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Volumn 40, Issue 9, 2001, Pages 2754-2765
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The role for an invariant aspartic acid in hypoxanthine phosphoribosyltransferases is examined using saturation mutagenesis, functional analysis, and X-ray crystallography
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Author keywords
[No Author keywords available]
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Indexed keywords
ALANINE;
ASPARTIC ACID;
GLUTAMIC ACID;
GLUTAMINE;
HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE;
ARTICLE;
CATALYSIS;
CONTROLLED STUDY;
ENZYME ACTIVITY;
ENZYME KINETICS;
ENZYME STRUCTURE;
HYDROGEN BOND;
MUTAGENESIS;
PH;
PRIORITY JOURNAL;
STEADY STATE;
STRUCTURE ACTIVITY RELATION;
STRUCTURE ANALYSIS;
TRYPANOSOMA CRUZI;
X RAY CRYSTALLOGRAPHY;
ALANINE;
AMINO ACID SUBSTITUTION;
ANIMALS;
ASPARAGINE;
ASPARTIC ACID;
CRYSTALLOGRAPHY, X-RAY;
ENZYME ACTIVATION;
ESCHERICHIA COLI;
GENETIC COMPLEMENTATION TEST;
GLUTAMIC ACID;
GLUTAMINE;
HUMANS;
HYDROGEN-ION CONCENTRATION;
HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE;
KINETICS;
MUTAGENESIS, SITE-DIRECTED;
PLASMODIUM FALCIPARUM;
RECOMBINANT PROTEINS;
STRUCTURE-ACTIVITY RELATIONSHIP;
SUBSTRATE SPECIFICITY;
BACTERIA (MICROORGANISMS);
TRYPANOSOMA;
TRYPANOSOMA CRUZI;
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EID: 0035814901
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi001195q Document Type: Article |
Times cited : (25)
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References (53)
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