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ENZYME

ENZYME entry: EC 3.4.14.12

PURL: https://purl.expasy.org/enzyme/EC/3.4.14.12
Accepted Name
Xaa-Xaa-Pro tripeptidyl-peptidase
Alternative Name(s)
prolyltripeptidyl aminopeptidase
prolyltripeptidyl amino peptidase
prolyl tripeptidyl peptidase
PTP-A
TPP
Reaction catalysed
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
Comment(s)
  • 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.
Cross-references
BRENDA3.4.14.12
EC2PDB3.4.14.12
ExplorEnz3.4.14.12
KEGG Ligand Database for Enzyme Nomenclature3.4.14.12
IUBMB Enzyme Nomenclature3.4.14.12
MEDLINEFind literature relating to 3.4.14.12
MetaCyc3.4.14.12
Rhea expert-curated reactions3.4.14.12
UniProtKB/Swiss-Prot
B2RJX3, PTP_PORG3Q7MUW6, PTP_PORGI

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