Xaa-Pro dipeptidyl-peptidase

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Xaa-Pro dipeptidyl-peptidase (EC 3.4.14.11, X-prolyl dipeptidyl aminopeptidase, PepX, X-prolyl dipeptidyl peptidase is an enzyme.^[1]^[2]^[3]^[4]^[5] It catalyses the following chemical 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

The intracellular enzyme from Lactococcus lactis (190-kDa) is the type example of peptidase family S15.

References

↑ Zevaco, C., Monnet, V. and Gripon, J.-C. (1990). "Intracellular X-prolyl dipeptidyl peptidase from Lactococcus lactis' spp. lactis: purification and properties". J. Appl. Bacteriol. 68: 357–366. doi:10.1111/j.1365-2672.1990.tb02886.x.
↑ Meyer-Barton, E.C., Klein, J.R., Imam, M. and Plapp, R. (1993). "Cloning and sequence analysis of the X-prolyl-dipeptidyl-aminopeptidase gene (pepX) from Lactobacillus delbrückii ssp. lactis DSM7290". Appl. Microbiol. Biotechnol. 40: 82–89. doi:10.1007/bf00170433. PMID 7765315.
↑ Habibi-Najafi, M.B. and Lee, B.H. (1994). "Purification and characterization of X-prolyl dipeptidyl peptidase from Lactobacillus casei' subsp. casei LLG". Appl. Microbiol. Biotechnol. 42: 280–286. doi:10.1007/s002530050250. PMID 7765768.
↑ Chich, J.-F., Gripon, J.-C. and Ribadeau-Dumas, B. (1995). "Preparation of bacterial X-prolyl dipeptidyl aminopeptidase and its stabilization by organic cosolvents". Anal. Biochem. 224: 245–249. doi:10.1006/abio.1995.1036. PMID 7710078.
↑ Chich, J.-F., Chapot-Chartier, M.P., Ribadeau-Dumas, B. and Gripon, J.-C. (1995). "Identification of the active site serine of the X-prolyl aminopeptidase from Lactococcus lactis'". FEBS Lett. 314: 139–142. doi:10.1016/0014-5793(92)80960-o.

External links

Xaa-Pro dipeptidyl-peptidase at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: proteases (EC 3.4)

3.4.11-19: Exopeptidase

3.4.11	Aminopeptidase Alanine Arginyl Aspartyl Cystinyl Leucyl Glutamyl Methionyl 1 2 O

3.4.13	Dipeptidase 1 2 3

3.4.14	Dipeptidyl peptidase Cathepsin C Dipeptidyl peptidase-4 Tripeptidyl peptidase Tripeptidyl peptidase I Tripeptidyl peptidase II

3.4.15	Angiotensin-converting enzyme

3.4.16	Serine type carboxypeptidases: Cathepsin A DD-transpeptidase

3.4.17	Metalloexopeptidases Carboxypeptidase A A2 B C E Glutamate II

Other/ungrouped	Metalloexopeptidase

3.4.21-25: Endopeptidase

Other/ungrouped: Amyloid precursor protein secretase

3.4.99: Unknown

Staphylokinase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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