Characterization of an extracellular dipeptidase from Streptococcus gordonii FSS2.

ABSTRACT: PepV, a dipeptidase found in culture fluids of Streptococcus gordonii FSS2, was purified and characterized, and its gene was cloned. PepV is a monomeric metalloenzyme of approximately 55 kDa that preferentially degrades hydrophobic dipeptides. The gene encodes a polypeptide of 467 amino acids, with a theoretical molecular mass of 51,114 Da and a calculated pI of 4.8. The S. gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp.

SUBMITTER: Goldstein JM 

PROVIDER: S-EPMC546950 | biostudies-literature | 2005 Feb

REPOSITORIES: biostudies-literature