ExplorEnz: EC 3.4.14.11

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3.4.14.11

Accepted name:

Xaa-Pro dipeptidyl-peptidase

Reaction:

Hydrolyses Xaa-Pro┼ bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro┼p-nitroanilide and (sequentially) Tyr-Pro┼Phe-Pro┼Gly-Pro┼Ile

Other name(s):

X-prolyl dipeptidyl aminopeptidase; PepX; X-prolyl dipeptidyl peptidase; X-Pro dipeptidyl-peptidase

Comments:

The intracellular enzyme from Lactococcus lactis (190-kDa) is the type example of peptidase family S15. The reaction is similar to that catalysed by dipeptidyl-peptidase IV of animals

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 54249-88-6

References:

1.	Zevaco, C., Monnet, V. and Gripon, J.-C. Intracellular X-prolyl dipeptidyl peptidase from Lactococcus lactis spp. lactis: purification and properties. J. Appl. Bacteriol. 68 (1990) 357–366.
2.	Meyer-Barton, E.C., Klein, J.R., Imam, M. and Plapp, R. Cloning and sequence analysis of the X-prolyl-dipeptidyl-aminopeptidase gene (pepX) from Lactobacillus delbrückii ssp. lactis DSM7290. Appl. Microbiol. Biotechnol. 40 (1993) 82–89. [PMID: 7765315]
3.	Habibi-Najafi, M.B. and Lee, B.H. Purification and characterization of X-prolyl dipeptidyl peptidase from Lactobacillus casei subsp. casei LLG. Appl. Microbiol. Biotechnol. 42 (1994) 280–286. [PMID: 7765768]
4.	Chich, J.-F., Gripon, J.-C. and Ribadeau-Dumas, B. Preparation of bacterial X-prolyl dipeptidyl aminopeptidase and its stabilization by organic cosolvents. Anal. Biochem. 224 (1995) 245–249. [DOI] [PMID: 7710078]
5.	Chich, J.-F., Chapot-Chartier, M.P., Ribadeau-Dumas, B. and Gripon, J.-C. Identification of the active site serine of the X-prolyl aminopeptidase from Lactococcus lactis. FEBS Lett. 314 (1995) 139–142.

[EC 3.4.14.11 created 1996]