메뉴 건너뛰기




Volumn 82, Issue 2, 2016, Pages 756-766

The Exiguobacterium sibiricum 255-15 GtfC enzyme represents a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; HYDROLASES; LACTIC ACID; PLANTS (BOTANY); SUGAR (SUCROSE); SUGARS;

EID: 84953897942     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03420-15     Document Type: Article
Times cited : (45)

References (34)
  • 1
    • 33845665889 scopus 로고    scopus 로고
    • Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of alpha-amylase-related proteins
    • Stam MR, Danchin EG, Rancurel C, Coutinho PM, Henrissat B. 2006. Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of alpha-amylase-related proteins. Protein Eng Des Sel 19:555-562. http://dx.doi.org/10.1093/protein/gzl044.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 555-562
    • Stam, M.R.1    Danchin, E.G.2    Rancurel, C.3    Coutinho, P.M.4    Henrissat, B.5
  • 2
    • 0037187437 scopus 로고    scopus 로고
    • Properties and applications of starch-converting enzymes of the alpha-amylase family
    • van der Maarel MJ, van der Veen B, Uitdehaag JC, Leemhuis H, Dijkhuizen L. 2002. Properties and applications of starch-converting enzymes of the alpha-amylase family. J Biotechnol 94:137-155. http://dx.doi.org/10.1016/S0168-1656(01)00407-2.
    • (2002) J Biotechnol , vol.94 , pp. 137-155
    • van der Maarel, M.J.1    van der Veen, B.2    Uitdehaag, J.C.3    Leemhuis, H.4    Dijkhuizen, L.5
  • 3
    • 0032896501 scopus 로고    scopus 로고
    • Glucansucrases: mechanism of action and structure-function relationships
    • Monchois V, Willemot RM, Monsan P. 1999. Glucansucrases: mechanism of action and structure-function relationships. FEMS Microbiol Rev 23:131-151.
    • (1999) FEMS Microbiol Rev , vol.23 , pp. 131-151
    • Monchois, V.1    Willemot, R.M.2    Monsan, P.3
  • 4
    • 4344560401 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of Lactobacillus reuteri 121 reuteransucrase
    • Kralj S, van Geel-Schutten GH, van der Maarel MJ, Dijkhuizen L. 2004. Biochemical and molecular characterization of Lactobacillus reuteri 121 reuteransucrase. Microbiology 150:2099-2112. http://dx.doi.org/10.1099/mic.0.27105-0.
    • (2004) Microbiology , vol.150 , pp. 2099-2112
    • Kralj, S.1    van Geel-Schutten, G.H.2    van der Maarel, M.J.3    Dijkhuizen, L.4
  • 5
    • 0032964202 scopus 로고    scopus 로고
    • X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family
    • Uitdehaag JC, Mosi R, Kalk KH, van der Veen BA, Dijkhuizen L, Withers SG, Dijkstra BW. 1999. X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family. Nat Struct Biol 6:432-436. http://dx.doi.org/10.1038/8235.
    • (1999) Nat Struct Biol , vol.6 , pp. 432-436
    • Uitdehaag, J.C.1    Mosi, R.2    Kalk, K.H.3    van der Veen, B.A.4    Dijkhuizen, L.5    Withers, S.G.6    Dijkstra, B.W.7
  • 6
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes
    • MacGregor EA, Janeček Š, Svensson B. 2001. Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. Biochim Biophys Acta 1546:1-20. http://dx.doi.org/10.1016/S0167-4838(00)00302-2.
    • (2001) Biochim Biophys Acta , vol.1546 , pp. 1-20
    • MacGregor, E.A.1    Janeček, Š.2    Svensson, B.3
  • 7
    • 78650734599 scopus 로고    scopus 로고
    • Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes
    • Vujičič-Žagar A, Pijning T, Kralj S, López CA, Eeuwema W, Dijkhuizen L, Dijkstra BW. 2010. Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes. Proc Natl Acad Sci U S A 107:21406-21411. http://dx.doi.org/10.1073/pnas.1007531107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 21406-21411
    • Vujičič-Žagar, A.1    Pijning, T.2    Kralj, S.3    López, C.A.4    Eeuwema, W.5    Dijkhuizen, L.6    Dijkstra, B.W.7
  • 8
    • 84932191952 scopus 로고    scopus 로고
    • Truncation of domain V of the multidomain glucansucrase GTF180 of Lactobacillus reuteri 180 heavily impairs its polysaccha-ride-synthesizing ability
    • Meng X, Dobruchowska JM, Pijning T, Gerwig GJ, Kamerling JP, Dijkhuizen L. 2015. Truncation of domain V of the multidomain glucansucrase GTF180 of Lactobacillus reuteri 180 heavily impairs its polysaccha-ride-synthesizing ability. Appl Microbiol Biotechnol 99:5885-5894. http://dx.doi.org/10.1007/s00253-014-6361-8.
    • (2015) Appl Microbiol Biotechnol , vol.99 , pp. 5885-5894
    • Meng, X.1    Dobruchowska, J.M.2    Pijning, T.3    Gerwig, G.J.4    Kamerling, J.P.5    Dijkhuizen, L.6
  • 9
    • 0029671161 scopus 로고    scopus 로고
    • A circularly permuted alpha-amylase-type alpha/beta-barrel structure in glucan-synthesizing glucosyltransferases
    • MacGregor EA, Jespersen HM, Svensson B. 1996. A circularly permuted alpha-amylase-type alpha/beta-barrel structure in glucan-synthesizing glucosyltransferases. FEBS Lett 378:263-266. http://dx.doi.org/10.1016/0014-5793(95)01428-4.
    • (1996) FEBS Lett , vol.378 , pp. 263-266
    • MacGregor, E.A.1    Jespersen, H.M.2    Svensson, B.3
  • 11
    • 84857938342 scopus 로고    scopus 로고
    • Structural characterization of linear isomalto-/malto-oligomer products synthesized by the novel GTFB 4,6-α-glucanotransferase enzyme from Lactobacillus reuteri 121
    • Dobruchowska JM, Gerwig GJ, Kralj S, Grijpstra P, Leemhuis H, Dijkhuizen L, Kamerling JP. 2012. Structural characterization of linear isomalto-/malto-oligomer products synthesized by the novel GTFB 4,6-α-glucanotransferase enzyme from Lactobacillus reuteri 121. Glycobiology 22:517-528. http://dx.doi.org/10.1093/glycob/cwr167.
    • (2012) Glycobiology , vol.22 , pp. 517-528
    • Dobruchowska, J.M.1    Gerwig, G.J.2    Kralj, S.3    Grijpstra, P.4    Leemhuis, H.5    Dijkhuizen, L.6    Kamerling, J.P.7
  • 15
    • 33748299372 scopus 로고    scopus 로고
    • Characterization of Exiguobacterium isolates from the Siberian permafrost. Description of Exiguobacterium sibiricum sp. nov
    • Rodrigues DF, Goris J, Vishnivetskaya T, Gilichinsky D, Thomashow MF, Tiedje JM. 2006. Characterization of Exiguobacterium isolates from the Siberian permafrost. Description of Exiguobacterium sibiricum sp. nov. Extremophiles 10:285-294.
    • (2006) Extremophiles , vol.10 , pp. 285-294
    • Rodrigues, D.F.1    Goris, J.2    Vishnivetskaya, T.3    Gilichinsky, D.4    Thomashow, M.F.5    Tiedje, J.M.6
  • 16
    • 58149510474 scopus 로고    scopus 로고
    • Architecture of thermal adaptation in an Exiguobacterium sibiricum strain isolated from 3 million year old permafrost: a genome and transcriptome approach
    • Rodrigues DF, Ivanova N, He Z, Huebner M, Zhou J, Tiedje JM. 2008. Architecture of thermal adaptation in an Exiguobacterium sibiricum strain isolated from 3 million year old permafrost: a genome and transcriptome approach. BMC Genomics 9:547. http://dx.doi.org/10.1186/1471-2164-9-547.
    • (2008) BMC Genomics , vol.9 , pp. 547
    • Rodrigues, D.F.1    Ivanova, N.2    He, Z.3    Huebner, M.4    Zhou, J.5    Tiedje, J.M.6
  • 17
    • 84890330527 scopus 로고    scopus 로고
    • MEGA6: Molecular Evolutionary Genetics Analysis version 6.0
    • Tamura K, Stecher G, Peterson D, Filipski A, Kumar S. 2013. MEGA6: Molecular Evolutionary Genetics Analysis version 6.0. Mol Biol Evol 30: 2725-2729. http://dx.doi.org/10.1093/molbev/mst197.
    • (2013) Mol Biol Evol , vol.30 , pp. 2725-2729
    • Tamura, K.1    Stecher, G.2    Peterson, D.3    Filipski, A.4    Kumar, S.5
  • 18
    • 65449188232 scopus 로고    scopus 로고
    • Jalview version 2-a multiple sequence alignment editor and analysis workbench
    • Waterhouse AM, Procter JB, Martin DM, Clamp M, Barton GJ. 2009. Jalview version 2-a multiple sequence alignment editor and analysis workbench. Bioinformatics 25:1189-1191. http://dx.doi.org/10.1093/bioinformatics/btp033.
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 20
    • 84943327444 scopus 로고    scopus 로고
    • Biochemical characterization of Lactobacillus reuteri glycoside hydrolase family 70 GTFB type of 4,6-α-glucanotransferase enzymes that synthesize soluble dietary starch fibers
    • Bai Y, van der Kaaij RM, Leemhuis H, Pijning T, van Leeuwen SS, Jin Z, Dijkhuizen L. 2015. Biochemical characterization of Lactobacillus reuteri glycoside hydrolase family 70 GTFB type of 4,6-α-glucanotransferase enzymes that synthesize soluble dietary starch fibers. Appl Environ Microbiol 81:7223-7232. http://dx.doi.org/10.1128/AEM.01860-15.
    • (2015) Appl Environ Microbiol , vol.81 , pp. 7223-7232
    • Bai, Y.1    van der Kaaij, R.M.2    Leemhuis, H.3    Pijning, T.4    van Leeuwen, S.S.5    Jin, Z.6    Dijkhuizen, L.7
  • 21
    • 84872202291 scopus 로고    scopus 로고
    • Glucansucrases: three-dimensional structures, reactions, mechanism, α-glucan analysis and their implications in biotechnology and food applications
    • Leemhuis H, Pijning T, Dobruchowska JM, van Leeuwen SS, Kralj S, Dijkstra BW, Dijkhuizen L. 2013. Glucansucrases: three-dimensional structures, reactions, mechanism, α-glucan analysis and their implications in biotechnology and food applications. J Biotechnol 163:250-272. http://dx.doi.org/10.1016/j.jbiotec.2012.06.037.
    • (2013) J Biotechnol , vol.163 , pp. 250-272
    • Leemhuis, H.1    Pijning, T.2    Dobruchowska, J.M.3    van Leeuwen, S.S.4    Kralj, S.5    Dijkstra, B.W.6    Dijkhuizen, L.7
  • 24
    • 0034213976 scopus 로고    scopus 로고
    • Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli
    • Batchelor M, Prasannan S, Daniell S, Reece S, Connerton I, Bloomberg G, Dougan G, Frankel G, Matthews S. 2000. Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli. EMBO J 19:2452-2464. http://dx.doi.org/10.1093/emboj/19.11.2452.
    • (2000) EMBO J , vol.19 , pp. 2452-2464
    • Batchelor, M.1    Prasannan, S.2    Daniell, S.3    Reece, S.4    Connerton, I.5    Bloomberg, G.6    Dougan, G.7    Frankel, G.8    Matthews, S.9
  • 25
    • 0037293103 scopus 로고    scopus 로고
    • Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain
    • Janeček Š, Svensson B, MacGregor EA. 2003. Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain. Eur J Biochem 270: 635-645. http://dx.doi.org/10.1046/j.1432-1033.2003.03404.x.
    • (2003) Eur J Biochem , vol.270 , pp. 635-645
    • Janeček, Š.1    Svensson, B.2    MacGregor, E.A.3
  • 26
    • 33845498615 scopus 로고    scopus 로고
    • Starch-binding domains in the postgenome era
    • Machovic M, Janeček Š. 2006. Starch-binding domains in the postgenome era. Cell Mol Life Sci 63:2710-2724. http://dx.doi.org/10.1007/s00018-006-6246-9.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2710-2724
    • Machovic, M.1    Janeček, Š.2
  • 27
    • 33645113873 scopus 로고    scopus 로고
    • Structure-function relationships of glucansucrase and fructansucrase enzymes from lactic acid bacteria
    • van Hijum SA, Kralj S, Ozimek LK, Dijkhuizen L, van Geel-Schutten IG. 2006. Structure-function relationships of glucansucrase and fructansucrase enzymes from lactic acid bacteria. Microbiol Mol Biol Rev 70:157-176. http://dx.doi.org/10.1128/MMBR.70.1.157-176.2006.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 157-176
    • van Hijum, S.A.1    Kralj, S.2    Ozimek, L.K.3    Dijkhuizen, L.4    van Geel-Schutten, I.G.5
  • 28
    • 21744437312 scopus 로고    scopus 로고
    • Rational transformation of Lactobacillus reuteri 121 reuteransucrase into a dextransucrase
    • Kralj S, van Geel-Schutten IG, Faber EJ, van der Maarel MJ, Dijkhuizen L. 2005. Rational transformation of Lactobacillus reuteri 121 reuteransucrase into a dextransucrase. Biochemistry 44:9206-9216. http://dx.doi.org/10.1021/bi050447q.
    • (2005) Biochemistry , vol.44 , pp. 9206-9216
    • Kralj, S.1    van Geel-Schutten, I.G.2    Faber, E.J.3    van der Maarel, M.J.4    Dijkhuizen, L.5
  • 29
    • 65249168070 scopus 로고    scopus 로고
    • Structural characterization of bioengineered alpha-D-glucans produced by mutant glucansucrase GTF180 enzymes of Lactobacillus reuteri strain 180
    • van Leeuwen SS, Kralj S, Eeuwema W, Gerwig GJ, Dijkhuizen L, Kamerling JP. 2009. Structural characterization of bioengineered alpha-D-glucans produced by mutant glucansucrase GTF180 enzymes of Lactobacillus reuteri strain 180. Biomacromolecules 10:580-588. http://dx.doi.org/10.1021/bm801240r.
    • (2009) Biomacromolecules , vol.10 , pp. 580-588
    • van Leeuwen, S.S.1    Kralj, S.2    Eeuwema, W.3    Gerwig, G.J.4    Dijkhuizen, L.5    Kamerling, J.P.6
  • 30
    • 0028085883 scopus 로고
    • Identification of amino acid residues in Streptococcus mutans glucosyltransferases influencing the structure of the glucan product
    • Shimamura A, Nakano YJ, Mukasa H, Kuramitsu HK. 1994. Identification of amino acid residues in Streptococcus mutans glucosyltransferases influencing the structure of the glucan product. J Bacteriol 176:4845-4850.
    • (1994) J Bacteriol , vol.176 , pp. 4845-4850
    • Shimamura, A.1    Nakano, Y.J.2    Mukasa, H.3    Kuramitsu, H.K.4
  • 31
    • 0012286188 scopus 로고    scopus 로고
    • How many conserved sequence regions are there in the α-amylase family?
    • Janeček Š. 2002. How many conserved sequence regions are there in the α-amylase family? Biologia 57(Suppl 11):29-41. http://biologia.savba.sk/Suppl_11/Janec?ek.pdf.
    • (2002) Biologia , vol.57 , pp. 29-41
    • Janeček, Š.1
  • 32
    • 84899863334 scopus 로고    scopus 로고
    • α-Amylase: an enzyme specificity found in various families of glycoside hydrolases
    • Janeček Š, Svensson B, MacGregor EA. 2014. α-Amylase: an enzyme specificity found in various families of glycoside hydrolases. Cell Mol Life Sci 71:1149-1170. http://dx.doi.org/10.1007/s00018-013-1388-z.
    • (2014) Cell Mol Life Sci , vol.71 , pp. 1149-1170
    • Janeček, Š.1    Svensson, B.2    MacGregor, E.A.3
  • 33
    • 84929847000 scopus 로고    scopus 로고
    • Differential metabolism of exopolysaccharides from probiotic Lactobacilli by the human gut symbiont Bacteroides thetaiotaomicron
    • Lammerts van Bueren A, Saraf A, Martens EC, Dijkhuizen L. 2015. Differential metabolism of exopolysaccharides from probiotic Lactobacilli by the human gut symbiont Bacteroides thetaiotaomicron. Appl Environ Microbiol 81:3973-3983. http://dx.doi.org/10.1128/AEM.00149-15.
    • (2015) Appl Environ Microbiol , vol.81 , pp. 3973-3983
    • Lammerts van Bueren, A.1    Saraf, A.2    Martens, E.C.3    Dijkhuizen, L.4
  • 34
    • 31744450975 scopus 로고    scopus 로고
    • Evolution of new protein topologies through multistep gene rearrangements
    • Peisajovich SG, Rockah L, Tawfik DS. 2006. Evolution of new protein topologies through multistep gene rearrangements. Nat Genet 38:168-174. http://dx.doi.org/10.1038/ng1717.
    • (2006) Nat Genet , vol.38 , pp. 168-174
    • Peisajovich, S.G.1    Rockah, L.2    Tawfik, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.