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Updated: Aug 17, 2026

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
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.
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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