Estb from Burkholderia gladioli: A novel esterase with a β-lactamase fold reveals steric factors to discriminate between esterolytic and β-lactam cleaving activity

Protein Science

Volumn 11, Issue 3, 2002, Pages 467-478

  Wagner, Ulrike G ^a   Petersen, Evamaria I ^b   Schwab, Helmut ^b   Kratky, Christoph ^a  

^a UNIVERSITY OF GRAZ   (Austria)

^b Erzherzog Johann University   (Austria)

Author keywords

Hydrolase; lactamase; Enzyme mechanism; Esterase

Indexed keywords

BACTERIAL ENZYME; BETA LACTAM; BETA LACTAMASE; DYFLOS; ESTB ESTERASE; ESTER; ESTERASE; PENICILLIN BINDING PROTEIN; PEPTIDASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BURKHOLDERIA GLADIOLI; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STEREOCHEMISTRY;

AMINO ACID SEQUENCE; BETA-LACTAMASES; BINDING SITES; BURKHOLDERIA; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESTERASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS); BURKHOLDERIA; BURKHOLDERIA GLADIOLI;

EID: 0036180211     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.33002     Document Type: Article

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