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Volumn 99, Issue 4, 2002, Pages 1859-1864
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Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase
a a a a a a a |
Author keywords
[No Author keywords available]
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Indexed keywords
HISTIDINOL DEHYDROGENASE;
MONOMER;
NICOTINAMIDE ADENINE DINUCLEOTIDE;
ZINC;
ARTICLE;
CATALYSIS;
COMPLEX FORMATION;
CRYSTAL STRUCTURE;
ENZYME BINDING;
ENZYME MECHANISM;
ENZYME STRUCTURE;
ENZYME SUBSTRATE;
ESCHERICHIA COLI;
GENE DUPLICATION;
MOLECULAR CLONING;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN EXPRESSION;
PROTEIN FOLDING;
PROTEIN PURIFICATION;
STRUCTURE ANALYSIS;
ALCOHOL OXIDOREDUCTASES;
AMINO ACID SEQUENCE;
BINDING SITES;
CATALYSIS;
CLONING, MOLECULAR;
DIMERIZATION;
ESCHERICHIA COLI;
HISTIDINE;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
NAD;
PROTEIN BINDING;
PROTEIN FOLDING;
PROTEIN STRUCTURE, TERTIARY;
SEQUENCE HOMOLOGY, AMINO ACID;
X-RAY DIFFRACTION;
ZINC;
ARCHAEA;
ESCHERICHIA COLI;
FUNGI;
NEGIBACTERIA;
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EID: 0037133242
PISSN: 00278424
EISSN: None
Source Type: Journal
DOI: 10.1073/pnas.022476199 Document Type: Article |
Times cited : (48)
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References (48)
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