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Volumn 40, Issue 51, 2001, Pages 15591-15601
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Conformation of the substrate and pterin cofactor bound to human tryptophan hydroxylase. Important role of Phe313 in substrate specificity
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Author keywords
[No Author keywords available]
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Indexed keywords
RESIDUE;
CATALYSIS;
CONFORMATIONS;
HYDROXYLATION;
IRON;
MUTAGENESIS;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
SYNTHESIS (CHEMICAL);
ENZYME KINETICS;
ARGININE;
HISTIDINE;
PHENYLALANINE;
PHENYLALANINE 4 MONOOXYGENASE;
PTERIN;
SERINE;
SEROTONIN;
TRYPTOPHAN;
TRYPTOPHAN HYDROXYLASE;
ARTICLE;
CATALYSIS;
ENZYME ACTIVE SITE;
ENZYME SPECIFICITY;
HUMAN;
HYDROXYLATION;
MUTATION;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PROTEIN CONFORMATION;
PROTEIN INTERACTION;
PROTON NUCLEAR MAGNETIC RESONANCE;
BINDING SITES;
BIOPTERIN;
HUMANS;
IRON;
KINETICS;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;
PHENYLALANINE;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTONS;
RECOMBINANT PROTEINS;
SUBSTRATE SPECIFICITY;
THERMODYNAMICS;
TRYPTOPHAN;
TRYPTOPHAN HYDROXYLASE;
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EID: 0035951089
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi015722x Document Type: Article |
Times cited : (61)
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References (67)
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