Structural basis for the role of Asp-120 in metallo-β-lactamases

Biochemistry

Volumn 46, Issue 37, 2007, Pages 10664-10674

  Crisp, Jonathan ^a   Conners, Rebecca ^a   Garrity, James D ^b   Carenbauer, Anne L ^b   Crowder, Michael W ^b   Spencer, James ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

^b MIAMI UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMINISHED ACTIVITY; MOXALACTAM; NITROGEN SPECIES; STENOTROPHOMONAS MALTOPHILIA;

AMIDES; ANTIBIOTICS; BACTERIA; CRYSTAL STRUCTURE; HYDROLYSIS; PROTON TRANSFER; SUBSTITUTION REACTIONS; ZINC;

ENZYMES;

AMIDE; AMINO ACID; ASPARAGINE; ASPARTIC ACID; BETA LACTAM ANTIBIOTIC; CYSTEINE; HYDROXIDE; LATAMOXEF; METAL ION; METALLO BETA LACTAMASE; MUTANT PROTEIN; NITROGEN; WATER; ZINC;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; STENOTROPHOMONAS MALTOPHILIA; WILD TYPE;

ASPARAGINE; ASPARTIC ACID; BETA-LACTAMASES; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; MOXALACTAM; MUTANT PROTEINS; PROTEIN SUBUNITS; SOLUTIONS; STATIC ELECTRICITY; STENOTROPHOMONAS MALTOPHILIA; ZINC;

STENOTROPHOMONAS MALTOPHILIA;

EID: 34548687684     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700707u     Document Type: Article

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