메뉴 건너뛰기




Volumn 275, Issue 23, 2008, Pages 6002-6010

Hybrid reuteransucrase enzymes reveal regions important for glucosidic linkage specificity and the transglucosylation/hydrolysis ratio

Author keywords

Glucansucrase; Glycosidic linkage; Hybrid enzymes; Product specificity; Reuteransucrase

Indexed keywords

1,4 ALPHA GLUCAN BRANCHING ENZYME; GLUCOSIDE; ISOMALTOSE; MALTOSE; OLIGOSACCHARIDE; POLYSACCHARIDE; SUCRASE; SUCROSE;

EID: 55949119834     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06729.x     Document Type: Article
Times cited : (16)

References (29)
  • 1
    • 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
  • 3
    • 0343550404 scopus 로고    scopus 로고
    • Sequence analysis of the gene encoding alternansucrase, a sucrose glucosyltransferase from Leuconostoc mesenteroides NRRL B-1355
    • Arguello-Morales MA, Remaud-Simeon M, Pizzut S, Sarcabal P Monsan P (2000) Sequence analysis of the gene encoding alternansucrase, a sucrose glucosyltransferase from Leuconostoc mesenteroides NRRL B-1355. FEMS Microbiol Lett 182, 81 85.
    • (2000) FEMS Microbiol Lett , vol.182 , pp. 81-85
    • Arguello-Morales, M.A.1    Remaud-Simeon, M.2    Pizzut, S.3    Sarcabal, P.4    Monsan, P.5
  • 4
    • 0036731751 scopus 로고    scopus 로고
    • Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with alpha-(1 - >4) and alpha-(1 - >6) glucosidic bonds
    • Kralj S, van Geel-Schutten GH, Rahaoui H, Leer RJ, Faber EJ, van der Maarel MJ Dijkhuizen L (2002) Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with alpha-(1 - >4) and alpha-(1 - >6) glucosidic bonds. Appl Environ Microbiol 68, 4283 4291.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 4283-4291
    • Kralj, S.1    Van Geel-Schutten, G.H.2    Rahaoui, H.3    Leer, R.J.4    Faber, E.J.5    Van Der Maarel, M.J.6    Dijkhuizen, L.7
  • 6
    • 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.
    • (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
  • 7
    • 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.
    • (1996) FEBS Lett , vol.378 , pp. 263-266
    • MacGregor, E.A.1    Jespersen, H.M.2    Svensson, B.3
  • 8
    • 34547679745 scopus 로고    scopus 로고
    • Identification of structural determinants for substrate binding and turnover by glucosyltransferase R supports the permutation hypothesis
    • Swistowska AM, Gronert S, Wittrock S, Collisi W, Hecht HJ Hofer B (2007) Identification of structural determinants for substrate binding and turnover by glucosyltransferase R supports the permutation hypothesis. FEBS Lett 581, 4036 4042.
    • (2007) FEBS Lett , vol.581 , pp. 4036-4042
    • Swistowska, A.M.1    Gronert, S.2    Wittrock, S.3    Collisi, W.4    Hecht, H.J.5    Hofer, B.6
  • 9
    • 39149100630 scopus 로고    scopus 로고
    • Re- or displacement of invariant residues in the C-terminal half of the catalytic domain strongly affects catalysis by glucosyltransferase R
    • Wittrock S, Swistowska AM, Collisi W, Hofmann B, Hecht HJ Hofer B (2008) Re- or displacement of invariant residues in the C-terminal half of the catalytic domain strongly affects catalysis by glucosyltransferase R. FEBS Lett 582, 491 496.
    • (2008) FEBS Lett , vol.582 , pp. 491-496
    • Wittrock, S.1    Swistowska, A.M.2    Collisi, W.3    Hofmann, B.4    Hecht, H.J.5    Hofer, B.6
  • 10
    • 0347458742 scopus 로고    scopus 로고
    • Involvement of Gln937 of Streptococcus downei GTF-I glucansucrase in transition-state stabilization
    • Monchois V, Vignon M, Escalier PC, Svensson B Russell RR (2000) Involvement of Gln937 of Streptococcus downei GTF-I glucansucrase in transition-state stabilization. Eur J Biochem 267, 4127 4136.
    • (2000) Eur J Biochem , vol.267 , pp. 4127-4136
    • Monchois, V.1    Vignon, M.2    Escalier, P.C.3    Svensson, B.4    Russell, R.R.5
  • 11
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat B Bairoch A (1996) Updating the sequence-based classification of glycosyl hydrolases. Biochem J 316, 695 696.
    • (1996) Biochem J , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 12
    • 33746780057 scopus 로고    scopus 로고
    • Role of asparagine 1134 in glucosidic bond and transglucosylation specificity of reuteransucrase from Lactobacillus reuteri 121
    • Kralj S, Eeuwema W, Eckhardt TH Dijkhuizen L (2006) Role of asparagine 1134 in glucosidic bond and transglucosylation specificity of reuteransucrase from Lactobacillus reuteri 121. FEBS J 273, 3735 3742.
    • (2006) FEBS J , vol.273 , pp. 3735-3742
    • Kralj, S.1    Eeuwema, W.2    Eckhardt, T.H.3    Dijkhuizen, L.4
  • 15
    • 45749092119 scopus 로고    scopus 로고
    • Engineering the glucansucrase GTFR enzyme reaction and glycosidic bond specificity: Toward tailor-made polymer and oligosaccharide products
    • Hellmuth H, Wittrock S, Kralj S, Dijkhuizen L, Hofer B Seibel J (2008) Engineering the glucansucrase GTFR enzyme reaction and glycosidic bond specificity: toward tailor-made polymer and oligosaccharide products. Biochemistry 47, 6678 6684.
    • (2008) Biochemistry , vol.47 , pp. 6678-6684
    • Hellmuth, H.1    Wittrock, S.2    Kralj, S.3    Dijkhuizen, L.4    Hofer, B.5    Seibel, J.6
  • 16
    • 0032697922 scopus 로고    scopus 로고
    • Isolation of key amino acid residues at the N-terminal end of the core region Streptococcus downei glucansucrase, GTF-I
    • Monchois V, Vignon M Russell RR (1999) Isolation of key amino acid residues at the N-terminal end of the core region Streptococcus downei glucansucrase, GTF-I. Appl Microbiol Biotechnol 52, 660 665.
    • (1999) Appl Microbiol Biotechnol , vol.52 , pp. 660-665
    • Monchois, V.1    Vignon, M.2    Russell, R.R.3
  • 17
    • 0037063346 scopus 로고    scopus 로고
    • Maltooligosaccharide disproportionation reaction: An intrinsic property of amylosucrase from Neisseria polysaccharea
    • Albenne C, Skov LK, Mirza O, Gajhede M, Potocki-Veronese G, Monsan P Remaud-Simeon M (2002) Maltooligosaccharide disproportionation reaction: an intrinsic property of amylosucrase from Neisseria polysaccharea. FEBS Lett 527, 67 70.
    • (2002) FEBS Lett , vol.527 , pp. 67-70
    • Albenne, C.1    Skov, L.K.2    Mirza, O.3    Gajhede, M.4    Potocki-Veronese, G.5    Monsan, P.6    Remaud-Simeon, M.7
  • 18
    • 0002639757 scopus 로고
    • A method for the colorimetric estimation of glycogen with iodine
    • Krisman CR (1962) A method for the colorimetric estimation of glycogen with iodine. Anal Biochem 4, 17 23.
    • (1962) Anal Biochem , vol.4 , pp. 17-23
    • Krisman, C.R.1
  • 19
    • 1342286824 scopus 로고    scopus 로고
    • Combinatorial engineering to enhance amylosucrase performance: Construction, selection, and screening of variant libraries for increased activity
    • van der Veen BA, Potocki-Veronese G, Albenne C, Joucla G, Monsan P Remaud-Simeon M (2004) Combinatorial engineering to enhance amylosucrase performance: construction, selection, and screening of variant libraries for increased activity. FEBS Lett 560, 91 97.
    • (2004) FEBS Lett , vol.560 , pp. 91-97
    • Van Der Veen, B.A.1    Potocki-Veronese, G.2    Albenne, C.3    Joucla, G.4    Monsan, P.5    Remaud-Simeon, M.6
  • 20
    • 41949099441 scopus 로고    scopus 로고
    • Structural analysis of the alpha-D-glucan (EPS35-5) produced by the Lactobacillus reuteri strain 35-5 glucansucrase GTFA enzyme
    • van Leeuwen SS, Kralj S, van Geel-Schutten IH, Gerwig GJ, Dijkhuizen L Kamerling JP (2008) Structural analysis of the alpha-D-glucan (EPS35-5) produced by the Lactobacillus reuteri strain 35-5 glucansucrase GTFA enzyme. Carbohydr Res 343, 1251 1265.
    • (2008) Carbohydr Res , vol.343 , pp. 1251-1265
    • Van Leeuwen, S.S.1    Kralj, S.2    Van Geel-Schutten, I.H.3    Gerwig, G.J.4    Dijkhuizen, L.5    Kamerling, J.P.6
  • 22
    • 34447132905 scopus 로고    scopus 로고
    • Three-way stabilization of the covalent intermediate in amylomaltase, an alpha-amylase-like transglycosylase
    • Barends TR, Bultema JB, Kaper T, van der Maarel MJ, Dijkhuizen L Dijkstra BW (2007) Three-way stabilization of the covalent intermediate in amylomaltase, an alpha-amylase-like transglycosylase. J Biol Chem 282, 17242 17249.
    • (2007) J Biol Chem , vol.282 , pp. 17242-17249
    • Barends, T.R.1    Bultema, J.B.2    Kaper, T.3    Van Der Maarel, M.J.4    Dijkhuizen, L.5    Dijkstra, B.W.6
  • 23
    • 0038070162 scopus 로고    scopus 로고
    • Conversion of cyclodextrin glycosyltransferase into a starch hydrolase by directed evolution: The role of alanine 230 in acceptor subsite +1
    • Leemhuis H, Rozeboom HJ, Wilbrink M, Euverink GJ, Dijkstra BW Dijkhuizen L (2003) Conversion of cyclodextrin glycosyltransferase into a starch hydrolase by directed evolution: the role of alanine 230 in acceptor subsite +1. Biochemistry 42, 7518 7526.
    • (2003) Biochemistry , vol.42 , pp. 7518-7526
    • Leemhuis, H.1    Rozeboom, H.J.2    Wilbrink, M.3    Euverink, G.J.4    Dijkstra, B.W.5    Dijkhuizen, L.6
  • 24
    • 34848871965 scopus 로고    scopus 로고
    • Conversion of a cyclodextrin glucanotransferase into an alpha-amylase: Assessment of directed evolution strategies
    • Kelly RM, Leemhuis H Dijkhuizen L (2007) Conversion of a cyclodextrin glucanotransferase into an alpha-amylase: assessment of directed evolution strategies. Biochemistry 46, 11216 11222.
    • (2007) Biochemistry , vol.46 , pp. 11216-11222
    • Kelly, R.M.1    Leemhuis, H.2    Dijkhuizen, L.3
  • 25
    • 0037070608 scopus 로고    scopus 로고
    • Mutations converting cyclodextrin glycosyltransferase from a transglycosylase into a starch hydrolase
    • Leemhuis H, Dijkstra BW Dijkhuizen L (2002) Mutations converting cyclodextrin glycosyltransferase from a transglycosylase into a starch hydrolase. FEBS Lett 514, 189 192.
    • (2002) FEBS Lett , vol.514 , pp. 189-192
    • Leemhuis, H.1    Dijkstra, B.W.2    Dijkhuizen, L.3
  • 29
    • 9144265007 scopus 로고    scopus 로고
    • Glucan synthesis in the genus Lactobacillus: Isolation and characterization of glucansucrase genes, enzymes and glucan products from six different strains
    • Kralj S, van Geel-Schutten GH, Dondorff MM, Kirsanovs S, van der Maarel MJ Dijkhuizen L (2004) Glucan synthesis in the genus Lactobacillus: isolation and characterization of glucansucrase genes, enzymes and glucan products from six different strains. Microbiology 150, 3681 3690.
    • (2004) Microbiology , vol.150 , pp. 3681-3690
    • Kralj, S.1    Van Geel-Schutten, G.H.2    Dondorff, M.M.3    Kirsanovs, S.4    Van Der Maarel, M.J.5    Dijkhuizen, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.