Characterization of an extracellular dipeptidase from Streptococcus gordonii FSS2.
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.
Goldstein
J M
JM
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602-7229, USA.
Kordula
T
T
Moon
J L
JL
Mayo
J A
JA
Travis
J
J
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
D004150:Dipeptidases