Ontology highlight
ABSTRACT:
SUBMITTER: Neuwirth C
PROVIDER: S-EPMC90874 | biostudies-literature | 2001 Dec
REPOSITORIES: biostudies-literature
Neuwirth C C Madec S S Siebor E E Pechinot A A Duez J M JM Pruneaux M M Fouchereau-Peron M M Kazmierczak A A Labia R R
Antimicrobial agents and chemotherapy 20011201 12
TEM-89 (CMT-3) is the first complex mutant beta-lactamase produced by a clinical strain of Proteus mirabilis (strain Pm 631). This new enzyme, which has a pI of 6.28, is derived from TEM-3 and has a single amino acid substitution also encountered in TEM-59 (inhibitor-resistant TEM beta-lactamase IRT-17): Ser-130 to Gly. TEM-89 hydrolyzed penicillins to the same extent that TEM-3 did but lost almost all hydrolytic activity for cephalosporins and, like TEM-59, was highly resistant to inhibitors. ...[more]