-
1
-
-
0028607322
-
12 structures for a reducing hexasaccharide: The Isomer Barrier to development of single-method saccharide sequencing or synthesis systems
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12 structures for a reducing hexasaccharide: the Isomer Barrier to development of single-method saccharide sequencing or synthesis systems. Glycobiology. 4:1994;759-767.
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(1994)
Glycobiology
, vol.4
, pp. 759-767
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Laine, R.A.1
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2
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0030272169
-
Design and synthesis of carbohydrate-based inhibitors of protein - carbohydrate interactions
-
A review of the computer-aided design and organic synthesis of therapeutic agents based upon protein - carbohydrate interactions. This review covers not just glycoside hydrolases but also inhibitors of other carbohydrate-metabolising enzymes and of the protein - carbohydrate interactions involved in leucocyte recognition. One of the neuraminidase inhibitors (4-deoxy-4-guanadino-Neu5Ac2en), designed on the basis of the 3D structure of the influenza virus sialidase, shows great potential as an anti-influenza drug. of special interest
-
Von Itzstein M, Colman P. Design and synthesis of carbohydrate-based inhibitors of protein - carbohydrate interactions. Curr Opin Struct Biol. 6:1996;703-709 A review of the computer-aided design and organic synthesis of therapeutic agents based upon protein - carbohydrate interactions. This review covers not just glycoside hydrolases but also inhibitors of other carbohydrate-metabolising enzymes and of the protein - carbohydrate interactions involved in leucocyte recognition. One of the neuraminidase inhibitors (4-deoxy-4-guanadino-Neu5Ac2en), designed on the basis of the 3D structure of the influenza virus sialidase, shows great potential as an anti-influenza drug. of special interest.
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(1996)
Curr Opin Struct Biol
, vol.6
, pp. 703-709
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-
Von Itzstein, M.1
Colman, P.2
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3
-
-
0030444832
-
Sialidases: Structures, biological significance and therapeutic potential
-
Sialidases are the glycoside hydrolases that catalyse the removal of sialic acid from glycoconjugates. This review, which is highly complementary to the preceding paper [2], covers their structures, biological occurrence and the potential for sialidase inhibitors in medicine. of special interest
-
Taylor G. Sialidases: structures, biological significance and therapeutic potential. Curr Opin Struct Biol. 6:1996;830-837 Sialidases are the glycoside hydrolases that catalyse the removal of sialic acid from glycoconjugates. This review, which is highly complementary to the preceding paper [2], covers their structures, biological occurrence and the potential for sialidase inhibitors in medicine. of special interest.
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(1996)
Curr Opin Struct Biol
, vol.6
, pp. 830-837
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Taylor, G.1
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4
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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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(1995)
Protein Sci
, vol.4
, pp. 361-372
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Withers, S.G.1
Aebersold, R.2
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5
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-
0029666454
-
13C-NMR study of Bacillus circulans xylanase
-
a of the catalytic acid/base, allowing it to function as Brønsted base for enzymatic deglycosylation. of outstanding interest
-
a of the catalytic acid/base, allowing it to function as Brønsted base for enzymatic deglycosylation. 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
-
6
-
-
0028303157
-
The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas fimi is glutamic acid 127: Evidence from detailed kinetic studies of mutants
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MacLeod AM, Lindhorst T, Withers SG, Warren RAJ. 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.
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Biochemistry
, vol.33
, pp. 6371-6376
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MacLeod, A.M.1
Lindhorst, T.2
Withers, S.G.3
Warren, R.A.J.4
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7
-
-
0028971418
-
Mechanism of Agrobacterium β-glucosidase: Kinetic analysis of the role of noncovalent enzyme/substrate interactions
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Namchuk MN, Withers SG. Mechanism of Agrobacterium β-glucosidase: kinetic analysis of the role of noncovalent enzyme/substrate interactions. Biochemistry. 34:1995;16194-16202.
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(1995)
Biochemistry
, vol.34
, pp. 16194-16202
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Namchuk, M.N.1
Withers, S.G.2
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8
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0026055308
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A classification of glycosyl hydrolases based on amino acid sequence similarities
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Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J. 280:1991;309-316.
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(1991)
Biochem J
, vol.280
, pp. 309-316
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Henrissat, B.1
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9
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0027225980
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New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
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Henrissat B, Bairoch A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J. 293:1993;781-788.
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(1993)
Biochem J
, vol.293
, pp. 781-788
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Henrissat, B.1
Bairoch, A.2
-
10
-
-
0029929874
-
Updating the sequence-based classification of glycosyl hydrolases
-
The latest paper in the sequence classification trilogy of glycosyl hydrolases. These three papers [8,9,10] present the rationale and details of the classification of glycoside hydrolases based on amino acid sequence similarities. In this paper, almost 60 families are described, together with details of the 'clan' grouping of structurally related families. The sequence classification has been implemented on the web at URL: http//www.expasy.ch/cgi-bin/list?glycosid.text. of special interest
-
Henrissat B, Bairoch A. Updating the sequence-based classification of glycosyl hydrolases. Biochem J. 316:1996;695-696 The latest paper in the sequence classification trilogy of glycosyl hydrolases. These three papers [8,9,10] present the rationale and details of the classification of glycoside hydrolases based on amino acid sequence similarities. In this paper, almost 60 families are described, together with details of the 'clan' grouping of structurally related families. The sequence classification has been implemented on the web at URL: http//www.expasy.ch/cgi-bin/list?glycosid.text. of special interest.
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(1996)
Biochem J
, vol.316
, pp. 695-696
-
-
Henrissat, B.1
Bairoch, A.2
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11
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0029645404
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Structures and mechanisms of glycosyl hydrolases
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Davies G, Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure. 3:1995;853-859.
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(1995)
Structure
, vol.3
, pp. 853-859
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Davies, G.1
Henrissat, B.2
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13
-
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0027740009
-
Structural features of the catalytic α/β-barrel domain predicted in starch and glycogen-debranching enzymes
-
Jespersen HM, MacGregor EA, Henrissat B, Sierks MR, Svensson B. Structural features of the catalytic α/β-barrel domain predicted in starch and glycogen-debranching enzymes. J Prot Chem. 12:1993;791-805.
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(1993)
J Prot Chem
, vol.12
, pp. 791-805
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-
Jespersen, H.M.1
MacGregor, E.A.2
Henrissat, B.3
Sierks, M.R.4
Svensson, B.5
-
14
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0031570331
-
The crystal structures of Sinapis alba myrosinase and of a covalent glycosyl - enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase
-
The first structure determination for an S-glycosidase. In addition to the native structure, the authors describe the trapping of the covalent glycosyl - enzyme intermediate, via the elegant synthesis and utilisation of a 2-fluorothioglucoside. This enzyme displays a striking sequence and structural similarity with an O-glycosidase from Family 1, the cyanogenic β-glucosidase from Trifolium repens. Both enzymes are involved in plant defence systems, suggesting a close evolutionary link. of outstanding interest
-
Burmeister WP, Cottaz S, Driguez H, Palmieri S, Henrissat B. The crystal structures of Sinapis alba myrosinase and of a covalent glycosyl - enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase. Structure. 5:1997;663-675 The first structure determination for an S-glycosidase. In addition to the native structure, the authors describe the trapping of the covalent glycosyl - enzyme intermediate, via the elegant synthesis and utilisation of a 2-fluorothioglucoside. This enzyme displays a striking sequence and structural similarity with an O-glycosidase from Family 1, the cyanogenic β-glucosidase from Trifolium repens. Both enzymes are involved in plant defence systems, suggesting a close evolutionary link. of outstanding interest.
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(1997)
Structure
, vol.5
, pp. 663-675
-
-
Burmeister, W.P.1
Cottaz, S.2
Driguez, H.3
Palmieri, S.4
Henrissat, B.5
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15
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84979146389
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Stereochemistry and the mechanism of enzymatic reactions
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Koshland DE. Stereochemistry and the mechanism of enzymatic reactions. Biol Rev. 28:1953;416-436.
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Biol Rev
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Koshland, D.E.1
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11944256494
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Catalytic mechanisms of enzymic glycosyl transfer
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Sinnott ML. Catalytic mechanisms of enzymic glycosyl transfer. Chem Rev. 90:1990;1171-1202.
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Chem Rev
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Sinnott, M.L.1
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18
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0031015902
-
Nomenclature for sugar-binding subsites in glycosyl hydrolases
-
Many systems for the nomenclature of sugar-binding subsites in carbohydrate-metabolising enzymes exist. In this paper, these various schemes are outlined and compared. The authors recommend that the structural biology community adopts the -n to +n subsite nomenclature that is widely used by enzymologists. Enzymatic cleavage takes place between subsites -1 and +1, with subsites labelled +1, +2 to +n towards the reducing end of the sugar and -1, -2, to -n towards the nonreducing end. The advantage of this system is that it allows the comparison both of different enzymes and different complexes of similar enzymes. The description and comparison of the subsites of the various disaccharidases, and exo or endo polysaccharidases thus becomes simple and consistent. of special interest
-
Davies GJ, Wilson KS, Henrissat B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J. 321:1997;557-559 Many systems for the nomenclature of sugar-binding subsites in carbohydrate-metabolising enzymes exist. In this paper, these various schemes are outlined and compared. The authors recommend that the structural biology community adopts the -n to +n subsite nomenclature that is widely used by enzymologists. Enzymatic cleavage takes place between subsites -1 and +1, with subsites labelled +1, +2 to +n towards the reducing end of the sugar and -1, -2, to -n towards the nonreducing end. The advantage of this system is that it allows the comparison both of different enzymes and different complexes of similar enzymes. The description and comparison of the subsites of the various disaccharidases, and exo or endo polysaccharidases thus becomes simple and consistent. of special interest.
-
(1997)
Biochem J
, vol.321
, pp. 557-559
-
-
Davies, G.J.1
Wilson, K.S.2
Henrissat, B.3
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19
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0029856409
-
Structure of the Fusarium oxysporum endoglucanase I with a non-hydrolysable substrate analogue: Substrate distortion gives rise to a pseudo-axial orientation for the leaving group
-
Sulzenbacher G, Driguez H, Henrissat B, Schülein M, Davies GJ. Structure of the Fusarium oxysporum endoglucanase I with a non-hydrolysable substrate analogue: substrate distortion gives rise to a pseudo-axial orientation for the leaving group. Biochemistry. 35:1996;15280-15287.
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(1996)
Biochemistry
, vol.35
, pp. 15280-15287
-
-
Sulzenbacher, G.1
Driguez, H.2
Henrissat, B.3
Schülein, M.4
Davies, G.J.5
-
20
-
-
0343488512
-
Structures of the endoglucanase I from Fusarium oxysporum: Native, cellobiose and 3,4-epoxybutyl β-D-cellobioside inhibited forms at 2.3 Å resolution
-
This and the preceding paper by Sulzenbacher et al. [19] describe the first endoglucanase structure from Family 7. The active site is located in a long substrate-binding groove as is typical for an endo-acting hydrolase. The corresponding cellobiohydrolase from this family, CBH I, has its substrate binding surface within a tunnel, implying a processive mechanism. The authors describe the use of a nonhydrolysable thio-oligosaccharide, which binds with a skew-boat conformation in the active site, resulting in an axial leaving-group orientation. This conformation brings catalytic benefit as it opens up the C-1 atom for nucleophilic attack, is closer to the reaction transition state and provides beneficial stereoelectronics. of special interest
-
Sulzenbacher G, Schülein M, Davies GJ. Structures of the endoglucanase I from Fusarium oxysporum: native, cellobiose and 3,4-epoxybutyl β-D-cellobioside inhibited forms at 2.3 Å resolution. Biochemistry. 36:1997;5902-5911 This and the preceding paper by Sulzenbacher et al. [19] describe the first endoglucanase structure from Family 7. The active site is located in a long substrate-binding groove as is typical for an endo-acting hydrolase. The corresponding cellobiohydrolase from this family, CBH I, has its substrate binding surface within a tunnel, implying a processive mechanism. The authors describe the use of a nonhydrolysable thio-oligosaccharide, which binds with a skew-boat conformation in the active site, resulting in an axial leaving-group orientation. This conformation brings catalytic benefit as it opens up the C-1 atom for nucleophilic attack, is closer to the reaction transition state and provides beneficial stereoelectronics. of special interest.
-
(1997)
Biochemistry
, vol.36
, pp. 5902-5911
-
-
Sulzenbacher, G.1
Schülein, M.2
Davies, G.J.3
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21
-
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0029896866
-
Characterization of CenC, an enzyme from Cellulomonas fimi with both endo- And exoglucanase activities
-
A rigorous analysis of the Family 9 cellulase CenC from Cellulomonas fimi. This enzyme displays properties indicative of both 'exo' and 'endo' activity, highlighting the problems and confusion that surround this nomenclature. The authors describe the simultaneous measurement of specific fluidity (resulting from an endo cleavage of the polymer into smaller fragments), together with reducing sugar release (more indicative of an exo mode of action). This analysis gives a quantitative measure of the degree of processivity of an enzyme and is thus much more powerful than the exo versus endo classification, which the authors show to be highly misleading. of outstanding interest
-
Tomme P, Kwan E, Gilkes NR, Kilburn DG, Warren RAJ. Characterization of CenC, an enzyme from Cellulomonas fimi with both endo- and exoglucanase activities. J Bacteriol. 178:1996;4216-4223 A rigorous analysis of the Family 9 cellulase CenC from Cellulomonas fimi. This enzyme displays properties indicative of both 'exo' and 'endo' activity, highlighting the problems and confusion that surround this nomenclature. The authors describe the simultaneous measurement of specific fluidity (resulting from an endo cleavage of the polymer into smaller fragments), together with reducing sugar release (more indicative of an exo mode of action). This analysis gives a quantitative measure of the degree of processivity of an enzyme and is thus much more powerful than the exo versus endo classification, which the authors show to be highly misleading. of outstanding interest.
-
(1996)
J Bacteriol
, vol.178
, pp. 4216-4223
-
-
Tomme, P.1
Kwan, E.2
Gilkes, N.R.3
Kilburn, D.G.4
Warren, R.A.J.5
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22
-
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0026734152
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Stereoselective hydrolysis catalyzed by related β-1,4-glucanases and β-1,4 xylanases
-
Gebler J, Gilkes NR, Claeyssens M, Wilson DN, Béguin P, Wakarchuk WW, Kilburn DG, Miller RC Jr, Warren RAJ, Withers SG. Stereoselective hydrolysis catalyzed by related β-1,4-glucanases and β-1,4 xylanases. J Biol Chem. 267:1992;12559-12561.
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J Biol Chem
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, pp. 12559-12561
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Gebler, J.1
Gilkes, N.R.2
Claeyssens, M.3
Wilson, D.N.4
Béguin, P.5
Wakarchuk, W.W.6
Kilburn, D.G.7
Miller R.C., Jr.8
Warren, R.A.J.9
Withers, S.G.10
-
23
-
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0030272829
-
Modern developments in molecular replacement
-
A review of the most recent developments in structure solution using molecular replacement. Of particular interest to those working on glycoside hydrolases is the review of current computer programs and methodologies for molecular replacement, plus the descriptions of molecular replacement utilising search models with low sequence similarity to the target structure. As more and more structural representatives from the glycoside hydrolase families become known, molecular replacement utilising the family-derived information is likely to become an important research tool. of special interest
-
Turkenburg JP, Dodson EJ. Modern developments in molecular replacement. Curr Opin Struct Biol. 6:1996;604-610 A review of the most recent developments in structure solution using molecular replacement. Of particular interest to those working on glycoside hydrolases is the review of current computer programs and methodologies for molecular replacement, plus the descriptions of molecular replacement utilising search models with low sequence similarity to the target structure. As more and more structural representatives from the glycoside hydrolase families become known, molecular replacement utilising the family-derived information is likely to become an important research tool. of special interest.
-
(1996)
Curr Opin Struct Biol
, vol.6
, pp. 604-610
-
-
Turkenburg, J.P.1
Dodson, E.J.2
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24
-
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0029940470
-
Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease
-
8 domain which displays sequence similarity to the catalytic domain of the Family 20 human hexosaminidases. Inherited genetic defects in the human hexosaminidases are responsible for a number of disease conditions. The authors have been able to utilise this structure and the sequence relationships within this family to define the structural basis of the pathogenic mutations that underlie Tay - Sachs and Sandhoff diseases. In addition, the chitobiose complex of this structure presents strong evidence in favour of anchimeric (substrate-assisted) catalysis by retaining N-acetyl-glucosamine hydrolases. of outstanding interest
-
8 domain which displays sequence similarity to the catalytic domain of the Family 20 human hexosaminidases. Inherited genetic defects in the human hexosaminidases are responsible for a number of disease conditions. The authors have been able to utilise this structure and the sequence relationships within this family to define the structural basis of the pathogenic mutations that underlie Tay - Sachs and Sandhoff diseases. In addition, the chitobiose complex of this structure presents strong evidence in favour of anchimeric (substrate-assisted) catalysis by retaining N-acetyl-glucosamine hydrolases. of outstanding interest.
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(1996)
Nat Struct Biol
, vol.3
, pp. 638-648
-
-
Tews, I.1
Perrakis, A.2
Oppenheim, A.3
Dauter, Z.4
Wilson, K.S.5
Vorgias, C.E.6
-
26
-
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0028956984
-
β-glucosidase, β-galactosidase, family A cellulases. Family F xylanases and two barley glucanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxy-terminal ends of β-strands four and seven
-
Jenkins J, Leggio LL, Harris G, Pickersgill R. β-glucosidase, β-galactosidase, family A cellulases. Family F xylanases and two barley glucanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxy-terminal ends of β-strands four and seven. FEBS Lett. 362:1995;281-285.
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FEBS Lett
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, pp. 281-285
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Jenkins, J.1
Leggio, L.L.2
Harris, G.3
Pickersgill, R.4
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27
-
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0029166485
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Conserved catalytic machinary and the prediction of a common fold for several families of glycosyl hydrolases
-
Henrissat B, Callebaud I, Fabrega S, Lehn P, Mornon J-P, Davies G. Conserved catalytic machinary and the prediction of a common fold for several families of glycosyl hydrolases. Proc Natl Acad Sci USA. 92:1995;7090-7094.
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Proc Natl Acad Sci USA
, vol.92
, pp. 7090-7094
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Henrissat, B.1
Callebaud, I.2
Fabrega, S.3
Lehn, P.4
Mornon, J.-P.5
Davies, G.6
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28
-
-
85044683051
-
A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino-acid similarities
-
Amino acid sequences for approximately 550 nucleotide-diphospho hexosyl-transferases are compared and analysed. They represent 38 different EC entries of the type EC 2.4.1.x and may be classified into 26 families. Related sequences appear to display the same reaction stereochemistry. This work represents the beginnings of a classification of glycosyltransferases which is similar to the glycoside hydrolase classification reviewed here. of outstanding interest
-
Campbell JA, Davies GJ, Bulone V, Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino-acid similarities. Biochem J. 1997; Amino acid sequences for approximately 550 nucleotide-diphospho hexosyl-transferases are compared and analysed. They represent 38 different EC entries of the type EC 2.4.1.x and may be classified into 26 families. Related sequences appear to display the same reaction stereochemistry. This work represents the beginnings of a classification of glycosyltransferases which is similar to the glycoside hydrolase classification reviewed here. of outstanding interest.
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(1997)
Biochem J
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Campbell, J.A.1
Davies, G.J.2
Bulone, V.3
Henrissat, B.4
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29
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0028268204
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Structural similarity of plant chitinase and lysozyme from animals and phage
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Holm L, Sander C. Structural similarity of plant chitinase and lysozyme from animals and phage. FEBS Lett. 340:1994;129-132.
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FEBS Lett
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, pp. 129-132
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Holm, L.1
Sander, C.2
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30
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0030032332
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Chitinases, chitosanases and lysozymes can be divided into procaryotic and eukaryotic families sharing a conserved core
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Monzingo AF, Marcotte EM, Hart PJ, Robertus JD. Chitinases, chitosanases and lysozymes can be divided into procaryotic and eukaryotic families sharing a conserved core. Nat Struct Biol. 3:1996;133-140.
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Nat Struct Biol
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Monzingo, A.F.1
Marcotte, E.M.2
Hart, P.J.3
Robertus, J.D.4
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32
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0029878731
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Structure of human β-glucuronidase reveals candidate lysosomal targeting and active-site motifs
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Jain S, Drendel WB, Chen Z-W, Matthews FS, Sly WS, Grubb JH. Structure of human β-glucuronidase reveals candidate lysosomal targeting and active-site motifs. Nat Struct Biol. 3:1996;375-381.
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Nat Struct Biol
, vol.3
, pp. 375-381
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Jain, S.1
Drendel, W.B.2
Chen, Z.-W.3
Matthews, F.S.4
Sly, W.S.5
Grubb, J.H.6
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33
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0029740205
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Crystal structure of thermostable Family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose
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Sakon J, Adney WS, Himmel ME, Thomas SR, Karplus PA. Crystal structure of thermostable Family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose. Biochemistry. 35:1996;10648-10660.
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Biochemistry
, vol.35
, pp. 10648-10660
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Sakon, J.1
Adney, W.S.2
Himmel, M.E.3
Thomas, S.R.4
Karplus, P.A.5
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34
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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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J Mol Biol
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Dominguez, R.1
Souchon, H.2
Lascombe, M.-B.3
Alzari, P.M.4
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35
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9444254083
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The active site of Trichoderma reesei cellobiohydrolase II: The role of tyrosine 169
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Koivula A, Reinikainen T, Ruohonen L, Valkeajärvi A, Claeyssens M, Teleman O, Kleywegt GJ, Szardenings M, Ruovinen J, Jones TA, Teeri TT. The active site of Trichoderma reesei cellobiohydrolase II: the role of tyrosine 169. Protein Eng. 9:1996;691-699.
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Protein Eng
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Koivula, A.1
Reinikainen, T.2
Ruohonen, L.3
Valkeajärvi, A.4
Claeyssens, M.5
Teleman, O.6
Kleywegt, G.J.7
Szardenings, M.8
Ruovinen, J.9
Jones, T.A.10
Teeri, T.T.11
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36
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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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J Mol Biol
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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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37
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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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Alzari PM, Souchon H, Dominguez R. The crystal structure of endoglucanase CelA, a Family 8 glycosyl hydrolase from Clostridium thermocellum. Structure. 4:1996;265-275.
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Structure
, vol.4
, pp. 265-275
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Alzari, P.M.1
Souchon, H.2
Dominguez, R.3
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38
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The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: A right-handed parallel β helix
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The first structure determination for a glycoside hydrolase from Family 28. The protein adopts the parallel β-helix fold. The potential active-site region is located in a groove perpendicular to the β-helical axis. The parallel β-helix fold is also found in the pectate lyase family of enzymes, which cleave similar substrates but via a totally different enzyme mechanism utilising a β-elimination. The fold, mechanism and substrate specificity are similar to the unclassified rhamnosidase from the phage P22 tailspike [61], suggesting that these enzymes may be classified as a clan once confirmation of the respective catalytic residues and, in the case of the P22 protein, stereochemistry are resolved. of outstanding interest
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Petersen TN, Kauppinen S, Larsen S. The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: a right-handed parallel β helix. Structure. 5:1997;533-544 The first structure determination for a glycoside hydrolase from Family 28. The protein adopts the parallel β-helix fold. The potential active-site region is located in a groove perpendicular to the β-helical axis. The parallel β-helix fold is also found in the pectate lyase family of enzymes, which cleave similar substrates but via a totally different enzyme mechanism utilising a β-elimination. The fold, mechanism and substrate specificity are similar to the unclassified rhamnosidase from the phage P22 tailspike [61], suggesting that these enzymes may be classified as a clan once confirmation of the respective catalytic residues and, in the case of the P22 protein, stereochemistry are resolved. of outstanding interest.
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Crystallisation of the catalytic domain of Clostridium celluloyticum CelF cellulase in the presence of a newly synthesized cellulase inhibitor
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A fine example of the essential synergy between synthetic chemists and biochemists! The crystallisation of this Family 48 enzyme - the major enzymatic component of the cellulosome - is achieved via the specific synthesis and utilisation of a thio-oligosaccharide substrate analogue. of special interest
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Reverbel-Leroy C, Parsiegla G, Moreau V, Juy M, Tardif C, Driguez H, Bélaich J-P, Haser R. Crystallisation of the catalytic domain of Clostridium celluloyticum CelF cellulase in the presence of a newly synthesized cellulase inhibitor. Acta Crystallogr D. 1997; A fine example of the essential synergy between synthetic chemists and biochemists! The crystallisation of this Family 48 enzyme - the major enzymatic component of the cellulosome - is achieved via the specific synthesis and utilisation of a thio-oligosaccharide substrate analogue. of special interest.
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Phage P22 tailspike protein: Crystal structure of the head-binding domain at 2.3 Å. fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition
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The phage P22 tailspike protein is a viral adhesion molecule with both receptor-binding and hydrolytic activities. As yet, it has not been classified into a sequence family because of the absence of similar sequences. The hydrolytic activity, however, is an endorhamnosidase which has several similarities to the recently determined Family 28 rhamnogalacturonase [55]. of outstanding interest
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Steinbacher S, Miller S, Baxa U, Budisa N, Weintraub A, Seckler R, Huber R. Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 Å. fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition. J Mol Biol. 267:1997;865-880 The phage P22 tailspike protein is a viral adhesion molecule with both receptor-binding and hydrolytic activities. As yet, it has not been classified into a sequence family because of the absence of similar sequences. The hydrolytic activity, however, is an endorhamnosidase which has several similarities to the recently determined Family 28 rhamnogalacturonase [55]. of outstanding interest.
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