Peptidase M20A, peptidase V-related (IPR010964)

Short name: M20A_pepV-rel

Overlapping homologous superfamilies

Family relationships


This entry consists of Beta-Ala-Xaa dipeptidase (peptidase V, PepV) from Lactobacillus delbrueckii [PMID: 12176387] and other putative bacterial zinc dipeptidases belonging to the MEROPS peptidase family M20 (clan MH), subfamily M20A.

PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminal, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity [PMID: 12176387, PMID: 16962986].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016805 dipeptidase activity
GO:0008270 zinc ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.