Lysine 22 in UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae is crucial for enzymatic activity and the formation of covalent adducts with the substrate phosphoenolpyruvate and the antibiotic fosfomycin

Biochemistry

Volumn 38, Issue 40, 1999, Pages 13162-13169

  Samland, Anne K ^a   Amrhein, Nikolaus ^a   Macheroux, Peter ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

FOSFOMYCIN; PHOSPHOENOLPYRUVATE; TRANSFERASE; URIDINE DIPHOSPHATE N ACETYLGALACTOSAMINE;

ARTICLE; BACTERIAL CELL WALL; CONFORMATIONAL TRANSITION; COVALENT BOND; DISSOCIATION CONSTANT; ENTEROBACTER CLOACAE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; THERMODYNAMICS;

3-PHOSPHOSHIKIMATE 1-CARBOXYVINYLTRANSFERASE; ALKYL AND ARYL TRANSFERASES; ANTI-BACTERIAL AGENTS; BINDING SITES; ENTEROBACTER CLOACAE; ENZYME ACTIVATION; FOSFOMYCIN; LYSINE; MODELS, MOLECULAR; PHOSPHOENOLPYRUVATE; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ENTEROBACTER CLOACAE;

EID: 0032832620     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991041e     Document Type: Article

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