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Xaa-Pro dipeptidilna peptidaza
Identifikatori
EC broj	3.4.14.11
CAS broj	54249-88-6
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Xaa-Pro dipeptidilna peptidaza (EC 3.4.14.11, X-prolil dipeptidilna aminopeptidaza, PepX, X-prolil dipeptidilna peptidaza, X-Pro dipeptidilna-peptidaza) je enzim.^[1]^[2]^[3]^[4]^[5] Ovaj enzim katalizuje sledeću hemijsku reakciju

Hidroliza Xaa-Pro veza uz odvajanje neblokiranih, N-terminalnih dipeptida. Supstrati su između ostalog Ala-Pro--p-nitroanilid i (sekvenciono) Tyr-Pro--Phe-Pro--Gly-Pro-Ile

Ovaj intraćelijski enzim iz Laktococcus lactis (190-kDa) pripada peptidaznoj familiji S15.

Reference

↑ 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.
↑ 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. 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. 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. 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.

Literatura

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Vanjske veze

MeSH Xaa-Pro+dipeptidyl-peptidase

[1] 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.

[2] 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. PMID 7765315.

[3] 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. PMID 7765768.

[4] 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. PMID 7710078.

[5] 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.

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