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Volumn 46, Issue 34, 2007, Pages 9840-9852

Mechanism of GlvA from Bacillus subtilis: A detailed kinetic analysis of a 6-phospho-α-glucosidase from glycoside hydrolase family 4

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS SUBTILIS; BOND CLEAVING; GLYCOSIDE HYDROLASE; KINETIC ANALYSIS;

EID: 34548287921     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700536p     Document Type: Article
Times cited : (49)

References (28)
  • 1
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat, B., and 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
  • 2
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat, B., and Davies, G. (1997) Structural and sequence-based classification of glycoside hydrolases, Curr. Opin. Struct. Biol. 7, 637-644.
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 3
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • Henrissat, B., Callebaut, I., Fabrega, S., Lehn, P., Mornon, J. P., and Davies, G. (1995) Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases, Proc. Natl. Acad. Sci. U.S.A. 92, 7090-7094.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.P.5    Davies, G.6
  • 4
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymic reactions
    • Koshland, D. E., Jr. (1953) Stereochemistry and the mechanism of enzymic reactions, Biol. Rev. 28, 416-436.
    • (1953) Biol. Rev , vol.28 , pp. 416-436
    • Koshland Jr., D.E.1
  • 5
    • 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
  • 6
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymatic glycosyl transfer
    • Sinnott, M. L. (1990) Catalytic mechanisms of enzymatic glycosyl transfer, Chem. Rev. 90, 1171-1202.
    • (1990) Chem. Rev , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 7
    • 0030808276 scopus 로고    scopus 로고
    • 6-Phospho-α-D-glucosidase from Fusobaderium mortiferum: Cloning, expression, and assignment to family 4 of the glycosylhydrolases
    • Bouma, C. L., Reizer, J., Reizer, A., Robrish, S. A., and Thompson, J. (1997) 6-Phospho-α-D-glucosidase from Fusobaderium mortiferum: cloning, expression, and assignment to family 4 of the glycosylhydrolases, J. Bacteriol. 179, 4129-4137.
    • (1997) J. Bacteriol , vol.179 , pp. 4129-4137
    • Bouma, C.L.1    Reizer, J.2    Reizer, A.3    Robrish, S.A.4    Thompson, J.5
  • 9
    • 0035813174 scopus 로고    scopus 로고
    • Metabolism of sucrose and its five linkage-isomeric α-D-glucosyl-D-fructoses by Klebsiella pneumoniae: Participation and properties of sucrose-6-phosphate hydrolase and phospho-α-glucosidase
    • Thompson, J., Robrish, S. A., Immel, S., Lichtenthaler, F. W., Hall, B. G., and Pikis, A. (2001) Metabolism of sucrose and its five linkage-isomeric α-D-glucosyl-D-fructoses by Klebsiella pneumoniae: participation and properties of sucrose-6-phosphate hydrolase and phospho-α-glucosidase, J. Biol. Chem. 276, 37415-37425.
    • (2001) J. Biol. Chem , vol.276 , pp. 37415-37425
    • Thompson, J.1    Robrish, S.A.2    Immel, S.3    Lichtenthaler, F.W.4    Hall, B.G.5    Pikis, A.6
  • 10
    • 0032538629 scopus 로고    scopus 로고
    • The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-α-glucosidase: Assignment to family 4 of the glycosylhydrolase superfamily
    • Thompson, J., Pikis, A., Ruvinov, S. B., Henrissat, B., Yamamoto, H., and Sekiguchi, J. (1998) The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-α-glucosidase: assignment to family 4 of the glycosylhydrolase superfamily, J. Biol. Chem. 273, 27347-27356.
    • (1998) J. Biol. Chem , vol.273 , pp. 27347-27356
    • Thompson, J.1    Pikis, A.2    Ruvinov, S.B.3    Henrissat, B.4    Yamamoto, H.5    Sekiguchi, J.6
  • 11
    • 0029002443 scopus 로고
    • Purification from Fusobaderium mortiferum ATCC 25557 of a 6-phosphoryl-O-α-D-glucopyranosyl:6- phosphoglucohydrolase that hydrolyzes maltose 6-phosphate and related phospho-α-D-glucosides
    • Thompson, J., Gentry-Weeks, C. R., Nguyen, N. Y., Folk, J. E., and Robrish, S. A. (1995) Purification from Fusobaderium mortiferum ATCC 25557 of a 6-phosphoryl-O-α-D-glucopyranosyl:6- phosphoglucohydrolase that hydrolyzes maltose 6-phosphate and related phospho-α-D-glucosides, J. Bacteriol. 177, 2505-2512.
    • (1995) J. Bacteriol , vol.177 , pp. 2505-2512
    • Thompson, J.1    Gentry-Weeks, C.R.2    Nguyen, N.Y.3    Folk, J.E.4    Robrish, S.A.5
  • 12
    • 0032726299 scopus 로고    scopus 로고
    • Cellobiose-6-phosphate hydrolase (CelF) of Escherichia coli: Characterization and assignment to the unusual family 4 of glycosylhydrolases
    • Thompson, J., Ruvinov, S. B., Freedberg, D. I., and Hall, B. G. (1999) Cellobiose-6-phosphate hydrolase (CelF) of Escherichia coli: characterization and assignment to the unusual family 4 of glycosylhydrolases, J. Bacteriol. 181, 7339-7345.
    • (1999) J. Bacteriol , vol.181 , pp. 7339-7345
    • Thompson, J.1    Ruvinov, S.B.2    Freedberg, D.I.3    Hall, B.G.4
  • 13
    • 3142761743 scopus 로고    scopus 로고
    • An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 β-glycosidase from Thermotoga maritima
    • Yip, V. L. Y., Varrot, A., Davies, G. J., Rajan, S. S., Yang, X. J., Thompson, J., Anderson, W. F., and Withers, S. G. (2004) An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 β-glycosidase from Thermotoga maritima, J. Am. Chem. Soc. 126, 8354-8355.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 8354-8355
    • Yip, V.L.Y.1    Varrot, A.2    Davies, G.J.3    Rajan, S.S.4    Yang, X.J.5    Thompson, J.6    Anderson, W.F.7    Withers, S.G.8
  • 14
    • 30744478437 scopus 로고    scopus 로고
    • Mechanistic analysis of the unusual redox-elimination sequence employed by Thermotoga maritima BglT: A 6-phospho-β-glucosidase from glycoside hydrolase family 4
    • Yip, V. L. Y., and Withers, S. G. (2006) Mechanistic analysis of the unusual redox-elimination sequence employed by Thermotoga maritima BglT: a 6-phospho-β-glucosidase from glycoside hydrolase family 4, Biochemistry 45, 571-580.
    • (2006) Biochemistry , vol.45 , pp. 571-580
    • Yip, V.L.Y.1    Withers, S.G.2
  • 17
    • 0001766231 scopus 로고
    • Oxidation of 1,2-5,6-di-O-isopropylidene-D-glucose by dimethyl sulfoxide-acetic anhydride
    • Sowa, W., and Thomas, G. H. S. (1966) Oxidation of 1,2-5,6-di-O-isopropylidene-D-glucose by dimethyl sulfoxide-acetic anhydride, Can. J. Chem. 44, 836-838.
    • (1966) Can. J. Chem , vol.44 , pp. 836-838
    • Sowa, W.1    Thomas, G.H.S.2
  • 18
    • 0001051336 scopus 로고
    • 13C N.M.R. spectrum of D-glucose-3-d. bond-polarization differences between the anomers of D-glucose
    • 13C N.M.R. spectrum of D-glucose-3-d. bond-polarization differences between the anomers of D-glucose, Carbohydr. Res. 15, 403-410.
    • (1970) Carbohydr. Res , vol.15 , pp. 403-410
    • Koch, H.J.1    Perlin, A.S.2
  • 19
    • 0141677298 scopus 로고
    • Studies in the stannic chloride catalysed glycosidation of phenols
    • Audichya, T. D., Ingle, T. R., and Bose, J. L. (1971) Studies in the stannic chloride catalysed glycosidation of phenols, Indian J. Chem. 9, 315-317.
    • (1971) Indian J. Chem , vol.9 , pp. 315-317
    • Audichya, T.D.1    Ingle, T.R.2    Bose, J.L.3
  • 20
    • 0242675935 scopus 로고    scopus 로고
    • Detailed dissection of a new mechanism for glycoside cleavage: α-1,4-glucan lyase
    • Lee, S. S., Yu, S., and Withers, S. G. (2003) Detailed dissection of a new mechanism for glycoside cleavage: α-1,4-glucan lyase, Biochemistry 42, 13081-13090.
    • (2003) Biochemistry , vol.42 , pp. 13081-13090
    • Lee, S.S.1    Yu, S.2    Withers, S.G.3
  • 22
    • 0015621418 scopus 로고
    • Mechanism of action of β-galactosidase: Effect of aglycone nature and α-deuterium substitution on hydrolysis of aryl galactosides
    • Sinnott, M. L., and Souchard, I. J. L. (1973) Mechanism of action of β-galactosidase: effect of aglycone nature and α-deuterium substitution on hydrolysis of aryl galactosides, Biochem. J. 133, 89-98.
    • (1973) Biochem. J , vol.133 , pp. 89-98
    • Sinnott, M.L.1    Souchard, I.J.L.2
  • 23
    • 0016285069 scopus 로고
    • The β-glucoside system of Escherichia coli. IV. Purification and properties of phospho-β- glucosidases A and B
    • Wilson, G., and Fox, C. F. (1974) The β-glucoside system of Escherichia coli. IV. Purification and properties of phospho-β- glucosidases A and B, J. Biol. Chem. 249, 5586-5598.
    • (1974) J. Biol. Chem , vol.249 , pp. 5586-5598
    • Wilson, G.1    Fox, C.F.2
  • 24
    • 0001434409 scopus 로고
    • Phosphate migration in some phosphate monoesters and diesters of methyl α-D-mannopyranoside
    • Cawley, T. N., and Letters, R. (1971) Phosphate migration in some phosphate monoesters and diesters of methyl α-D-mannopyranoside, Carbohydr. Res. 19, 373-382.
    • (1971) Carbohydr. Res , vol.19 , pp. 373-382
    • Cawley, T.N.1    Letters, R.2
  • 25
    • 0034716940 scopus 로고    scopus 로고
    • Hydrogen bonding and catalysis: A novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase
    • Joshi, M. D., Sidhu, G., Pot, I., Brayer, G. D., Withers, S. G., and Mcintosh, L. P. (2000) Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase, J. Mol. Biol. 299, 255-279.
    • (2000) J. Mol. Biol , vol.299 , pp. 255-279
    • Joshi, M.D.1    Sidhu, G.2    Pot, I.3    Brayer, G.D.4    Withers, S.G.5    Mcintosh, L.P.6
  • 26
    • 0026803010 scopus 로고
    • Mechanism of Agrobacterium β-glucosidase: Kinetic studies
    • Kempton, J. B., and Withers, S. G. (1992) Mechanism of Agrobacterium β-glucosidase: kinetic studies, Biochemistry 31, 9961-9969.
    • (1992) Biochemistry , vol.31 , pp. 9961-9969
    • Kempton, J.B.1    Withers, S.G.2
  • 27
    • 0036126185 scopus 로고    scopus 로고
    • Metabolism of sucrose and its five isomers by Fusobaderium mortiferum
    • Pikis, A., Immel, S., Robrish, S. A., and Thompson, J. (2002) Metabolism of sucrose and its five isomers by Fusobaderium mortiferum, Microbiology 148, 843-852.
    • (2002) Microbiology , vol.148 , pp. 843-852
    • Pikis, A.1    Immel, S.2    Robrish, S.A.3    Thompson, J.4


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