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Journal of the American Chemical Society

Volumn 124, Issue 19, 2002, Pages 5333-5340

An ultrahigh resolution structure of TEM-1 β-lactamase suggests a role for Glu166 as the general base in acylation

(3) Minasov, George a Wang, Xiaojun a Shoichet, Brian K a

a NORTHWESTERN UNIVERSITY (United States)

Author keywords

[No Author keywords available]

Indexed keywords

TRANSITION-STATE ANALOGUES;

AMINO ACIDS; ANTIBIOTICS; CARRIER CONCENTRATION; CHEMICAL BONDS; HYDROLYSIS; X RAY CRYSTALLOGRAPHY;

ENZYMES;

BETA LACTAM; BETA LACTAMASE; CARBOXYLIC ACID; GLUTATHIONE; SERINE PROTEINASE;

ACYLATION; ANTIBIOTIC RESISTANCE; ARTICLE; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STRUCTURE; HYDROGEN BOND; HYDROLYSIS; MOLECULAR DYNAMICS; PH; PROTON TRANSPORT; R FACTOR; X RAY CRYSTALLOGRAPHY;

BETA-LACTAMASES; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ELECTRONS; GLUTAMIC ACID; HYDROGEN; MODELS, MOLECULAR; PROTEIN CONFORMATION;

EID: 0037094114 PISSN: 00027863 EISSN: None Source Type: Journal
DOI: 10.1021/ja0259640 Document Type: Article

Times cited : (193)

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