HMM Summary Page: TIGR01886

Functiondipeptidase PepV
Gene SymbolpepV
Trusted Cutoff632.00
Domain Trusted Cutoff632.00
Noise Cutoff530.20
Domain Noise Cutoff530.20
Isology Typeequivalog
EC Number3.4.13.-
HMM Length466
Mainrole CategoryProtein fate
Subrole CategoryDegradation of proteins, peptides, and glycopeptides
Gene Ontology TermGO:0006508: proteolysis biological_process
GO:0008237: metallopeptidase activity molecular_function
AuthorSelengut J
Entry DateApr 23 2003 10:07AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis model represents a small clade of dipeptidase enzymes which are members of the larger M25 subfamily of metalloproteases. Two characterized enzymes are included in the seed. One, from Lactococcus lactis has been shown to act on a wide range of dipeptides, but not larger peptides. The enzyme from Lactobacillus delbrueckii was originally characterized as a Xaa-His dipeptidase, specifically a carnosinase (beta-Ala-His) by complementation of an E. coli mutant. Further study, including the crystallization of the enzyme [1], has shown it to also be a non-specific dipeptidase. This group also includes enzymes from Streptococcus and Enterococcus.
ReferencesRN [1] RM PMID: 12176387 RT Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides. RA Jozic D, Bourenkow G, Bartunik H, Scholze H, Dive V, Henrich B, Huber R, Bode W, Maskos K. RL Structure (Camb) 2002 Aug;10(8):1097-106