메뉴 건너뛰기




Volumn 190, Issue 9, 2008, Pages 3362-3373

The sim operon facilitates the transport and metabolism of sucrose isomers in Lactobacillus casei ATCC 334

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GLUCOSIDASE; DISACCHARIDE; GLUCOSE; MALTOSE; MESSENGER RNA; METAL ION; NICOTINAMIDE ADENINE DINUCLEOTIDE; OLIGOMER; PHOSPHO ALPHA GLUCOSIDASE; PHOSPHOENOLPYRUVATE; PHOSPHOTRANSFERASE; POLYPEPTIDE; SUCROSE; UNCLASSIFIED DRUG;

EID: 42549089296     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.02008-07     Document Type: Article
Times cited : (11)

References (51)
  • 2
    • 0032947332 scopus 로고    scopus 로고
    • Lactobacillus casei 64H contains a phosphoenolpyruvate-dependent phosphotransferase system for uptake of galactose, as confirmed by analysis of ptsH and different gal mutants
    • Bettenbrock, K., U. Siebers, P. Ehrenreich, and C.-A. Alpert. 1999. Lactobacillus casei 64H contains a phosphoenolpyruvate-dependent phosphotransferase system for uptake of galactose, as confirmed by analysis of ptsH and different gal mutants. J. Bacteriol. 181:225-230.
    • (1999) J. Bacteriol , vol.181 , pp. 225-230
    • Bettenbrock, K.1    Siebers, U.2    Ehrenreich, P.3    Alpert, C.-A.4
  • 3
    • 0030808276 scopus 로고    scopus 로고
    • 6-Phospho-α-D-glucosidasc from Fusobacterium mortiferum: Cloning, expression, and assignment to family 4 of the glycosylhydrolases
    • Bouma, C. L., J. Reizer, A. Reizer, S. A. Robrish, and J. Thompson. 1997. 6-Phospho-α-D-glucosidasc from Fusobacterium 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
  • 4
    • 0024312842 scopus 로고
    • Molecular characterization of the plasmid-encoded lactose-PTS of Lactobacillus casei
    • Chassy, B. M., and C.-A. Alpert. 1989. Molecular characterization of the plasmid-encoded lactose-PTS of Lactobacillus casei. FEMS Microbiol. Rev. 63:157-165.
    • (1989) FEMS Microbiol. Rev , vol.63 , pp. 157-165
    • Chassy, B.M.1    Alpert, C.-A.2
  • 5
    • 0020570242 scopus 로고
    • Regulation of lactose-phosphoenolpyruvate dependent phosphotransferase system and β-D-phosphogalactoside galactohydrolase activities in Lactobacillus casei
    • Chassy, B. M., and J. Thompson. 1983. Regulation of lactose-phosphoenolpyruvate dependent phosphotransferase system and β-D-phosphogalactoside galactohydrolase activities in Lactobacillus casei. J. Bacteriol. 154:1195-1203.
    • (1983) J. Bacteriol , vol.154 , pp. 1195-1203
    • Chassy, B.M.1    Thompson, J.2
  • 6
    • 0020522266 scopus 로고
    • Regulation and characterization of the galactose-phosphoenolpyruvate-dependent phosphotransferase system in Lactobacillus casei
    • Chassy, B. M., and J. Thompson. 1983. Regulation and characterization of the galactose-phosphoenolpyruvate-dependent phosphotransferase system in Lactobacillus casei. J. Bacteriol. 154:1204-1214.
    • (1983) J. Bacteriol , vol.154 , pp. 1204-1214
    • Chassy, B.M.1    Thompson, J.2
  • 7
    • 33845626641 scopus 로고    scopus 로고
    • How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria
    • Deutscher, J., C. Francke, and P. W. Postma. 2006. How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. Microbiol. Mol. Biol. Rev. 70:939-1031.
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , pp. 939-1031
    • Deutscher, J.1    Francke, C.2    Postma, P.W.3
  • 8
    • 0031105265 scopus 로고    scopus 로고
    • Establishing a model to study the regulation of the lactose operon in Lactobacillus casei
    • Gosalbes, M. J., V. Monedero, C.-A Alpert, and G. Pérez- Martínez. 1997. Establishing a model to study the regulation of the lactose operon in Lactobacillus casei. FEMS Microbiol. Lett. 148:83-89.
    • (1997) FEMS Microbiol. Lett , vol.148 , pp. 83-89
    • Gosalbes, M.J.1    Monedero, V.2    Alpert, C.-A.3    Pérez- Martínez, G.4
  • 9
    • 0032987321 scopus 로고    scopus 로고
    • Elements involved in catabolite repression and substrate induction of the lactose operon in Lactobacillus casei
    • Gosalbes, M. J., V. Monedero, and G. Pérez-Martínez. 1999. Elements involved in catabolite repression and substrate induction of the lactose operon in Lactobacillus casei. J. Bacteriol. 181:3928-3934.
    • (1999) J. Bacteriol , vol.181 , pp. 3928-3934
    • Gosalbes, M.J.1    Monedero, V.2    Pérez-Martínez, G.3
  • 10
    • 0036664701 scopus 로고    scopus 로고
    • Role of sweeteners in the etiology and prevention of dental caries
    • Hamada, S. 2002. Role of sweeteners in the etiology and prevention of dental caries. Pure Appl. Chem. 74:1293-1300.
    • (2002) Pure Appl. Chem , vol.74 , pp. 1293-1300
    • Hamada, S.1
  • 11
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat, B., and A. Bairoch. 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
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat, B., and G. Davies. 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
  • 13
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reactions
    • Koshland, D. E., Jr. 1953. Stereochemistry and the mechanism of enzymatic reactions. Biol. Rev. 28:416-436.
    • (1953) Biol. Rev , vol.28 , pp. 416-436
    • Koshland Jr., D.E.1
  • 15
    • 0018612938 scopus 로고
    • Pentitol metabolism in Lactobacillus casei
    • London, J., and N. M. Chace. 1979. Pentitol metabolism in Lactobacillus casei. J. Bacteriol. 140:949-954.
    • (1979) J. Bacteriol , vol.140 , pp. 949-954
    • London, J.1    Chace, N.M.2
  • 16
    • 0020974752 scopus 로고
    • Xt1 phospho-carrier protein of the phosphoenolpyruvate-dependent xylitolphosphotransferase found in Lactobacillus casei C183
    • Xt1 phospho-carrier protein of the phosphoenolpyruvate-dependent xylitolphosphotransferase found in Lactobacillus casei C183. J. Bacteriol. 156:611-619.
    • (1983) J. Bacteriol , vol.156 , pp. 611-619
    • London, J.1    Hausman, S.Z.2
  • 17
    • 33750341148 scopus 로고    scopus 로고
    • Makarova, K., A. Slesarev, Y. Wolf, A. Sorokin, B. Mirkin, E. Koonin, A. Pavlov, N. Pavlova, V. Karamychev, N. Polouchine, V. Shakhova, I. Grigoriev, Y. Lou, D. Rohksar, S. Lucas, K. Huang, D. M. Goodstein, T. Hawkins, V. Plengvidhya, D. Welker, J. Hughes, Y. Goh, A. Benson, K. Baldwin, J.-H. Lee, I. Diaz-Muniz, B. Dosti, V. Smeianov, W. Wechter, R. Barabote, G. Lorca, E. Altermann, R. Barrangou, B. Ganesan, Y. Xie, H. Rawsthorne, D. Tamir, C. Parker, F. Breidt, J. Broadbent, R. Hutkins, D. O'Sullivan, J. Steele, G. Unlu, M. Saier, T. Klaenhammer, P. Richardson, S. Kozyavkin, B. Weimer, and D. Mills. 2006. Comparative genomics of the lactic acid bacteria. Proc. Natl. Acad. Sci. USA 103:15611-15616.
    • Makarova, K., A. Slesarev, Y. Wolf, A. Sorokin, B. Mirkin, E. Koonin, A. Pavlov, N. Pavlova, V. Karamychev, N. Polouchine, V. Shakhova, I. Grigoriev, Y. Lou, D. Rohksar, S. Lucas, K. Huang, D. M. Goodstein, T. Hawkins, V. Plengvidhya, D. Welker, J. Hughes, Y. Goh, A. Benson, K. Baldwin, J.-H. Lee, I. Diaz-Muniz, B. Dosti, V. Smeianov, W. Wechter, R. Barabote, G. Lorca, E. Altermann, R. Barrangou, B. Ganesan, Y. Xie, H. Rawsthorne, D. Tamir, C. Parker, F. Breidt, J. Broadbent, R. Hutkins, D. O'Sullivan, J. Steele, G. Unlu, M. Saier, T. Klaenhammer, P. Richardson, S. Kozyavkin, B. Weimer, and D. Mills. 2006. Comparative genomics of the lactic acid bacteria. Proc. Natl. Acad. Sci. USA 103:15611-15616.
  • 18
    • 33845779367 scopus 로고    scopus 로고
    • The phosphotransferase system of Lactobacillus casei: Regulation of carbon metabolism and connection to cold shock response
    • Monedero, V., A. Mazé, G. Boël, M. Zuniga, S. Beaufils, A. Hartke, and J. Deutscher. 2007. The phosphotransferase system of Lactobacillus casei: regulation of carbon metabolism and connection to cold shock response. J. Mol. Microbiol. Biotechnol. 12:20-32.
    • (2007) J. Mol. Microbiol. Biotechnol , vol.12 , pp. 20-32
    • Monedero, V.1    Mazé, A.2    Boël, G.3    Zuniga, M.4    Beaufils, S.5    Hartke, A.6    Deutscher, J.7
  • 19
    • 39649109260 scopus 로고    scopus 로고
    • Monedero, V., M. J. Yebra, S. Poncet, and J. Deutscher. 4 November 2007, posting date. Maltose transport in Lactobacillus casei and its regulation by inducer exclusion. Res. Microbiol. doi:10.1016/j.resmic.2007.10. 002.
    • Monedero, V., M. J. Yebra, S. Poncet, and J. Deutscher. 4 November 2007, posting date. Maltose transport in Lactobacillus casei and its regulation by inducer exclusion. Res. Microbiol. doi:10.1016/j.resmic.2007.10. 002.
  • 20
    • 0020677925 scopus 로고
    • Non-cariogenicity of the disaccharide palatinose in experimental dental caries of rats
    • Ooshima, T., A. Izumitani, S. Sobue, N. Okahashi, and S. Hamada. 1983. Non-cariogenicity of the disaccharide palatinose in experimental dental caries of rats. Infect. Immun. 39:43-49.
    • (1983) Infect. Immun , vol.39 , pp. 43-49
    • Ooshima, T.1    Izumitani, A.2    Sobue, S.3    Okahashi, N.4    Hamada, S.5
  • 21
    • 0025848293 scopus 로고
    • Trchalulose does not induce dental caries in rats infected with mutans streptococci
    • Ooshima, T., A. Izumitani, T. Minami, T. Fujiwara, Y. Nakajima, and S. Hamada. 1991. Trchalulose does not induce dental caries in rats infected with mutans streptococci. Caries Res. 25:277-282.
    • (1991) Caries Res , vol.25 , pp. 277-282
    • Ooshima, T.1    Izumitani, A.2    Minami, T.3    Fujiwara, T.4    Nakajima, Y.5    Hamada, S.6
  • 22
    • 33745819926 scopus 로고    scopus 로고
    • Genetic requirements for growth of Escherichia coli K12 on methyl-α-D-glucopyranoside and the five α-D- glucosyl-D-fructose isomers of sucrose
    • Pikis, A., S. Hess, I. Arnold, B. Erni, and J. Thompson. 2006. Genetic requirements for growth of Escherichia coli K12 on methyl-α-D-glucopyranoside and the five α-D- glucosyl-D-fructose isomers of sucrose. J. Biol. Chem. 281:17900-17908.
    • (2006) J. Biol. Chem , vol.281 , pp. 17900-17908
    • Pikis, A.1    Hess, S.2    Arnold, I.3    Erni, B.4    Thompson, J.5
  • 23
    • 0036126185 scopus 로고    scopus 로고
    • Metabolism of sucrose and its five isomers by Fusobacterium mortiferum
    • Pikis, A., S. Immel, S. A. Robrish, and J. Thompson. 2002. Metabolism of sucrose and its five isomers by Fusobacterium 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
  • 24
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria
    • Postma, P. W., J. W. Lengeler, and G. R. Jacobson. 1993. Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57:543-594.
    • (1993) Microbiol. Rev , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 29
    • 0024257073 scopus 로고
    • The phosphoenolpyruvate:sugar phosphotransferase system in gram-positive bacteria: Properties, mechanism, and regulation
    • Reizer, J., M. H. Saier, Jr., J. Deutscher, F. Grenier, J. Thompson, and W. Hengstenberg. 1988. The phosphoenolpyruvate:sugar phosphotransferase system in gram-positive bacteria: properties, mechanism, and regulation. Crit. Rev. Microbiol. 15:297-338.
    • (1988) Crit. Rev. Microbiol , vol.15 , pp. 297-338
    • Reizer, J.1    Saier Jr., M.H.2    Deutscher, J.3    Grenier, F.4    Thompson, J.5    Hengstenberg, W.6
  • 30
    • 0028177254 scopus 로고
    • Phosphoenolpyruvate-dependent maltose: Phosphotransferase activity in Fusobacterium mortiferum ATCC 25557: specificity, inducibility, and product analysis
    • Robrish, S. A., H. M. Fales, C. Gentry-Weeks, and J. Thompson. 1994. Phosphoenolpyruvate-dependent maltose: phosphotransferase activity in Fusobacterium mortiferum ATCC 25557: specificity, inducibility, and product analysis. J. Bacteriol. 176:3250-3256.
    • (1994) J. Bacteriol , vol.176 , pp. 3250-3256
    • Robrish, S.A.1    Fales, H.M.2    Gentry-Weeks, C.3    Thompson, J.4
  • 33
    • 0029002443 scopus 로고
    • Purification from Fusobacterium 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., C. R. Gentry-Weeks, N. Y. Nguyen, J. E. Folk, and S. A. Robrish. 1995. Purification from Fusobacterium 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
  • 35
    • 0037072817 scopus 로고    scopus 로고
    • β-Glucoside kinase (BglK) from Klebsiella pneumoniae: Purification, properties, and synthesis of 6-phospho-β-D-glucosides
    • Thompson, J., F. W. Lichtenthaler, S. Peters, and A. Pikis. 2002. β-Glucoside kinase (BglK) from Klebsiella pneumoniae: purification, properties, and synthesis of 6-phospho-β-D-glucosides. J. Biol. Chem. 277:34310-34321.
    • (2002) J. Biol. Chem , vol.277 , pp. 34310-34321
    • Thompson, J.1    Lichtenthaler, F.W.2    Peters, S.3    Pikis, A.4
  • 36
    • 0032538629 scopus 로고    scopus 로고
    • The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-α-glucosidase
    • Thompson, J., A. Pikis, S. B. Ruvinov, B. Henrissat, H. Yamamoto, and J. Sekiguchi. 1998. The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-α-glucosidase. 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
  • 37
    • 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., S. A. Robrish, S. Immel, F. W. Lichtenthaler, B. G. Hall, and A. Pikis. 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
  • 38
    • 0035932526 scopus 로고    scopus 로고
    • Phosphorylation and metabolism of sucrose and its five linkage-isomeric α-D-glucosyl-D-fructoses by Klebsiella pneumoniae
    • Thompson, J., S. A. Robrish, A. Pikis, A. Brust, and F. W. Lichtenthaler. 2001. Phosphorylation and metabolism of sucrose and its five linkage-isomeric α-D-glucosyl-D-fructoses by Klebsiella pneumoniae. Carbohydr. Res. 331:149-161.
    • (2001) Carbohydr. Res , vol.331 , pp. 149-161
    • Thompson, J.1    Robrish, S.A.2    Pikis, A.3    Brust, A.4    Lichtenthaler, F.W.5
  • 39
    • 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., S. B. Ruvinov, D. I. Freedberg, and B. G. Hall. 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
  • 41
    • 0028307380 scopus 로고
    • Glucose transport by the phosphoenolpyruvate:mannose phosphotransferase system in Lactobacillus casei ATCC 393 and its role in carbon catabolite repression
    • Veyrat, A., V. Monedero, and G. Pérez-Martinez. 1994. Glucose transport by the phosphoenolpyruvate:mannose phosphotransferase system in Lactobacillus casei ATCC 393 and its role in carbon catabolite repression. Microbiology 140:1141-1149.
    • (1994) Microbiology , vol.140 , pp. 1141-1149
    • Veyrat, A.1    Monedero, V.2    Pérez-Martinez, G.3
  • 42
    • 0034100838 scopus 로고    scopus 로고
    • Enzyme I and HPr from Lactobacillus casei: Their role in sugar transport, carbon catabolite repression and inducer exclusion
    • Viana, R., V. Monedero, V. Dossonnet, C. Vadeboncoeur, G. Pérez-Martíez, and J. Deutscher. 2000, Enzyme I and HPr from Lactobacillus casei: their role in sugar transport, carbon catabolite repression and inducer exclusion. Mol. Microbiol. 36:570-584.
    • (2000) Mol. Microbiol , vol.36 , pp. 570-584
    • Viana, R.1    Monedero, V.2    Dossonnet, V.3    Vadeboncoeur, C.4    Pérez-Martíez, G.5    Deutscher, J.6
  • 43
    • 0016285069 scopus 로고
    • The β-glucoside system of Escherichia coli. IV. Purification and properties of phospho-β- glucosidases A and B
    • Wilson, G., and C. F. Fox. 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
  • 44
    • 0027332856 scopus 로고
    • 6-Phospho-β-galactosidases of Gram-positive and 6-phospho-β- glucosidase B of Gram-negative bacteria: Comparison of structure and function by kinetic and immunological methods and mutagenesis of the lacG gene of Staphylococcus aureus
    • Witt, E., R. Frank, and W. Hengstenberg. 1993. 6-Phospho-β-galactosidases of Gram-positive and 6-phospho-β- glucosidase B of Gram-negative bacteria: comparison of structure and function by kinetic and immunological methods and mutagenesis of the lacG gene of Staphylococcus aureus. Protein Eng. 6:913-929.
    • (1993) Protein Eng , vol.6 , pp. 913-929
    • Witt, E.1    Frank, R.2    Hengstenberg, W.3
  • 45
    • 30744461594 scopus 로고    scopus 로고
    • Molecular analysis of the glucose-specific phosphoenolpyruvate:sugar phosphotransferase system from Lactobacillus casei and its links with the control of sugar metabolism
    • Yebra, M. J., V. Monedero, M. Zuniga, J. Deutscher, and G. Pérez-Martínez. 2006. Molecular analysis of the glucose-specific phosphoenolpyruvate:sugar phosphotransferase system from Lactobacillus casei and its links with the control of sugar metabolism. Microbiology 152:95-104.
    • (2006) Microbiology , vol.152 , pp. 95-104
    • Yebra, M.J.1    Monedero, V.2    Zuniga, M.3    Deutscher, J.4    Pérez-Martínez, G.5
  • 46
    • 0033986867 scopus 로고    scopus 로고
    • Genetics of L-sorbose transport and metabolism in Lactobacillus casei
    • Yebra, M. J., A. Veyrat, M. A. Santos, and G. Pérez- Martínez. 2000. Genetics of L-sorbose transport and metabolism in Lactobacillus casei. J. Bacteriol. 182:155-163.
    • (2000) J. Bacteriol , vol.182 , pp. 155-163
    • Yebra, M.J.1    Veyrat, A.2    Santos, M.A.3    Pérez- Martínez, G.4
  • 47
    • 34548287921 scopus 로고    scopus 로고
    • Mechanism of GlvA from Bacillus subtilis: A detailed kinetic analysis of a 6-phospho-α-glucosidase from glycoside hydrolase family 4
    • Yip, V. L. Y., J. Thompson, and S. G. Withers. 2007. Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-α-glucosidase from glycoside hydrolase family 4. Biochemistry 46:9840-9852.
    • (2007) Biochemistry , vol.46 , pp. 9840-9852
    • Yip, V.L.Y.1    Thompson, J.2    Withers, S.G.3
  • 48
    • 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., A. Varrot, G. J. Davies, S. S. Rajan, X. Yang, J. Thompson, W. F. Anderson, and S. G. Withers. 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.5    Thompson, J.6    Anderson, W.F.7    Withers, S.G.8
  • 49
    • 33646844667 scopus 로고    scopus 로고
    • Family 4 glycoside hydrolases are special: The first β-elimination mechanism amongst glycoside hydrolases
    • Yip, V. L. Y., and S. G. Withers. 2006. Family 4 glycoside hydrolases are special: the first β-elimination mechanism amongst glycoside hydrolases. Biocatal. Biotransform. 24:167-176.
    • (2006) Biocatal. Biotransform , vol.24 , pp. 167-176
    • Yip, V.L.Y.1    Withers, S.G.2
  • 50
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: Anatomy of a finely tuned catalyst
    • Zechel, D. L., and S. G. Withers. 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
  • 51
    • 0035644196 scopus 로고    scopus 로고
    • Dissection of nucleophilic and acid-base catalysis in glycosidases
    • Zechel, D. L., and S. G. Withers. 2001. Dissection of nucleophilic and acid-base catalysis in glycosidases. Curr. Opin. Chem. Biol. 5:643-649.
    • (2001) Curr. Opin. Chem. Biol , vol.5 , pp. 643-649
    • Zechel, D.L.1    Withers, S.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.