CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.1370 | Neurolysin; domain 3 |
|
1.10.1370.40 |
Domain Context
CATH Clusters
| Superfamily | 1.10.1370.40 |
| Functional Family | Dipeptidyl carboxypeptidase II |
Enzyme Information
| 3.4.15.5 |
Peptidyl-dipeptidase Dcp.
based on mapping to UniProt P24171
Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides, with broad specificity. Does not hydrolyze bonds in which P1' is Pro, or both P1 and P1' are Gly.
-!- Inhibited by captopril, as is peptidyl-dipeptidase A. -!- Belongs to peptidase family M3. -!- Formerly EC 3.4.15.3.
|
UniProtKB Entries (1)
| P24171 |
DCP_ECOLI
Escherichia coli K-12
Dipeptidyl carboxypeptidase
|
PDB Structure
| PDB | 1Y79 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal Structure of the E.coli Dipeptidyl Carboxypeptidase Dcp: Further Indication of a Ligand-dependant Hinge Movement Mechanism
J.Mol.Biol.
|
