Regulation of the Marinomonas mediterranea antimicrobial protein lysine oxidase by L-lysine and the sensor histidine kinase PpoS.

ABSTRACT: Some Gram-negative bacteria express a novel enzyme with lysine-epsilon-oxidase (LOD) activity (EC 1.4.3.20). The oxidation of l-Lys generates, among other products, hydrogen peroxide, which confers antimicrobial properties to this kind of enzyme and has been shown to be involved in cell death during biofilm development and differentiation. In addition to LOD, the melanogenic marine bacterium Marinomonas mediterranea, which forms part of the microbiota of the marine plant Posidonia oceanica, expresses two other oxidases of biotechnological interest, a multicopper oxidase, PpoA, with laccase activity and a tyrosinase named PpoB, which is responsible for melanin synthesis. By using both lacZ fusions with the lodAB promoter and quantitative reverse transcription-PCR (qRT-PCR), this study shows

SUBMITTER: Molina-Quintero LR 

PROVIDER: S-EPMC2937512 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature