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Volumn 40, Issue 45, 2001, Pages 13529-13537
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Maintenance of α-helical structures by phenyl rings in the active-site tyrosine triad contributes to catalysis and stability of ketosteroid isomerase from Pseudomonas putida biotype B
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Author keywords
[No Author keywords available]
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Indexed keywords
PHENYL RINGS;
CATALYSIS;
CATALYST ACTIVITY;
CRYSTAL STRUCTURE;
ENZYMES;
HYDROGEN BONDS;
RINGS (COMPONENTS);
BIOCHEMISTRY;
PHENYL GROUP;
SERINE;
STEROID DELTA ISOMERASE;
TYROSINE;
ALPHA HELIX;
AMINO ACID SUBSTITUTION;
ARTICLE;
CATALYSIS;
CIRCULAR DICHROISM;
CRYSTAL STRUCTURE;
ENZYME ACTIVE SITE;
ENZYME STABILITY;
ENZYME STRUCTURE;
HYDROGEN BOND;
KINETICS;
MOLECULAR INTERACTION;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN FOLDING;
PSEUDOMONAS PUTIDA;
STRUCTURE ANALYSIS;
AMINO ACID SUBSTITUTION;
BINDING SITES;
CATALYSIS;
CIRCULAR DICHROISM;
CRYSTALLIZATION;
CRYSTALLOGRAPHY, X-RAY;
ENZYME STABILITY;
KINETICS;
MODELS, MOLECULAR;
MUTATION;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
PSEUDOMONAS PUTIDA;
STEROID ISOMERASES;
TYROSINE;
NEGIBACTERIA;
PSEUDOMONAS;
PSEUDOMONAS PUTIDA;
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EID: 0035856578
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi015547k Document Type: Article |
Times cited : (11)
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References (40)
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