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Volumn 39, Issue 49, 2000, Pages 15002-15011
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An examination of the role of Asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme
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Author keywords
[No Author keywords available]
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Indexed keywords
ASPARAGINE;
ASPARTIC ACID;
GLUCOSE 6 PHOSPHATE DEHYDROGENASE;
HISTIDINE;
MUTANT PROTEIN;
NICOTINAMIDE ADENINE DINUCLEOTIDE;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;
WATER;
ARTICLE;
BINDING SITE;
CATALYSIS;
CRYSTAL STRUCTURE;
ENZYME ACTIVITY;
ENZYME BINDING;
ENZYME STRUCTURE;
HYDROGEN BOND;
IONIZATION;
KINETICS;
LEUCONOSTOC;
NONHUMAN;
PH;
PRIORITY JOURNAL;
STRUCTURE ANALYSIS;
X RAY CRYSTALLOGRAPHY;
X RAY DIFFRACTION;
ASPARTIC ACID;
CATALYTIC DOMAIN;
CRYSTALLOGRAPHY, X-RAY;
GLUCOSE-6-PHOSPHATE;
GLUCOSEPHOSPHATE DEHYDROGENASE;
GLUTAMIC ACID;
HISTIDINE;
HYDROGEN-ION CONCENTRATION;
KINETICS;
LEUCONOSTOC;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
MOVEMENT;
MUTAGENESIS, SITE-DIRECTED;
MUTATION;
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EID: 0034642245
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi0014608 Document Type: Article |
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Times cited : (48)
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References (31)
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