Characterization of an extracellular dipeptidase from Streptococcus gordonii FSS2.
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ABSTRACT:
SUBMITTER: Goldstein JM
PROVIDER: S-EPMC546950 | biostudies-literature | 2005 Feb
REPOSITORIES: biostudies-literature
Publications
Characterization of an extracellular dipeptidase from Streptococcus gordonii FSS2.
Goldstein J M JM Kordula T T Moon J L JL Mayo J A JA Travis J J
Infection and immunity 20050201 2
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. ...[more]
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