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  • Title: Biochemical-genetic analysis and distribution of FAR-1, a class A beta-lactamase from Nocardia farcinica.
    Author: Laurent F, Poirel L, Naas T, Chaibi EB, Labia R, Boiron P, Nordmann P.
    Journal: Antimicrob Agents Chemother; 1999 Jul; 43(7):1644-50. PubMed ID: 10390216.
    Abstract:
    From genomic DNA of the clinical isolate Nocardia farcinica VIC, a 1. 6-kb Sau3AI fragment was cloned and expressed in Escherichia coli JM109. The recombinant strain expressed a beta-lactamase (pI, 4.6), FAR-1, which conferred high levels of resistance to amoxicillin, piperacillin, ticarcillin, and cephalothin. The hydrolysis constants (kcat, Km, Ki, and 50% inhibitory concentration) confirmed the MIC results and showed that FAR-1 activity is inhibited by clavulanic acid and at a low level by tazobactam and sulbactam. Moreover, FAR-1 beta-lactamase hydrolyzes aztreonam (at a low level) without significant activity against ceftazidime, cefotaxime and imipenem. FAR-1 mature protein of molecular mass ca 32 kDa, has less than 60% amino acid identity with any other class A beta-lactamases, being most closely related to PEN-A from Burkholderia cepacia (52%). A blaFAR-1-like gene was found in all studied N. farcinica strains, underlining the constitutive origin of this gene.
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