.5
  • 27
    • 84855962980 scopus 로고    scopus 로고
    • Adaptive evolution for fast growth on glucose and the effects on the regulation of glucose transport system in Clostridium tyrobutyricum
    • 10.1002/bit.23346
    • Jiang L, Li S, Hu Y, Xu Q, Huang H, (2012) Adaptive evolution for fast growth on glucose and the effects on the regulation of glucose transport system in Clostridium tyrobutyricum. Biotechnol Bioeng 109(3):: 708-718. doi:10.1002/bit.23346. PubMed: 21956266.
    • (2012) Biotechnol Bioeng , vol.109 , pp. 708-718
    • Jiang, L.1    Li, S.2    Hu, Y.3    Xu, Q.4    Huang, H.5
  • 28
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling
    • 10.1002/elps.1150181505
    • Guex N, Peitsch MC, (1997) SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling. Electrophoresis 18: 2714--2723. doi:10.1002/elps.1150181505. PubMed: 9504803.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 29
    • 84873739307 scopus 로고    scopus 로고
    • Properties of recombinant trehalose synthase from Deinococcus radiodurans expressed in Escherichia coli
    • 23032750
    • Filipkowski P, Pietrow O, Panek A, Synowiecki J, (2012) Properties of recombinant trehalose synthase from Deinococcus radiodurans expressed in Escherichia coli. Acta Biochim Pol 59: 425-431. PubMed: 23032750.
    • (2012) Acta Biochim Pol , vol.59 , pp. 425-431
    • Filipkowski, P.1    Pietrow, O.2    Panek, A.3    Synowiecki, J.4
  • 30
    • 0035155847 scopus 로고    scopus 로고
    • Analysis and modification of trehalose 6-phosphate levels in the yeast Saccharomyces cerevisiae with the use of Bacillus subtilis phosphotrehalase
    • 11115409
    • Van Vaeck C, Wera S, Van Dijck P, Thevelein JM, (2001) Analysis and modification of trehalose 6-phosphate levels in the yeast Saccharomyces cerevisiae with the use of Bacillus subtilis phosphotrehalase. Biochem J 353: 157-162. PubMed: 11115409.
    • (2001) Biochem J , vol.353 , pp. 157-162
    • Van Vaeck, C.1    Wera, S.2    Van Dijck, P.3    Thevelein, J.M.4
  • 31
    • 78349313324 scopus 로고    scopus 로고
    • Structural insights on the new mechanism of trehalose synthesis by trehalose synthase TreT from Pyrococcus horikoshii
    • 10.1016/j.jmb.2010.09.056
    • Woo EJ, Ryu SI, Song HN, Jung TY, Yeon SM, et al. (2010) Structural insights on the new mechanism of trehalose synthesis by trehalose synthase TreT from Pyrococcus horikoshii. J Mol Biol 404: 247-259. doi:10.1016/j.jmb.2010.09.056. PubMed: 20888836.
    • (2010) J Mol Biol , vol.404 , pp. 247-259
    • Woo, E.J.1    Ryu, S.I.2    Song, H.N.3    Jung, T.Y.4    Yeon, S.M.5
  • 32
    • 0042069937 scopus 로고    scopus 로고
    • Cloning and characterization of a gene encoding trehalose phosphorylase (TP) from Pleurotus sajor-caju
    • 10.1016/S1046-5928(03)00104-9
    • Han SE, Kwon HB, Lee SB, Yi BY, Murayama I, et al. (2003) Cloning and characterization of a gene encoding trehalose phosphorylase (TP) from Pleurotus sajor-caju. Protein Expr Purif 30: 194-202. doi:10.1016/S1046-5928(03)00104-9. PubMed: 12880768.
    • (2003) Protein Expr Purif , vol.30 , pp. 194-202
    • Han, S.E.1    Kwon, H.B.2    Lee, S.B.3    Yi, B.Y.4    Murayama, I.5
  • 33
    • 0033754243 scopus 로고    scopus 로고
    • Trehalose synthesis by sequential reactions of recombinant maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase from Brevibacterium helvolum
    • 10.1128/AEM.66.11.4620-4624.2000
    • Kim YH, Kwon TK, Park S, Seo HS, Cheong JJ, et al. (2000) Trehalose synthesis by sequential reactions of recombinant maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase from Brevibacterium helvolum. Appl Environ Microbiol 66: 4620-4624. doi:10.1128/AEM.66.11.4620-4624.2000. PubMed: 11055902.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 4620-4624
    • Kim, Y.H.1    Kwon, T.K.2    Park, S.3    Seo, H.S.4    Cheong, J.J.5
  • 34
    • 33846621068 scopus 로고    scopus 로고
    • Insights on the evolution of trehalose biosynthesis
    • 10.1186/1471-2148-6-109
    • Avonce N, Mendoza-Vargas A, Morett E, Iturriaga G, (2006) Insights on the evolution of trehalose biosynthesis. BMC Evol Biol 6: 109. doi:10.1186/1471-2148-6-109. PubMed: 17178000.
    • (2006) BMC Evol Biol , vol.6 , pp. 109
    • Avonce, N.1    Mendoza-Vargas, A.2    Morett, E.3    Iturriaga, G.4
  • 35
    • 4444273325 scopus 로고    scopus 로고
    • Cloning, expression and identification of a new trehalose synthase gene from Thermobifida fusca genome
    • 10.1093/abbs/36.7.477
    • Wei YT, Zhu QX, Luo ZF, Lu FS, Chen FZ, et al. (2004) Cloning, expression and identification of a new trehalose synthase gene from Thermobifida fusca genome. Acta Biochim Biophys Sin 36: 477-484. doi:10.1093/abbs/36.7.477. PubMed: 15248022.
    • (2004) Acta Biochim Biophys Sin , vol.36 , pp. 477-484
    • Wei, Y.T.1    Zhu, Q.X.2    Luo, Z.F.3    Lu, F.S.4    Chen, F.Z.5
  • 36
    • 67649863768 scopus 로고    scopus 로고
    • Molecular cloning and expression of a novel trehalose synthase gene from Enterobacter hormaechei
    • 10.1186/1475-2859-8-34
    • Yue M, Wu XL, Gong WN, Ding HB, (2009) Molecular cloning and expression of a novel trehalose synthase gene from Enterobacter hormaechei. Microb Cell Factories 8: 34. doi:10.1186/1475-2859-8-34. PubMed: 19523196.
    • (2009) Microb Cell Factories , vol.8 , pp. 34
    • Yue, M.1    Wu, X.L.2    Gong, W.N.3    Ding, H.B.4
  • 37
    • 67349177547 scopus 로고    scopus 로고
    • Gene cloning, expression, and characterization of a novel trehalose synthase from Arthrobacter aurescens
    • 10.1007/s00253-009-1863-5
    • Wu XL, Ding HB, Yue M, Qiao Y, (2009) Gene cloning, expression, and characterization of a novel trehalose synthase from Arthrobacter aurescens. Appl Microbiol Biotechnol 83: 477-482. doi:10.1007/s00253-009-1863-5. PubMed: 19172263.
    • (2009) Appl Microbiol Biotechnol , vol.83 , pp. 477-482
    • Wu, X.L.1    Ding, H.B.2    Yue, M.3    Qiao, Y.4
  • 38
    • 0023661282 scopus 로고
    • Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity
    • 3502087
    • Buisson G, Duée E, Haser R, Payan F, (1987) Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity. EMBO J 6: 3909-3916. PubMed: 3502087.
    • (1987) EMBO J , vol.6 , pp. 3909-3916
    • Buisson, G.1    Duée, E.2    Haser, R.3    Payan, F.4
  • 39
    • 33749676801 scopus 로고    scopus 로고
    • Gene cloning, expression, and biochemical characterization of a recombinant trehalose synthase from Picrophilus torridus in Escherichia coli
    • 10.1021/jf060828q
    • Chen YS, Lee GC, Shaw JF, (2006) Gene cloning, expression, and biochemical characterization of a recombinant trehalose synthase from Picrophilus torridus in Escherichia coli. J Agric Food Chem 54: 7098-7104. doi:10.1021/jf060828q. PubMed: 16968068.
    • (2006) J Agric Food Chem , vol.54 , pp. 7098-7104
    • Chen, Y.S.1    Lee, G.C.2    Shaw, J.F.3
  • 40
    • 34249298002 scopus 로고    scopus 로고
    • Role of the C-terminal domain of Thermus thermophilus trehalose synthase in the thermophilicity, thermostability, and efficient production of trehalose
    • 10.1021/jf070181p
    • Wang JH, Tsai MY, Chen JJ, Lee GC, Shaw JF, (2007) Role of the C-terminal domain of Thermus thermophilus trehalose synthase in the thermophilicity, thermostability, and efficient production of trehalose. J Agric Food Chem 55: 3435-3443. doi:10.1021/jf070181p. PubMed: 17394343.
    • (2007) J Agric Food Chem , vol.55 , pp. 3435-3443
    • Wang, J.H.1    Tsai, M.Y.2    Chen, J.J.3    Lee, G.C.4    Shaw, J.F.5
  • 41
    • 23444448605 scopus 로고    scopus 로고
    • Cloning and expression of a trehalose synthase from Pseudomonas stutzeri CJ38 in Escherichia coli for the production of trehalose
    • 10.1007/s00253-004-1862-5
    • Lee JH, Lee KH, Kim CG, Lee SY, Kim GJ, et al. (2005) Cloning and expression of a trehalose synthase from Pseudomonas stutzeri CJ38 in Escherichia coli for the production of trehalose. Appl Microbiol Biotechnol 68: 213-219. doi:10.1007/s00253-004-1862-5. PubMed: 15654636.
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 213-219
    • Lee, J.H.1    Lee, K.H.2    Kim, C.G.3    Lee, S.Y.4    Kim, G.J.5
  • 42
    • 0025868757 scopus 로고
    • Thermodynamics of hydrolysis of disaccharides. Lactulose, alpha-D-melibiose, palatinose, D-trehalose, D-turanose and 3-o-beta-D-galactopyranosyl-D-arabinose
    • 10.1016/0301-4622(91)85029-P
    • Tewari YB, Goldberg RN, (1991) Thermodynamics of hydrolysis of disaccharides. Lactulose, alpha-D-melibiose, palatinose, D-trehalose, D-turanose and 3-o-beta-D-galactopyranosyl-D-arabinose. Biophys Chem 40: 59-67. doi:10.1016/0301-4622(91)85029-P. PubMed: 1873472.
    • (1991) Biophys Chem , vol.40 , pp. 59-67
    • Tewari, Y.B.1    Goldberg, R.N.2
  • 43
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics
    • 10.1093/nar/gkn663
    • Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, et al. (2009) The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res 37: D233-D238. doi:10.1093/nar/gkn663. PubMed: 18838391.
    • (2009) Nucleic Acids Res , vol.37
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5
  • 44
    • 0031591389 scopus 로고    scopus 로고
    • The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 angstrom resolution: Structural characterization of proline-substitution sites for protein thermostabilization
    • 10.1006/jmbi.1997.1018
    • 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 angstrom resolution: Structural characterization of proline-substitution sites for protein thermostabilization. J Mol Biol 269: 142-153. doi:10.1006/jmbi.1997.1018. PubMed: 9193006.
    • (1997) J Mol Biol , vol.269 , pp. 142-153
    • Watanabe, K.1    Hata, Y.2    Kizaki, H.3    Katsube, Y.4    Suzuki, Y.5
  • 45
    • 0035979360 scopus 로고    scopus 로고
    • Crystal structures of amylosucrase from Neisseria polysaccharea in complex with D-glucose and the active site mutant Glu328Gln in complex with the natural substrate sucrose
    • 10.1021/bi010706l
    • Mirza O, Skov LK, Remaud-Simeon M, de Montalk GP, Albenne C, et al. (2001) Crystal structures of amylosucrase from Neisseria polysaccharea in complex with D-glucose and the active site mutant Glu328Gln in complex with the natural substrate sucrose. Biochemistry 40: 9032-9039. doi:10.1021/bi010706l. PubMed: 11467966.
    • (2001) Biochemistry , vol.40 , pp. 9032-9039
    • Mirza, O.1    Skov, L.K.2    Remaud-Simeon, M.3    de Montalk, G.P.4    Albenne, C.5
  • 46
    • 34948875934 scopus 로고    scopus 로고
    • Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization
    • 10.1074/jbc.M704515200
    • Ravaud S, Robert X, Watzlawick H, Haser R, Mattes R, et al. (2007) Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization. J Biol Chem 282: 28126-28136. doi:10.1074/jbc.M704515200. PubMed: 17597061.
    • (2007) J Biol Chem , vol.282 , pp. 28126-28136
    • Ravaud, S.1    Robert, X.2    Watzlawick, H.3    Haser, R.4    Mattes, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.