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Volumn 49, Issue 45, 2010, Pages 9685-9687
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Structures of the Michaelis complex (1.2 Å) and the covalent acyl intermediate (2.0 Å) of cefamandole bound in the active sites of the mycobacterium tuberculosis β-lactamase K73A and E166A mutants
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Author keywords
[No Author keywords available]
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Indexed keywords
ACTIVE SITE;
ACTIVE SITE RESIDUES;
CATALYTIC MECHANISMS;
COVALENTLY BOUND;
DEACYLATION;
LACTAMASES;
MICHAELIS COMPLEX;
MYCOBACTERIUM TUBERCULOSIS;
CHEMOTHERAPY;
BETA LACTAMASE;
CEFAMANDOLE;
ACYLATION;
ARTICLE;
DEACYLATION;
ENZYME ACTIVE SITE;
HYDROGEN BOND;
MUTATIONAL ANALYSIS;
MYCOBACTERIUM TUBERCULOSIS;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN STRUCTURE;
AMINO ACID SUBSTITUTION;
BETA-LACTAMASES;
CATALYTIC DOMAIN;
CEFAMANDOLE;
DNA, BACTERIAL;
GENOME, BACTERIAL;
KINETICS;
MODELS, MOLECULAR;
MYCOBACTERIUM TUBERCULOSIS;
PROTEIN BINDING;
MYCOBACTERIUM TUBERCULOSIS;
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EID: 78149457617
PISSN: 00062960
EISSN: 15204995
Source Type: Journal
DOI: 10.1021/bi1015088 Document Type: Article |
Times cited : (47)
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References (25)
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