CATH Domain 2d5lA01

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

Enzyme Information

3.4.14.12

Xaa-Xaa-Pro tripeptidyl-peptidase.

based on mapping to UniProt Q7MUW6

Hydrolysis of Xaa-Xaa-Pro-|-Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline.

-!- This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium Porphyromonas gingivalis, which has been implicated in adult periodontal disease. -!- The enzyme releases tripeptides from the free amino terminus of peptides and small proteins, such as interleukin-6. -!- The enzyme possesses an absolute requirement for a proline residue at the P1 position but is completely inactivated by a proline residue at the P1' position. -!- The size of the peptide does not affect the rate of reaction.

UniProtKB Entries (1)

Q7MUW6

PTP_PORGI

Porphyromonas gingivalis W83

Prolyl tripeptidyl peptidase

PDB Structure

PDB	2D5L
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Crystal Structure and Mechanism of Tripeptidyl Activity of Prolyl Tripeptidyl Aminopeptidase from Porphyromonas gingivalis Ito, K., Nakajima, Y., Xu, Y., Yamada, N., Onohara, Y., Ito, T., Matsubara, F., Kabashima, T., Nakayama, K., Yoshimoto, T. J.Mol.Biol.