Single mutations outside the active site affect the substrate specificity in a β-glycosidase
Sandro Marana
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2011
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Structural Basis for the Substrate Specificity of Endo-β- N -acetylglucosaminidase F 3 † , ‡
Christopher Waddling
Biochemistry Usa, 2000
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Mutational Analysis of the Major Loop of Bacillus 1,3-1,4-beta -D-Glucan 4-Glucanohydrolases. EFFECTS ON PROTEIN STABILITY AND SUBSTRATE BINDING
Antoni Planas
Journal of Biological Chemistry, 1997
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Mutation in an hydrophobic sequence motif common to N-hydroxylating enzymes
Oliver Seth
1999
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Evolution of a new enzyme activity from the same motif fold
Ian Molineux
Molecular Microbiology, 2008
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The effect of hinge mutations on effector binding and domain rotation in Εscherichia coli D -3 -phosphoglycerate dehydrogenase
Sanghamitra Dey
The Journal of Biological Chemistry, 2007
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A comparative analysis of functional & structural impact of N171A in endo-β- N-acetylglucosaminidases through computational approach
Dr. B. V E N K A T A R A M A N ENTREPRENEUR & A BIOTECH STARTUP FROM RURAL AREA
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The Effect of Hinge Mutations on Effector Binding and Domain Rotation in Escherichia coli D-3-Phosphoglycerate Dehydrogenase
Sanghamitra Dey
Journal of Biological Chemistry, 2007
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Characterization of the interdependency between residues that bind the substrate in a β-glycosidase
Sandro Marana
Brazilian Journal of Medical and Biological Research, 2010
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Engineering the pH-optimum of activity of the GH12 family endoglucanase by site-directed mutagenesis
Gusakov Alexander, Alexander Gusakov, Tishkov Vladimir I.
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Substrate Specificity Engineering of β-Mannosidase and β-Glucosidase from Pyrococcus by Exchange of Unique Active Site Residues
Andrea Vasella
Biochemistry, 2002
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Three acidic residues are at the active site of a β-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68
Tirso Pons
Proteins: Structure, Function, and Bioinformatics, 2004
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A transitional hydrolase to glycosynthase mutant by Glu to Asp substitution at the catalytic nucleophile in a retaining glycosidase
Antoni Planas
Carbohydrate Research, 2014
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Role of Glu445 in the substrate binding of β-glucosidase
Priyadharshini Ramachandran, Manish Tiwari
Process Biochemistry, 2012
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Expanding the Substrate Scope of Enzymes: Combining Mutations Obtained by CASTing
Jerome Peyralans
Chemistry-a European Journal, 2006
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Glycosylasparaginase activity requires the alpha-carboxyl group, but not the alpha-amino group, on N(4)-(2-Acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine
Joanna J. Kaylor
Archives of biochemistry and biophysics, 2001
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Alternate-Site Enzyme Promiscuity
Manfred Reetz, Régis Mondière
Angewandte Chemie International Edition, 2007
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Characterization of active-site mutants ofSchizosaccharomyces pombephosphoglycerate mutase
Doris Duncan
European Journal of Biochemistry, 2000
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Role of Chemistry versus Substrate Binding in Recruiting Promiscuous Enzyme Functions
Sergey Malitsky
Biochemistry, 2011
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Site directed mutagenesis: a tool for enzyme mechanism dissection
Carston R Wagner
Trends in Biotechnology, 1990
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Mutational and Structural Analysis of Aglycone Specificity in Maize and Sorghum β-Glucosidases
Asim Esen
Journal of Biological Chemistry, 2003
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Structural consequences of the replacement of Glu239 by Gln in the catalytic chain ofEscherichia coli aspartate transcarbamylase
Patrice Vachette, Patrick Tauc
Journal of Molecular Biology, 1990
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Mutational Insights into the Roles of Amino Acid Residues in Ligand Binding for Two Closely Related Family 16 Carbohydrate Binding Modules
Roderick Mackie
Journal of Biological Chemistry, 2010
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How nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificity
Andrea Strazzulli
Proceedings of the National Academy of Sciences of the United States of America, 2012
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Structural Basis for the Substrate Specificity of a Bacillus 1, 3-1, 4-[beta]-Glucanase
Antoni Planas
Journal of molecular …, 2006
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Functional significance of Glu-77 and Tyr-137 within the active site of isoaspartyl dipeptidase
Frank Raushel
2005
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Identification of Candidate Active Site Residues in Lysosomal beta -Hexosaminidase A
Daniel Leclerc
Journal of Biological Chemistry, 1997
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Association of bi-functional activity in the N-terminal domain of glycogen debranching enzyme
Lee minho 67
Biochemical and Biophysical Research Communications, 2014
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INSILICO ANALYSIS OF STRUCTURAL IMPACT OF N171A IN ENDO-Β-N ACETYLGLUCOSAMINIDASES
Dr. B. V E N K A T A R A M A N ENTREPRENEUR & A BIOTECH STARTUP FROM RURAL AREA
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A Measure of the Broad Substrate Specificity of Enzymes Based on ‘Duplicate’ Catalytic Residues
Bjarni Asgeirsson
PLoS ONE, 2012
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De novo design of a trans-β-N-acetylglucosaminidase activity from a GH1 β-glycosidase by mechanism engineering
Charles Tellier
Glycobiology, 2014
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Kinetic and Structural Characterization of Mutations of Glycine 216 in a-Lytic Protease: A New Target for Engineering Substrate Specificity
David Agard
J Mol Biol, 1995
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Glycosylasparaginase Activity Requires the α-Carboxyl Group, but Not the α-Amino Group, on N4-(2-Acetamido- 2-deoxy-β--glucopyranosyl)--asparagine
Joanna J. Kaylor
Archives of Biochemistry and Biophysics, 2001
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The N-acetyl-binding pocket of N-acetylglucosaminyltransferases also accommodates a sugar analog with a chemical handle at C2
P. Qasba
Glycobiology, 2012
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Mutational Analysis of Conserved Carboxylate Residues in the Nucleotide Binding Sites of P-Glycoprotein
Michel Julien
Biochemistry, 2000
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