The crystal structure of a (-) γ-lactamase from an Aureobacterium species reveals a tetrahedral intermediate in the active site

Journal of Molecular Biology

Volumn 338, Issue 3, 2004, Pages 519-532

  Line, Kirsty ^a   Isupov, Michail N ^a   Littlechild, Jennifer A ^a  

^a UNIVERSITY OF EXETER   (United Kingdom)

Author keywords

BD1, (3aR,7aS) 3a,4,7,7a tetrahydro benzo 1,3 dioxol 2 one; BPOA2, bromoperoxidase A2 from Streptomyces aureofaciens; Catalytic mechanism; Cofactor free haloperoxidase; MCD, monochlorodimedone; Oxyanion hole; X ray structure; hydrolase

Indexed keywords

BACTERIAL ENZYME; CAMPHOR DERIVATIVE; ETHYLENE DERIVATIVE; GAMMA LACTAM DERIVATIVE; GAMMA LACTAMASE; HYDROLASE INHIBITOR; LIGAND; NORCAMPHOR; PENICILLINASE; RECOMBINANT ENZYME; SERINE DEHYDRATASE; UNCLASSIFIED DRUG;

ARTICLE; AUREOBACTERIUM; BACTERIUM; CATALYSIS; COVALENT BOND; CRYSTAL STRUCTURE; DENSITY; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HOST CELL; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

AUREOBACTERIUM; MICROBACTERIUM; STAPHYLOCOCCUS PHAGE 3A; STREPTOMYCES; STREPTOMYCES AUREOFACIENS;

EID: 1842686191     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.03.001     Document Type: Article

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