Enzymatic and molecular characterisation of leucine aminopeptidase of Burkholderia pseudomallei.

ABSTRACT:

Background

Leucine aminopeptidase (LAP) has been known to be a housekeeping protease, DNA-binding protein and repressor or activator in the operon regulation of virulence-associated genes in several bacterial species. LAP activity was consistently detected in overnight cultures of Burkholderia pseudomallei, the causative agent of melioidosis and this enzyme was partially purified and characterised in this study. The intra- and inter-species nucleotide and deduced amino acid sequence variation of LAP encoding gene (pepA) was determined. A pepA/PCR-RFLP assay was designed to facilitate the identification of major LAP sequence types amongst clinical and environmental isolates of B. pseudomallei.

Results

LAP activity was detected in B. pseudomallei culture supernantants by zymog

SUBMITTER: Liew SM 

PROVIDER: S-EPMC3680066 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature