Effect of pH on the active site of an Arg121Cys mutant of the metallo-β-lactamase from Bacillus cereus: Implications for the enzyme mechanism

Biochemistry

Volumn 44, Issue 12, 2005, Pages 4841-4849

  Davies, Anna M ^a   Rasia, Rodolfo M ^b   Vila, Alejandro J ^b   Sutton, Brian J ^a   Fabiane, Stella M ^a  

^a KING'S COLLEGE LONDON   (United Kingdom)

^b UNIVERSIDAD NACIONAL DE ROSARIO   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

ARGON; BACTERIA; CRYSTAL STRUCTURE; HYDROLYSIS; PH EFFECTS; ZINC;

BACTERIAL ENZYMES; HYDROXIDES; LIGANDS; PROTONATION;

ENZYMES;

ARGININE; BETA LACTAMASE; CYSTEINE; HYDROXIDE; LIGAND; METALLO BETA LACTAMASE; MUTANT PROTEIN; UNCLASSIFIED DRUG; WATER; ZINC;

ACIDITY; AMINO ACID SEQUENCE; ARTICLE; BACILLUS CEREUS; BINDING AFFINITY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME STRUCTURE; HYDROLYSIS; PH; PRIORITY JOURNAL; PROTON TRANSPORT; STRUCTURE ANALYSIS;

AMINO ACID SUBSTITUTION; ARGININE; BACILLUS CEREUS; BACTERIAL PROTEINS; BETA-LACTAMASES; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; ENZYME ACTIVATION; HYDROGEN-ION CONCENTRATION; LIGANDS; METALLOPROTEINS; OXIDATION-REDUCTION; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; ZINC;

EID: 15444376903     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047709t     Document Type: Article

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