-
1
-
-
84979146389
-
Stereochemistry and the mechanism of enzymatic reactions
-
Koshland, D.E. Jr. Stereochemistry and the mechanism of enzymatic reactions. Biol. Rev. 28, 415-436 (1953).
-
(1953)
Biol. Rev.
, vol.28
, pp. 415-436
-
-
Koshland Jr., D.E.1
-
2
-
-
11944256494
-
Catalytic mechanism of enzymic glycosyl transfer
-
Sinnott, M.L. Catalytic mechanism of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202 (1990).
-
(1990)
Chem. Rev.
, vol.90
, pp. 1171-1202
-
-
Sinnott, M.L.1
-
3
-
-
0000916620
-
The hen egg-white lysozyme molecule
-
Phillips, D.C. The hen egg-white lysozyme molecule. Proc. Natl. Acad. Sci. USA 57, 484-495 (1967).
-
(1967)
Proc. Natl. Acad. Sci. USA
, vol.57
, pp. 484-495
-
-
Phillips, D.C.1
-
4
-
-
0016304955
-
Crystal structure of 3 lysozyme-tetrasaccharide lactone complex
-
Ford, L.O., Johnson, L.N., Machin, P.A., Phillips, D.C. & Tjian. R. Crystal structure of 3 lysozyme-tetrasaccharide lactone complex. J. Mol. Biol. 88, 349-371 (1974).
-
(1974)
J. Mol. Biol.
, vol.88
, pp. 349-371
-
-
Ford, L.O.1
Johnson, L.N.2
Machin, P.A.3
Phillips, D.C.4
Tjian, R.5
-
5
-
-
0025778735
-
Lysozyme revisited: Crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D
-
Strynadka, N.C.J. & James, M.N.G. Lysozyme revisited: crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D. J. Mol. Biol. 220, 401-424 (1991).
-
(1991)
J. Mol. Biol.
, vol.220
, pp. 401-424
-
-
Strynadka, N.C.J.1
James, M.N.G.2
-
6
-
-
0027992695
-
Structural changes of active site cleft and different saccharide binding modes in human lysozyme co-crystallized with hexa-N-acetyl-chitohexaose at pH 4.0
-
Song, H., Inaka, K., Maenaka, K. & Matsushima, M. Structural changes of active site cleft and different saccharide binding modes in human lysozyme co-crystallized with hexa-N-acetyl-chitohexaose at pH 4.0. J. Mol. Biol. 244, 522-540 (1994).
-
(1994)
J. Mol. Biol.
, vol.244
, pp. 522-540
-
-
Song, H.1
Inaka, K.2
Maenaka, K.3
Matsushima, M.4
-
7
-
-
0028932655
-
Structures of partridge egg-white lysozyme with and without tri-N-acetylchitotriose inhibitor at 1.9 ̊ resolution
-
Turner, M.A. & Howell, P.L. Structures of partridge egg-white lysozyme with and without tri-N-acetylchitotriose inhibitor at 1.9 ̊ resolution. Protein Sci. 4, 442-449 (1995).
-
(1995)
Protein Sci.
, vol.4
, pp. 442-449
-
-
Turner, M.A.1
Howell, P.L.2
-
9
-
-
14644422478
-
Mechanisms of cellulases and xylanases: A detailed kinetic study of the exo-β - 1,4-glycanase from Cellulomonas fimi
-
Tull, D. & Withers, S.G. Mechanisms of cellulases and xylanases: a detailed kinetic study of the exo-β - 1,4-glycanase from Cellulomonas fimi. Biochemistry 266, 15621-15625 (1994).
-
(1994)
Biochemistry
, vol.266
, pp. 15621-15625
-
-
Tull, D.1
Withers, S.G.2
-
10
-
-
0023940907
-
2-Deoxy-2-fIuoro-D-glycosyl fluorides
-
Withers, S.G., Rupitz, K. & Street, I.P. 2-Deoxy-2-fIuoro-D-glycosyl fluorides. J. Biol. Chem. 263, 7929-7932 (1988).
-
(1988)
J. Biol. Chem.
, vol.263
, pp. 7929-7932
-
-
Withers, S.G.1
Rupitz, K.2
Street, I.P.3
-
11
-
-
0026055093
-
Glutamic acid 274 is the nucleophile in the active site of a "retaining" exoglucanase from Cellulomonas fimi
-
Tull, D. et al. Glutamic acid 274 is the nucleophile in the active site of a "retaining" exoglucanase from Cellulomonas fimi. J. Biol. Chem. 266, 15621-15625 (1991).
-
(1991)
J. Biol. Chem.
, vol.266
, pp. 15621-15625
-
-
Tull, D.1
-
12
-
-
0028943508
-
Approaches to labeling and identification of active site residues in glycosidases
-
Withers, S.G. & Aebersold, R. Approaches to labeling and identification of active site residues in glycosidases. Protein Sci. 4, 361-372 (1995).
-
(1995)
Protein Sci.
, vol.4
, pp. 361-372
-
-
Withers, S.G.1
Aebersold, R.2
-
14
-
-
0026666602
-
Binding energy and catalysis: Fluorinated and deoxygenated glycosides as mechanistic probes of Escherichia coli (lac Z) β-galactosidase
-
McCarter, J.D., Adams, M.J. & Withers, S.G. Binding energy and catalysis: Fluorinated and deoxygenated glycosides as mechanistic probes of Escherichia coli (lac Z) β-galactosidase. Biochem. J. 286, 721-727 (1992).
-
(1992)
Biochem. J.
, vol.286
, pp. 721-727
-
-
McCarter, J.D.1
Adams, M.J.2
Withers, S.G.3
-
15
-
-
0001410590
-
Identification of a covalent α-D-glucopyranosyl enzyme intermediate formed on a β-glucosidase
-
Withers, S.G. & Street, I.P. Identification of a covalent α-D-glucopyranosyl enzyme intermediate formed on a β-glucosidase. J. Am. Chem. Soc. 110, 8551-8553 (1988).
-
(1988)
J. Am. Chem. Soc.
, vol.110
, pp. 8551-8553
-
-
Withers, S.G.1
Street, I.P.2
-
16
-
-
0001463551
-
Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a "retaining" glycosidase
-
Withers, S.G. et al. Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a "retaining" glycosidase. J. Am. Chem. Soc. 112, 5887-5889 (1990).
-
(1990)
J. Am. Chem. Soc.
, vol.112
, pp. 5887-5889
-
-
Withers, S.G.1
-
17
-
-
0021266241
-
Mode of action and substrate specificities of cellulases from cloned bacterial genes
-
Gilkes, N.R., Langford, M.L., Kilburn, D.G., Miller, R.C. Jr. & Warren, R.A.J. Mode of action and substrate specificities of cellulases from cloned bacterial genes. J. Biol. Chem. 259, 10455-10459 (1984).
-
(1984)
J. Biol. Chem.
, vol.259
, pp. 10455-10459
-
-
Gilkes, N.R.1
Langford, M.L.2
Kilburn, D.G.3
Miller Jr., R.C.4
Warren, R.A.J.5
-
18
-
-
0025984332
-
Structural and functional relationships in two families of β-1,4-glycanases
-
Gilkes, N.R. et al. Structural and functional relationships in two families of β-1,4-glycanases. Eur. J. Biochem. 202, 3657-3677 (1991).
-
(1991)
Eur. J. Biochem.
, vol.202
, pp. 3657-3677
-
-
Gilkes, N.R.1
|