title: Properties of beta-lactamase from Pseudomonas syringae.
abstract: Pseudomonas syringae isolate BR2R produces tabtoxin, a beta-lactam-containing antibiotic, and the causative agent of wildfire disease of green bean (Phaseolus vulgaris). beta-Lactamase production has been suggested as the mechanism that protects P. syringae from tabtoxin. We sought to determine whether the organism produces beta-lactamase and whether the enzyme plays a role in protection from this antibiotic. P. syringae and mutants defective in tabtoxin production and resistance produce beta-lactamase. Three distinct beta-lactamases with molecular weights of 41,000 were identified. The isoelectric points of the proteins were 6.1, 6.8, and 9.2. The enzymes preferentially hydrolyze cephalosporin. This investigation demonstrates that the organism produces multiple beta-lactamases and describes characteristics of the proteins.
authors.affiliation: Department of Biological Sciences, University of Wisconsin-Parkside, Kenosha 53141, USA.
authors.forename: R H
authors.initials: RH
authors.lastname: Coleman
authors.forename: J
authors.initials: J
authors.lastname: Shaffer
authors.forename: H
authors.initials: H
authors.lastname: True
mesh_terms: D007525:Isoelectric Focusing; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D001618:beta-Lactamases / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D012967:Sodium Dodecyl Sulfate; D001618:beta-Lactamases