The thermophilic, homohexameric aminopeptidase of Borrelia burgdorferi is a member of the M29 family of metallopeptidases.

ABSTRACT: Proteases are implicated in several aspects of the physiology of microorganisms, as well as in host-pathogen interactions. Aminopeptidases are also emerging as novel drug targets in infectious agents. In this study, we have characterized an aminopeptidase from the spirochete Borrelia burgdorferi, the causative agent of Lyme disease. The aminopeptidolytic activity was identified in cell extracts from B. burgdorferi by using the substrate leucine-7-amido-4-methylcoumarin. A protein displaying this activity was purified from B. burgdorferi by a two-step chromatographic procedure, yielding a approximately 300-kDa homo-oligomeric enzyme formed by monomers of approximately 50 kDa. Gel enzymography experiments showed that enzymatic activity depends on the oligomeric structure of the protease but

SUBMITTER: Bertin PB 

PROVIDER: S-EPMC1087410 | biostudies-literature | 2005 Apr

REPOSITORIES: biostudies-literature