-
1
-
-
0026055308
-
A classification of glycosyl hydrolases based on amino acid sequence similarities
-
Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280 Pt 2 (1991) 309-316
-
(1991)
Biochem. J.
, vol.280
, Issue.PART 2
, pp. 309-316
-
-
Henrissat, B.1
-
2
-
-
0029997062
-
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. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. USA 93 (1996) 5674
-
(1996)
Proc. Natl. Acad. Sci. USA
, vol.93
, pp. 5674
-
-
Henrissat, B.1
Callebaut, I.2
Fabrega, S.3
Lehn, P.4
Mornon, J.P.5
Davies, G.6
-
3
-
-
0029392961
-
Families, superfamilies and subfamilies of glycosyl hydrolases
-
Henrissat B., and Romeu A. Families, superfamilies and subfamilies of glycosyl hydrolases. Biochem. J. 311 Pt 1 (1995) 350-351
-
(1995)
Biochem. J.
, vol.311
, Issue.PART 1
, pp. 350-351
-
-
Henrissat, B.1
Romeu, A.2
-
4
-
-
0024615303
-
Purification and thermostability of beta-galactosidase (lactase) from an autolytic strain of Streptococcus salivarius subsp. thermophilus
-
Chang B.S., and Mahoney R.R. Purification and thermostability of beta-galactosidase (lactase) from an autolytic strain of Streptococcus salivarius subsp. thermophilus. J. Dairy Res. 56 (1989) 117-127
-
(1989)
J. Dairy Res.
, vol.56
, pp. 117-127
-
-
Chang, B.S.1
Mahoney, R.R.2
-
5
-
-
0017247874
-
Lactose reduction of milk by fiber-entrapped beta-galactosidase. Pilot-plant experiments
-
Pastore M., and Morisi F. Lactose reduction of milk by fiber-entrapped beta-galactosidase. Pilot-plant experiments. Methods Enzymol. 44 (1976) 822-830
-
(1976)
Methods Enzymol.
, vol.44
, pp. 822-830
-
-
Pastore, M.1
Morisi, F.2
-
6
-
-
0033963529
-
Glycosidase mechanisms: anatomy of a finely tuned catalyst
-
Zechel D.L., and Withers S.G. Glycosidase mechanisms: anatomy of a finely tuned catalyst. Acc. Chem. Res. 33 (2000) 11-18
-
(2000)
Acc. Chem. Res.
, vol.33
, pp. 11-18
-
-
Zechel, D.L.1
Withers, S.G.2
-
7
-
-
0035314098
-
Mechanisms of glycosyl transferases and hydrolases
-
Withers S.G. Mechanisms of glycosyl transferases and hydrolases. Carbohyd. Polym. 44 (2001) 325-337
-
(2001)
Carbohyd. Polym.
, vol.44
, pp. 325-337
-
-
Withers, S.G.1
-
9
-
-
0035933580
-
The identification of the catalytic nucleophiles of two beta-galactosidases from glycoside hydrolase family 35
-
Blanchard J.E., Gal L., He S., Foisy J., Warren R.A., and Withers S.G. The identification of the catalytic nucleophiles of two beta-galactosidases from glycoside hydrolase family 35. Carbohyd. Res. 333 (2001) 7-17
-
(2001)
Carbohyd. Res.
, vol.333
, pp. 7-17
-
-
Blanchard, J.E.1
Gal, L.2
He, S.3
Foisy, J.4
Warren, R.A.5
Withers, S.G.6
-
10
-
-
0032545380
-
Identification of Glu-540 as the catalytic nucleophile of human beta-glucuronidase using electrospray mass spectrometry
-
Wong A.W., He S., Grubb J.H., Sly W.S., and Withers S.G. Identification of Glu-540 as the catalytic nucleophile of human beta-glucuronidase using electrospray mass spectrometry. J. Biol. Chem. 273 (1998) 34057-34062
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 34057-34062
-
-
Wong, A.W.1
He, S.2
Grubb, J.H.3
Sly, W.S.4
Withers, S.G.5
-
11
-
-
0001463551
-
Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a "retaining" glycosidase
-
Withers S.G., Warren R.A.J., Street I.P., Rupitz K., Kempton J.B., and Aebersold R. Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a "retaining" glycosidase. J. Am. Chem. Soc. 112 (1990) 5887-5889
-
(1990)
J. Am. Chem. Soc.
, vol.112
, pp. 5887-5889
-
-
Withers, S.G.1
Warren, R.A.J.2
Street, I.P.3
Rupitz, K.4
Kempton, J.B.5
Aebersold, R.6
-
12
-
-
33845546936
-
Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases
-
Shipkowski S., and Brenchley J.E. Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases. Appl. Environ. Microbiol. 72 (2006) 7730-7738
-
(2006)
Appl. Environ. Microbiol.
, vol.72
, pp. 7730-7738
-
-
Shipkowski, S.1
Brenchley, J.E.2
-
13
-
-
0036968554
-
Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose
-
Hidaka M., Fushinobu S., Ohtsu N., Motoshima H., Matsuzawa H., Shoun H., and Wakagi T. Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose. J. Mol. Biol. 322 (2002) 79-91
-
(2002)
J. Mol. Biol.
, vol.322
, pp. 79-91
-
-
Hidaka, M.1
Fushinobu, S.2
Ohtsu, N.3
Motoshima, H.4
Matsuzawa, H.5
Shoun, H.6
Wakagi, T.7
-
14
-
-
0023940907
-
2-Deoxy-2-fluoro-d-glycosyl fluorides. A new class of specific mechanism-based glycosidase inhibitors
-
Withers S.G., Rupitz K., and Street I.P. 2-Deoxy-2-fluoro-d-glycosyl fluorides. A new class of specific mechanism-based glycosidase inhibitors. J. Biol. Chem. 263 (1988) 7929-7932
-
(1988)
J. Biol. Chem.
, vol.263
, pp. 7929-7932
-
-
Withers, S.G.1
Rupitz, K.2
Street, I.P.3
-
15
-
-
0001410590
-
Identification of a covalent alpha-d-glucopyranosyl-enzyme intermediate formed on an beta-glucosidase
-
Withers S.G., and Street I.P. Identification of a covalent alpha-d-glucopyranosyl-enzyme intermediate formed on an beta-glucosidase. J. Am. Chem. Soc. 110 (1988) 8551-8553
-
(1988)
J. Am. Chem. Soc.
, vol.110
, pp. 8551-8553
-
-
Withers, S.G.1
Street, I.P.2
-
16
-
-
0036403621
-
Trapping of alpha-glycosidase intermediates
-
Mosi R.M., and Withers S.G. Trapping of alpha-glycosidase intermediates. Methods Enzymol. 354 (2002) 64-84
-
(2002)
Methods Enzymol.
, vol.354
, pp. 64-84
-
-
Mosi, R.M.1
Withers, S.G.2
-
17
-
-
0028853287
-
Identification of derivatized peptides without radiolabels: tandem mass spectrometric localization of the tagged active-site nucleophiles of two cellulases and a beta-glucosidase
-
Tull D., Miao S., Withers S.G., and Aebersold R. Identification of derivatized peptides without radiolabels: tandem mass spectrometric localization of the tagged active-site nucleophiles of two cellulases and a beta-glucosidase. Anal. Biochem. 224 (1995) 509-514
-
(1995)
Anal. Biochem.
, vol.224
, pp. 509-514
-
-
Tull, D.1
Miao, S.2
Withers, S.G.3
Aebersold, R.4
-
18
-
-
0026668499
-
Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli
-
Gebler J.C., Aebersold R., and Withers S.G. Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli. J. Biol. Chem. 267 (1992) 11126-11130
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 11126-11130
-
-
Gebler, J.C.1
Aebersold, R.2
Withers, S.G.3
-
19
-
-
34248545508
-
-
Leatherbarrow, R. (1990) 4.0 Ed. Erithacus Software Ltd., Staines, UK.
-
-
-
-
20
-
-
0026785573
-
Inactivation of a beta-glucosidase through the accumulation of a stable 2-deoxy-2-fluoro-alpha-d-glucopyranosyl-enzyme intermediate: a detailed investigation
-
Street I.P., Kempton J.B., and Withers S.G. Inactivation of a beta-glucosidase through the accumulation of a stable 2-deoxy-2-fluoro-alpha-d-glucopyranosyl-enzyme intermediate: a detailed investigation. Biochemistry 31 (1992) 9970-9978
-
(1992)
Biochemistry
, vol.31
, pp. 9970-9978
-
-
Street, I.P.1
Kempton, J.B.2
Withers, S.G.3
-
21
-
-
0028303157
-
The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas fimi is glutamic acid 127: evidence from detailed kinetic studies of mutants
-
MacLeod A.M., Lindhorst T., Withers S.G., and Warren R.A. The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas fimi is glutamic acid 127: evidence from detailed kinetic studies of mutants. Biochemistry 33 (1994) 6371-6376
-
(1994)
Biochemistry
, vol.33
, pp. 6371-6376
-
-
MacLeod, A.M.1
Lindhorst, T.2
Withers, S.G.3
Warren, R.A.4
-
22
-
-
0038546856
-
Trypanosoma cruzi trans-sialidase operates through a covalent sialyl-enzyme intermediate: tyrosine is the catalytic nucleophile
-
Watts A.G., Damager I., Amaya M.L., Buschiazzo A., Alzari P., Frasch A.C., and Withers S.G. Trypanosoma cruzi trans-sialidase operates through a covalent sialyl-enzyme intermediate: tyrosine is the catalytic nucleophile. J. Am. Chem. Soc. 125 (2003) 7532-7533
-
(2003)
J. Am. Chem. Soc.
, vol.125
, pp. 7532-7533
-
-
Watts, A.G.1
Damager, I.2
Amaya, M.L.3
Buschiazzo, A.4
Alzari, P.5
Frasch, A.C.6
Withers, S.G.7
-
23
-
-
3142761743
-
An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 beta-glycosidase from Thermotoga maritima
-
Yip V.L., Varrot A., Davies G.J., Rajan S.S., Yang X., Thompson J., Anderson W.F., and Withers S.G. An unusual mechanism of glycoside hydrolysis involving redox and elimination steps by a family 4 beta-glycosidase from Thermotoga maritima. J. Am. Chem. Soc. 126 (2004) 8354-8355
-
(2004)
J. Am. Chem. Soc.
, vol.126
, pp. 8354-8355
-
-
Yip, V.L.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
|