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Volumn 363, Issue 3, 2002, Pages 745-752
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Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine
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Author keywords
elimination; Mutagenesis; Pyridoxal 5 phosphate; Stopped flow kinetics; Tryptophan indole lyase
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Indexed keywords
AMINO ACIDS;
BACTERIA;
CRYSTAL STRUCTURE;
ENZYMES;
HYDROGEN BONDS;
REACTION KINETICS;
REACTION SPECIFICITY;
BIOCHEMISTRY;
PHENYLALANINE;
THREONINE;
TYROSINE PHENOL LYASE;
ARTICLE;
BINDING SITE;
CITROBACTER FREUNDII;
CRYSTAL STRUCTURE;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME STRUCTURE;
ENZYME SUBSTRATE;
FLOW KINETICS;
MUTAGENICITY;
NONHUMAN;
PRIORITY JOURNAL;
REACTION ANALYSIS;
RESIDUE ANALYSIS;
X RAY CRYSTALLOGRAPHY;
AMINO ACID SEQUENCE;
BINDING SITES;
CITROBACTER FREUNDII;
ESCHERICHIA COLI;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
PHENYLALANINE;
PYRIDOXAL PHOSPHATE;
SEQUENCE ALIGNMENT;
STRUCTURE-ACTIVITY RELATIONSHIP;
THREONINE;
TYROSINE;
TYROSINE PHENOL-LYASE;
CITROBACTER;
CITROBACTER FREUNDII;
PROTEUS VULGARIS;
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EID: 0036565775
PISSN: 02646021
EISSN: None
Source Type: Journal
DOI: 10.1042/0264-6021:3630745 Document Type: Article |
Times cited : (26)
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References (33)
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