Characterization of the β-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studies

Protein Engineering

Volumn 13, Issue 12, 2000, Pages 857-863

  Alkema, Wynand B L ^a   Hensgens, Charles M H ^a   Kroezinga, Els H ^a   De Vries, Erik ^a   Floris, René ^a   Van Der Laan, Jan Metske ^b   Dijkstra, Bauke W ^a   Janssen, Dick B ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b DSM RESOLVE   (Netherlands)

Author keywords

Penicillin acylase; Site directed mutagenesis; Substrate induced conformational change; X ray structure; lactam binding site

Indexed keywords

6 AMINOPENICILLANIC ACID; ACETANILIDE; AMIDASE; BETA LACTAM ANTIBIOTIC; CARBONYL DERIVATIVE; CARBOXYLIC ACID DERIVATIVE; PENICILLIN DERIVATIVE; PENICILLIN G; PHENYLACETIC ACID; THIAZOLIDINE DERIVATIVE;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; DRUG BINDING SITE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROGEN BOND; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034462589     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/13.12.857     Document Type: Article

References (27)