| Accession | TIGR01886 |
| Name | dipeptidase |
| Function | dipeptidase PepV |
| Gene Symbol | pepV |
| Trusted Cutoff | 632.00 |
| Domain Trusted Cutoff | 632.00 |
| Noise Cutoff | 530.20 |
| Domain Noise Cutoff | 530.20 |
| Isology Type | equivalog |
| EC Number | 3.4.13.- |
| HMM Length | 466 |
| Mainrole Category | Protein fate |
| Subrole Category | Degradation of proteins, peptides, and glycopeptides |
| Gene Ontology Term | GO:0006508: proteolysis biological_process |
| | GO:0008237: metallopeptidase activity molecular_function |
| Author | Selengut J |
| Entry Date | Apr 23 2003 10:07AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This 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. |
| References | RN [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 |
