CATH Classification

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.
Aertgeerts, K., Levin, I., Shi, L., Snell, G.P., Jennings, A., Prasad, G.S., Zhang, Y., Kraus, M.L., Salakian, S., Sridhar, V., Wijnands, R., Tennant, M.G.
J.Biol.Chem.
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