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Characterization of an extracellular dipeptidase from Streptococcus gordonii FSS2
J M Goldstein1, T Kordula, J L Moon
1Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602-7229, USA.
Infection and Immunity
|January 25, 2005
Summary
Streptococcus gordonii FSS2 metalloenzyme PepV, a dipeptidase, was purified and characterized. Its gene was cloned, revealing homology to related bacterial dipeptidases.
Area of Science:
- Microbiology
- Enzymology
- Molecular Biology
Background:
- Dipeptidases play crucial roles in peptide metabolism.
- Streptococcus species are important oral commensals, but their enzymatic activities are not fully understood.
Purpose of the Study:
- To purify and characterize the dipeptidase PepV from Streptococcus gordonii FSS2.
- To clone and analyze the gene encoding PepV.
Main Methods:
- Purification of PepV from bacterial culture fluids.
- Biochemical characterization of the enzyme's properties.
- Gene cloning and sequence analysis.
Main Results:
- PepV was identified as a monomeric metalloenzyme (approx. 55 kDa) that prefers hydrophobic dipeptides.
- The S. gordonii PepV gene encodes a 467-amino acid protein (theoretical mass 51,114 Da, pI 4.8).
- The PepV gene shows homology to PepV families in Lactobacillus and Lactococcus species.
Conclusions:
- PepV from S. gordonii is a novel metalloenzyme with specific substrate preferences.
- The genetic analysis provides insights into the evolution of dipeptidases in related bacterial genera.
- This study contributes to understanding peptide metabolism in oral streptococci.