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10
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0025778735
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Lysozyme revisited: Crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D
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Strynadka NCJ, James MNG. Lysozyme revisited: crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D. J Mol Biol. 220:1991;401-424.
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Strynadka, N.C.J.1
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11
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0028020739
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Crystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product
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Hadfield AT, Harvey DJ, Archer DB, MacKenzie DA, Jeenes DJ, Radford SE, Lowe G, Dobson CM, Johnson LN. Crystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product. J Mol Biol. 243:1994;846-872.
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Hadfield, A.T.1
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Radford, S.E.6
Lowe, G.7
Dobson, C.M.8
Johnson, L.N.9
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12
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0027730754
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A covalent enzyme - substrate intermediate with saccharide distortion in a mutant T4 lysozyme
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Kuroki R, Weaver LH, Matthews BW. A covalent enzyme - substrate intermediate with saccharide distortion in a mutant T4 lysozyme. Science. 262:1993;2030-2033.
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Kuroki, R.1
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14
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0026665418
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The structure of the complex between influenza virus neuraminidase and sialic acid, the rival receptor
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Varghese JN, McKimm-Breschkin JL, Caldwell JB, Kortt AA, Colman PM. The structure of the complex between influenza virus neuraminidase and sialic acid, the rival receptor. Proteins. 14:1992;327-332.
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Varghese, J.N.1
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15
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0030011313
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Tumor marker disaccharide D-Gal-β1,3-GalNAc complexed to heat-labile enterotoxin from Escherichia coli
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Van den Akker F, Steensma E, Hol WGJ. Tumor marker disaccharide D-Gal-β1,3-GalNAc complexed to heat-labile enterotoxin from Escherichia coli. Protein Sci. 5:1996;1184-1188.
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Van Den Akker, F.1
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Hol, W.G.J.3
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17
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0030584665
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The crystal structure of endoglucanase CelA, a Family 8 glycosyl hydrolase from Clostridium thermocellum
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6 barrel folding motif and helps to better understand the evolutionary relationship between different families of β-glycosyl hydrolases. of special interest
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6 barrel folding motif and helps to better understand the evolutionary relationship between different families of β-glycosyl hydrolases. of special interest.
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Structure
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Alzari, P.M.1
Souchon, H.2
Dominguez, R.3
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18
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0029940470
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Bacterial chitobiase structure provides insights into catalytic mechanism and the basis of Tay - Sachs disease
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This crystal structure of an abortive complex of a di-N-acetyl-glucosamine bound to a chitobiase clearly shows one distorted saccharide at the binding subsite -1 in a 'twisted-boat' conformation, whereas the other sugar is in a typical chair form. The enzyme is believed to 'dock' the substrate into its active-site pocket. The proposed mechanism of catalysis involves substrate assistance by the N-acetyl substituent at C2. of outstanding interest
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Tews I, Perrakis A, Oppenheim A, Dauter Z, Wilson KS, Vorgias CE. Bacterial chitobiase structure provides insights into catalytic mechanism and the basis of Tay - Sachs disease. Nat Struct Biol. 3:1996;638-648 This crystal structure of an abortive complex of a di-N-acetyl-glucosamine bound to a chitobiase clearly shows one distorted saccharide at the binding subsite -1 in a 'twisted-boat' conformation, whereas the other sugar is in a typical chair form. The enzyme is believed to 'dock' the substrate into its active-site pocket. The proposed mechanism of catalysis involves substrate assistance by the N-acetyl substituent at C2. of outstanding interest.
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(1996)
Nat Struct Biol
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Tews, I.1
Perrakis, A.2
Oppenheim, A.3
Dauter, Z.4
Wilson, K.S.5
Vorgias, C.E.6
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19
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0028874610
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Structure of the 70 kDa soluble lytic transglycosylase complexed with bulgenin A. Implications for the enzymatic mechanism
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Thunnissen A-MWH, Rozeboom HJ, Kalk KH, Dijkstra BW. Structure of the 70 kDa soluble lytic transglycosylase complexed with bulgenin A. Implications for the enzymatic mechanism. Biochemistry. 34:1995;12729-12737.
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Thunnissen, A.-M.1
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Kalk, K.H.3
Dijkstra, B.W.4
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20
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0029856409
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Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: Substrate distortion gives rise to the preferred axial orientation for the leaving group
-
Assessing the conformation of the saccharide at the subsite -1 for retaining β-glycosyl hydrolases has always been difficult. In this paper, a nonhydrolyzable thio-oligosaccharide is successfully used with an endoglucanase I to show the deformation of the saccharide binding at subsite -1. In this crystal structure, the saccharide spans the cleavage centre of the enzyme and shows a 'twisted-boat' conformation. Hence, the scissile bond is axial to this saccharide, which may be important for catalysis. of outstanding interest
-
Sulzenbacher G, Driguez H, Henrissat B, Schülein M, Davies GJ. Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group. Biochemistry. 35:1996;15280-15287 Assessing the conformation of the saccharide at the subsite -1 for retaining β-glycosyl hydrolases has always been difficult. In this paper, a nonhydrolyzable thio-oligosaccharide is successfully used with an endoglucanase I to show the deformation of the saccharide binding at subsite -1. In this crystal structure, the saccharide spans the cleavage centre of the enzyme and shows a 'twisted-boat' conformation. Hence, the scissile bond is axial to this saccharide, which may be important for catalysis. of outstanding interest.
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(1996)
Biochemistry
, vol.35
, pp. 15280-15287
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Sulzenbacher, G.1
Driguez, H.2
Henrissat, B.3
Schülein, M.4
Davies, G.J.5
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21
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0343488512
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Structure of the endoglucanase I from Fusarium oxysporum: Native, cellobio, and 3,4-epoxybutyl β-D-cellobioside-inhibited forms, at 2.3 Å resolution
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Sulzenbacher G, Schülein M, Davies GJ. Structure of the endoglucanase I from Fusarium oxysporum: native, cellobio, and 3,4-epoxybutyl β-D-cellobioside-inhibited forms, at 2.3 Å resolution. Biochemistry. 36:1997;5902-5911.
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(1997)
Biochemistry
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Sulzenbacher, G.1
Schülein, M.2
Davies, G.J.3
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22
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0030056077
-
Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: Relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism
-
High-resolution crystal structures of the inverting enzyme glucoamylase complexed with D-gluco-dihydroacarbose and acarbose show saccharide distortion at the catalytic center toward a half-chair conformation. This study also reports an analysis of the extent of such distortion as a function of pH. of special interest
-
Aleshin AE, Stoffer B, Firsov LM, Svensson B, Honzatko RB. Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism. Biochemistry. 35:1996;8319-8328 High-resolution crystal structures of the inverting enzyme glucoamylase complexed with D-gluco-dihydroacarbose and acarbose show saccharide distortion at the catalytic center toward a half-chair conformation. This study also reports an analysis of the extent of such distortion as a function of pH. of special interest.
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(1996)
Biochemistry
, vol.35
, pp. 8319-8328
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Aleshin, A.E.1
Stoffer, B.2
Firsov, L.M.3
Svensson, B.4
Honzatko, R.B.5
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23
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0027943686
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Crystal structure of the catalytic domain of the β-1,4-glycanase Cex from Cellulomonas fimi
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White A, Withers SG, Gilkes NR, Rose DR. Crystal structure of the catalytic domain of the β-1,4-glycanase Cex from Cellulomonas fimi. Biochemistry. 33:1994;12546-12552.
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Biochemistry
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White, A.1
Withers, S.G.2
Gilkes, N.R.3
Rose, D.R.4
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24
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0029993491
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The crystal structure of a Family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism
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Dominguez R, Souchon H, Lascombe M-B, Alzari PM. The crystal structure of a Family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism. J Mol Biol. 257:1996;1042-1051.
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Dominguez, R.1
Souchon, H.2
Lascombe, M.-B.3
Alzari, P.M.4
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25
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0026803010
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Mechanism of Agrobacterium β-glucosidase: Kinetic studies
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Kempton JB, Withers SG. Mechanism of Agrobacterium β-glucosidase: kinetic studies. Biochemistry. 31:1992;9961-9969.
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Biochemistry
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Kempton, J.B.1
Withers, S.G.2
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26
-
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0029666454
-
13C-NMR study of Bacillus circulans xylanase
-
a shift is observed for the acid/base catalyst Glu78, compared with the free enzyme. This phenomenon is presumed to be a common feature for glycosidases. of outstanding interest
-
a shift is observed for the acid/base catalyst Glu78, compared with the free enzyme. This phenomenon is presumed to be a common feature for glycosidases. of outstanding interest.
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(1996)
Biochemistry
, vol.35
, pp. 9958-9966
-
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McIntosh, L.P.1
Hand, G.2
Johnson, P.E.3
Joshi, M.D.4
Körner, M.5
Plesniak, L.A.6
Ziser, L.7
Wakarchuk, W.W.8
Withers, S.G.9
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27
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0029955152
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Secondary structure and NMR assignments of Bacillus circulans xylanase
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Plesniak LA, Wakarchuk WW, McIntosh LP. Secondary structure and NMR assignments of Bacillus circulans xylanase. Protein Sci. 5:1996;1118-1135.
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Plesniak, L.A.1
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McIntosh, L.P.3
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28
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0028224697
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Mechanisms of cellulases and xylanases: A detailed kinetic study of the exo-β-1,4-glycanase from Cellulomonas fimi
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Tull D, Withers SG. Mechanisms of cellulases and xylanases: a detailed kinetic study of the exo-β-1,4-glycanase from Cellulomonas fimi. Biochemistry. 33:1994;6363-6370.
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Biochemistry
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Tull, D.1
Withers, S.G.2
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29
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0028982484
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Structure/reactivity relationships for β-galactosidase (Escherichia coli, lac Z). 1. Brønsted parameters for cleavage of alkyl β-D-galactopyranosides
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Richard JP, Westerfeld JG, Lin S. Structure/reactivity relationships for β-galactosidase (Escherichia coli, lac Z). 1. Brønsted parameters for cleavage of alkyl β-D-galactopyranosides. Biochemistry. 34:1995;11703-11712.
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Richard, J.P.1
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Lin, S.3
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30
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0029818948
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Mechanistic consequences of mutation of active site carboxylates in a retaining β-1,4-glycanase from Cellulomonas fimi
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This report presents a new method to identify the catalytic nucleophile of retaining β-glycosyl hydrolases, without the use of active-site labelling agents. Results of activity assays for enzyme mutants at conserved aspartate/glutamate positions are indicative of the possible catalytic function of the mutated residue. As a test case, results obtained with three sidechains of the β-1,4-glycanase cex-cd correlate with their expected role. This method is likely to be applicable to other retaining β-glycosyl hydrolases. of special interest
-
MacLeod AM, Tull D, Rupitz K, Warren RAJ, Withers SG. Mechanistic consequences of mutation of active site carboxylates in a retaining β-1,4-glycanase from Cellulomonas fimi. Biochemistry. 35:1996;13165-13172 This report presents a new method to identify the catalytic nucleophile of retaining β-glycosyl hydrolases, without the use of active-site labelling agents. Results of activity assays for enzyme mutants at conserved aspartate/glutamate positions are indicative of the possible catalytic function of the mutated residue. As a test case, results obtained with three sidechains of the β-1,4-glycanase cex-cd correlate with their expected role. This method is likely to be applicable to other retaining β-glycosyl hydrolases. of special interest.
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(1996)
Biochemistry
, vol.35
, pp. 13165-13172
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MacLeod, A.M.1
Tull, D.2
Rupitz, K.3
Warren, R.A.J.4
Withers, S.G.5
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31
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0023635589
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2-Deoxy-2-fluoroglucosides: A novel class of mechanism-based glucosidase inhibitors
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Withers SG, Street IP, Bird P, Dolphin DH. 2-Deoxy-2-fluoroglucosides: a novel class of mechanism-based glucosidase inhibitors. J Am Chem Soc. 109:1987;7530-7531.
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Withers, S.G.1
Street, I.P.2
Bird, P.3
Dolphin, D.H.4
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32
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0023940907
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2-Deoxy-2-fluoro-D-glycosyl fluorides. A new class of specific mechanism-based glycosidase inhibitors
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Withers SG, Rupitz K, Street IP. 2-Deoxy-2-fluoro-D-glycosyl fluorides. A new class of specific mechanism-based glycosidase inhibitors. J Biol Chem. 263:1988;7929-7932.
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Withers, S.G.1
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Street, I.P.3
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33
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0028943508
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Approaches to labeling and identification of active site residues in glycosidases
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Withers SG, Aebersold R. Approaches to labeling and identification of active site residues in glycosidases. Protein Sci. 4:1995;361-372.
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Protein Sci
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Withers, S.G.1
Aebersold, R.2
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34
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0030595119
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The 1.8 Å resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase Family 18
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Terwisscha van Scheltinga AC, Hennig M, Dijkstra BW. The 1.8 Å resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase Family 18. J Mol Biol. 262:1996;243-257.
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J Mol Biol
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, pp. 243-257
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Terwisscha Van Scheltinga, A.C.1
Hennig, M.2
Dijkstra, B.W.3
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35
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0030606294
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Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei
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Ståhlberg J, Divne C, Koivula A, Piens K, Claeyssens M, Teeri TT, Jones TA. Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei. J Mol Biol. 264:1996;337-349.
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Ståhlberg, J.1
Divne, C.2
Koivula, A.3
Piens, K.4
Claeyssens, M.5
Teeri, T.T.6
Jones, T.A.7
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36
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0029739757
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Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-xylanase II from Trichoderma reesei
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Havukainen R, Törrönen A, Laitinen T, Rouvinen J. Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-xylanase II from Trichoderma reesei. Biochemistry. 35:1996;9617-9624.
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Biochemistry
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Havukainen, R.1
Törrönen, A.2
Laitinen, T.3
Rouvinen, J.4
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37
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0001463551
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Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a 'retaining' glycosidase
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Withers SG, Warren RAJ, Street IP, Rupitz K, Kempton JB, Aabersold 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.
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Withers, S.G.1
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Street, I.P.3
Rupitz, K.4
Kempton, J.B.5
Aabersold, R.6
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38
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0030947305
-
Identification of the catalytic nucleophile of endoglucanase I from Fusarium oxysporum by mass spectrometry
-
2-fluoro-saccharides are used to inactivate endoglucanase from Fusarium oxysporum and thus to identify the catalytic nucleophile. The saccharide - enzyme complex is shown to be catalytically competent, undergoing transglycosylation with D-cellobiose. of special interest
-
Mackenzie LF, Davies GJ, Schülein M, Withers SG. Identification of the catalytic nucleophile of endoglucanase I from Fusarium oxysporum by mass spectrometry. Biochemistry. 36:1997;5893-5901 2-fluoro-saccharides are used to inactivate endoglucanase from Fusarium oxysporum and thus to identify the catalytic nucleophile. The saccharide - enzyme complex is shown to be catalytically competent, undergoing transglycosylation with D-cellobiose. of special interest.
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(1997)
Biochemistry
, vol.36
, pp. 5893-5901
-
-
Mackenzie, L.F.1
Davies, G.J.2
Schülein, M.3
Withers, S.G.4
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39
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85030300411
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β-1,4-glycanases of Cellulomonas fimi: Families, mechanisms and kinetics
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T.W. Jeffries, Viikari L. Washington: American Chemical Society. in press
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Bray MR, Creagh AL, Damude HG, Gilkes NR, Haynes CA, Jervis E, Kilburn DG, MacLeod AM, Meinke A, Miller RC Jr, et al. β-1,4-glycanases of Cellulomonas fimi: families, mechanisms and kinetics. Jeffries TW, Viikari L. Enzymes for Pulp and Paper Processing. 1997;American Chemical Society, Washington. in press.
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Enzymes for Pulp and Paper Processing
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-
Bray, M.R.1
Creagh, A.L.2
Damude, H.G.3
Gilkes, N.R.4
Haynes, C.A.5
Jervis, E.6
Kilburn, D.G.7
MacLeod, A.M.8
Meinke, A.9
Miller R.C. Jr10
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40
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-
0030052194
-
Crystallographic observation of a covalent intermediate in a β-glycosidase
-
A minimally modified slow substrate is used to observe the structural features of the catalytic intermediate in a retaining β-glycosyl hydrolase. Upon cleavage of the disaccharide substrate by the enzyme in the crystal, a reversible covalent glycosyl - enzyme complex is formed. of outstanding interest
-
White A, Tull D, Johns K, Withers SG, Rose DR. Crystallographic observation of a covalent intermediate in a β-glycosidase. Nat Struct Biol. 3:1996;149-154 A minimally modified slow substrate is used to observe the structural features of the catalytic intermediate in a retaining β-glycosyl hydrolase. Upon cleavage of the disaccharide substrate by the enzyme in the crystal, a reversible covalent glycosyl - enzyme complex is formed. of outstanding interest.
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(1996)
Nat Struct Biol
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, pp. 149-154
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White, A.1
Tull, D.2
Johns, K.3
Withers, S.G.4
Rose, D.R.5
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41
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0001410590
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Identification of a covalent α-D-glucopyranosyl enzyme intermediate formed on a β-glucosidase
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Withers SG, Street IP. Identification of a covalent α-D-glucopyranosyl enzyme intermediate formed on a β-glucosidase. J Am Chem Soc. 110:1988;8551-8553.
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Withers, S.G.1
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Post CB, Karplus M. Does lysozyme follow the lysozyme pathway? An alternative based on dynamics, structural, and stereoelectronic considerations. J Am Chem Soc. 108:1986;1317-1319.
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