title: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602-7229, USA.
authors.forename: J M
authors.initials: JM
authors.lastname: Goldstein
authors.forename: T
authors.initials: T
authors.lastname: Kordula
authors.forename: J L
authors.initials: JL
authors.lastname: Moon
authors.forename: J A
authors.initials: JA
authors.lastname: Mayo
authors.forename: J
authors.initials: J
authors.lastname: Travis
mesh_terms: D000595:Amino Acid Sequence; D004150:Dipeptidases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D013291:Streptococcus / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D004150:Dipeptidases