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Volumn 402, Issue 1, 2002, Pages 24-30
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Analysis of the roles of amino acid residues in the flavoprotein tryptophan 2-monooxygenase modified by 2-oxo-3-pentynoate: Characterization of His338, Cys339, and Cys511 mutant enzymes
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Author keywords
Flavoprotein; Isotope effects; L amino acid oxidase; Mutagenesis; Oxidase; Tryptophan monooxygenase
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Indexed keywords
ACETAMIDE DERIVATIVE;
AMINO ACID;
CYSTEINE;
DEUTERIUM;
FLAVOPROTEIN;
HISTIDINE;
ISOTOPE;
METHIONINE;
MUTANT PROTEIN;
OXIDOREDUCTASE;
TRYPTOPHAN;
TRYPTOPHAN 2 MONOOXYGENASE;
UNCLASSIFIED DRUG;
ARTICLE;
CATALYSIS;
CHEMICAL MUTAGENESIS;
DECARBOXYLATION;
ENZYME ACTIVITY;
ENZYME MODIFICATION;
ENZYME STRUCTURE;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PSEUDOMONAS;
PSEUDOMONAS SAVASTANOI;
SEQUENCE HOMOLOGY;
STEADY STATE;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
CATALYSIS;
CYSTINE;
ESCHERICHIA COLI;
FATTY ACIDS, UNSATURATED;
HISTIDINE;
KINETICS;
METHIONINE;
MIXED FUNCTION OXYGENASES;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
PROTEIN CONFORMATION;
PSEUDOMONAS;
SEQUENCE ALIGNMENT;
STRUCTURE-ACTIVITY RELATIONSHIP;
TRYPTOPHAN;
PSEUDOMONAS;
PSEUDOMONAS SAVASTANOI;
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EID: 0036612879
PISSN: 00039861
EISSN: None
Source Type: Journal
DOI: 10.1016/S0003-9861(02)00063-2 Document Type: Article |
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Times cited : (9)
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References (18)
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