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Volumn 403, Issue 3, 2007, Pages 441-449

Acid-base catalysis in Leuconostoc mesenteroides sucrose phosphorylase probed by site-directed mutagenesis and detailed kinetic comparison of wild-type and Glu237 → Gln mutant enzymes

Author keywords

Br nsted catalysis; Chemical rescue; Family GH 13; Phosphorylase; pKa modulation; Retaining mechanism

Indexed keywords

ACID BASE CATALYSIS; ANIONIC NUCLEOPHILES; DEGLUCOSYLATION; GLUTAMATE; LEUCONOSTOC MESENTEROIDES; SUCROSE PHOSPHORYLASE;

EID: 34247867966     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070042     Document Type: Article
Times cited : (34)

References (17)
  • 1
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • Sinnott, M. L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202
    • (1990) Chem. Rev , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 3
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: Anatomy of a finely tuned catalyst
    • Zechel, D. L. and Withers, S. G. (2000) Glycosidase mechanisms: anatomy of a finely tuned catalyst. Acc. Chem. Res. 33, 11-18
    • (2000) Acc. Chem. Res , vol.33 , pp. 11-18
    • Zechel, D.L.1    Withers, S.G.2
  • 4
    • 77956925456 scopus 로고    scopus 로고
    • Mieyal, J. J. and Abeles, R. H. (1972) Disaccharide phosphorylases. In The Enzymes (Boyer, P. D., ed.), pp. 515-532, Academic Press, New York
    • Mieyal, J. J. and Abeles, R. H. (1972) Disaccharide phosphorylases. In The Enzymes (Boyer, P. D., ed.), pp. 515-532, Academic Press, New York
  • 5
    • 33745358234 scopus 로고    scopus 로고
    • Asp-196 → Ala mutant of Leuconostoc mesenteroides sucrose phosphorylase exhibits altered stereochemical course and kinetic mechanism of glucosyl transfer to and from phosphate
    • Schwarz, A. and Nidetzky, B. (2006) Asp-196 → Ala mutant of Leuconostoc mesenteroides sucrose phosphorylase exhibits altered stereochemical course and kinetic mechanism of glucosyl transfer to and from phosphate. FEBS Lett. 580, 3905-3910
    • (2006) FEBS Lett , vol.580 , pp. 3905-3910
    • Schwarz, A.1    Nidetzky, B.2
  • 7
    • 33845665889 scopus 로고    scopus 로고
    • Dividing the large glycoside hydrolase family 13 into subfamilies: Towards improved functional annotations of α-amylase-related proteins
    • Stam, M. R., Danchin, E. G. J., Rancurel, C., Coutinho, P. M. and 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, 555-562
    • (2006) Protein Eng. Des. Sel , vol.19 , pp. 555-562
    • Stam, M.R.1    Danchin, E.G.J.2    Rancurel, C.3    Coutinho, P.M.4    Henrissat, B.5
  • 8
    • 0028429952 scopus 로고
    • Protein engineering in the α-amylase family: Catalytic mechanism, substrate specificity, and stability
    • Svensson, B. (1994) Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol. Biol. 25, 141-157
    • (1994) Plant Mol. Biol , vol.25 , pp. 141-157
    • Svensson, B.1
  • 9
    • 0030778420 scopus 로고    scopus 로고
    • α-amylase family: Molecular biology and evolution
    • Janecek, S. (1997) α-amylase family: molecular biology and evolution. Prog. Biophys. Mol. Biol. 67, 67-97
    • (1997) Prog. Biophys. Mol. Biol , vol.67 , pp. 67-97
    • Janecek, S.1
  • 10
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the α-amylase family of enzymes
    • MacGregor, E. A., Janecek, S. and Svensson, B. (2001) Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochim. Biophys. Acta 1546, 1-20
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 1-20
    • MacGregor, E.A.1    Janecek, S.2    Svensson, B.3
  • 11
    • 0037006989 scopus 로고    scopus 로고
    • Mechanistic analyses of catalysis in human pancreatic α-amylase: Detailed kinetic and structural studies of mutants of three conserved carboxylic acids
    • Rydberg, E. H., Li, C., Maurus, R., Overall, C. M., Brayer, G. D. and Withers, S. G. (2002) Mechanistic analyses of catalysis in human pancreatic α-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids. Biochemistry 41, 4492-4502
    • (2002) Biochemistry , vol.41 , pp. 4492-4502
    • Rydberg, E.H.1    Li, C.2    Maurus, R.3    Overall, C.M.4    Brayer, G.D.5    Withers, S.G.6
  • 12
    • 17644368570 scopus 로고    scopus 로고
    • Catalytic mechanism of α-retaining glucosyl transfer by Corynebacterium callunae starch phosphorylase: The role of histidine-334 examined through kinetic characterization of site-directed mutants
    • Schwarz, A., Pierfederici, F. M. and Nidetzky, B. (2005) Catalytic mechanism of α-retaining glucosyl transfer by Corynebacterium callunae starch phosphorylase: the role of histidine-334 examined through kinetic characterization of site-directed mutants. Biochem. J. 387, 437-445
    • (2005) Biochem. J , vol.387 , pp. 437-445
    • Schwarz, A.1    Pierfederici, F.M.2    Nidetzky, B.3
  • 13
    • 0036401975 scopus 로고    scopus 로고
    • One-step stereocontrolled synthesis of α-anomeric carboxylic acid esters from unprotected glycosyl donors: A water-soluble aspirin pro-drug analogue
    • Hanessian, S., Mascitti, V., Lu, P.-P. and Ishida, H. (2002) One-step stereocontrolled synthesis of α-anomeric carboxylic acid esters from unprotected glycosyl donors: a water-soluble aspirin pro-drug analogue. Synthesis 14, 1959-1968
    • (2002) Synthesis , vol.14 , pp. 1959-1968
    • Hanessian, S.1    Mascitti, V.2    Lu, P.-P.3    Ishida, H.4
  • 14
    • 0019201530 scopus 로고
    • Formylation of glucose by cefamandole nafate at alkaline pH
    • Indelicato, J. M., Stewart, B. A. and Engel, G. L. (1980) Formylation of glucose by cefamandole nafate at alkaline pH. J. Pharm. Sci. 69, 1183-1188
    • (1980) J. Pharm. Sci , vol.69 , pp. 1183-1188
    • Indelicato, J.M.1    Stewart, B.A.2    Engel, G.L.3
  • 15
    • 2142715897 scopus 로고    scopus 로고
    • Lipase-catalysed preparation of acetates of 4-nitrophenyl β-D-xylopyranoside and their use in kinetic studies of acetyl migration
    • Mastihubova, M. and Biely, P. (2004) Lipase-catalysed preparation of acetates of 4-nitrophenyl β-D-xylopyranoside and their use in kinetic studies of acetyl migration. Carbohydr. Res. 339, 1353-1360
    • (2004) Carbohydr. Res , vol.339 , pp. 1353-1360
    • Mastihubova, M.1    Biely, P.2
  • 17
    • 33845931590 scopus 로고    scopus 로고
    • Structural rearrangements of sucrose phosphorylase from Bifidobacterium adolescentis during sucrose conversion
    • Mirza, O., Skov, L. K., Sprogøe, D., van den Broek, L. A., Beldman, G., Kastrup, J. S. and Gajhede, M. (2006) Structural rearrangements of sucrose phosphorylase from Bifidobacterium adolescentis during sucrose conversion. J. Biol. Chem. 281, 35576-35584
    • (2006) J. Biol. Chem , vol.281 , pp. 35576-35584
    • Mirza, O.1    Skov, L.K.2    Sprogøe, D.3    van den Broek, L.A.4    Beldman, G.5    Kastrup, J.S.6    Gajhede, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.