A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 126.96.36.199
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|Prolyl tripeptidyl peptidase.|
|Prolyltripeptidyl amino peptidase.|
|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.
|PRIAM enzyme-specific profiles||188.8.131.52|
|KEGG Ligand Database for Enzyme Nomenclature||184.108.40.206|
|IUBMB Enzyme Nomenclature||220.127.116.11|
|MEDLINE||Find literature relating to 18.104.22.168|
entries corresponding to 3.4.14.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-