title: Molecular characterization of the SHV-11 beta-lactamase of Shigella dysenteriae.
abstract: A beta-lactamase with an M(r) of 29,000 and a pI of 7.6 was partially purified from a clinical isolate of Shigella dysenteriae. The bla gene encoded the SHV-11 enzyme carrying the substitution Leu-->Gln at position 35 and was linked to a strong promoter. This variant, unlike the prototype SHV-1 enzyme, hydrolyzed oxacillin, cloxacillin, and oxyiminocephalosporins such as cefotaxime.
authors.affiliation: Department of Chemistry, Bose Institute, Calcutta 700 009, India.
authors.forename: J
authors.initials: J
authors.lastname: Ahamed
authors.forename: M
authors.initials: M
authors.lastname: Kundu
mesh_terms: D003001:Cloning, Molecular; D003227:Conjugation, Genetic / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D006868:Hydrolysis; D012762:Shigella dysenteriae / Q000201:enzymology*; D018440:beta-Lactam Resistance / Q000235:genetics; D001618:beta-Lactamases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: C107197:beta-lactamase SHV-11; D001618:beta-Lactamases