CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.140 | 8 Propeller |
|
2.140.10 | Methanol Dehydrogenase; Chain A |
|
2.140.10.30 | Dipeptidylpeptidase IV, N-terminal domain |
Domain Context
CATH Clusters
| Superfamily | Dipeptidylpeptidase IV, N-terminal domain |
| Functional Family | Dipeptidyl peptidase 4 |
Enzyme Information
| 3.4.21.- |
Serine endopeptidases.
based on mapping to UniProt Q12884
|
| 3.4.14.5 |
Dipeptidyl-peptidase IV.
based on mapping to UniProt Q12884
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
-!- A membrane-bound serine-type peptidase in mammals. -!- EC 3.4.14.11 catalyzes a similar reaction. -!- Belongs to peptidase family S9B.
|
| 3.4.21.26 |
Prolyl oligopeptidase.
based on mapping to UniProt Q12884
Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.
-!- Found in vertebrates, plants and Flavobacterium. -!- Generally cytosolic, commonly activated by thiol compounds. -!- Belongs to peptidase family S9A. -!- Formerly EC 3.4.22.18.
|
UniProtKB Entries (1)
| Q12884 |
SEPR_HUMAN
Homo sapiens
Prolyl endopeptidase FAP
|
PDB Structure
| PDB | 1Z68 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Spodoptera |
| Primary Citation |
Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha.
J.Biol.Chem.
|