Rate-limiting steps and role of active site lys443 in the mechanism of carbapenam synthetase

Biochemistry

Volumn 46, Issue 32, 2007, Pages 9337-9345

  Arnett, Samantha O ^a   Gerratana, Barbara ^a,b   Townsend, Craig A ^a  

^a JOHNS HOPKINS UNIVERSITY   (United States)

^b Bldg 142   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITES; CARBAPENAM SYNTHETASES; INTRAMOLECULAR RING FORMATION;

ADENOSINETRIPHOSPHATE; BIOSYNTHESIS; CATALYSIS; CONFORMATIONS; PH EFFECTS; STEREOCHEMISTRY;

ENZYME KINETICS;

ADENOSINE TRIPHOSPHATE; BETA LACTAM; CARBAPEN 2 EM 3 CARBOXYLATE; CARBAPENAM SYNTHETASE; CARBAPENEM DERIVATIVE; CARBOXYLIC ACID DERIVATIVE; DEUTERIUM; ISOTOPE; LYSINE; MAGNESIUM ION; SOLVENT; SYNTHETASE; UNCLASSIFIED DRUG;

ADENYLATION; AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CATALYST; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME SUBSTRATE COMPLEX; MEASUREMENT; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STEREOCHEMISTRY; STRUCTURE ANALYSIS; VISCOSITY;

ALANINE; BINDING SITES; CARBON-NITROGEN LIGASES; CATALYSIS; DEUTERIUM; ENZYME ACTIVATION; ESCHERICHIA COLI PROTEINS; HYDROGEN-ION CONCENTRATION; KINETICS; LYSINE; SOLVENTS; SUBSTRATE SPECIFICITY; VARIATION (GENETICS); VISCOSITY;

EID: 34547863927     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0618464     Document Type: Article

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