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Characterization of an Extracellular Dipeptidase from Streptococcus gordonii FSS2

Authors
Publisher
American Society for Microbiology
Publication Date
Source
PMC
Keywords
Disciplines
  • Biology
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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.

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