Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 3.4.11.9

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.4.11.9

Enzymes and Genes:
proline aminopeptidase P II Inferred from experiment : pepP ( Escherichia coli K-12 substr. MG1655 )

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Undetermined; a substrate lacks a chemical formula

Enzyme Commission Primary Name: Xaa-Pro aminopeptidase

Enzyme Commission Synonyms: proline aminopeptidase, aminopeptidase P, aminoacylproline aminopeptidase, X-Pro aminopeptidase

Enzyme Commission Summary:
This enzyme catalyzes release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.

A Mn2+-dependent, generally membrane-bound enzyme present in both mammalian and bacterial cells. In peptidase family M24 (methionyl aminopeptidase family).

Citations: [Yoshimoto94, Yoshimoto88, Yaron68, Fleminger82, Orawski87, Hooper90, Yaron70]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:3.4.11.9 , ENZYME:EC:3.4.11.9 , IUBMB-ExplorEnz:EC:3.4.11.9 , UniProt:RELATED-TO:P0A3Z2 , UniProt:RELATED-TO:P15034 , UniProt:RELATED-TO:P44881 , UniProt:RELATED-TO:P47566 , UniProt:RELATED-TO:Q09795 , UniProt:RELATED-TO:Q95333


References

Fleminger82: Fleminger G, Carmel A, Goldenberg D, Yaron A (1982). "Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and calf lung." Eur J Biochem 125(3);609-15. PMID: 6749499

Hooper90: Hooper NM, Hryszko J, Turner AJ (1990). "Purification and characterization of pig kidney aminopeptidase P. A glycosyl-phosphatidylinositol-anchored ectoenzyme." Biochem J 267(2);509-15. PMID: 2139778

Orawski87: Orawski AT, Susz JP, Simmons WH (1987). "Aminopeptidase P from bovine lung: solubilization, properties, and potential role in bradykinin degradation." Mol Cell Biochem 75(2);123-32. PMID: 3627107

Yaron68: Yaron A, Mlynar D (1968). "Aminopeptidase-P." Biochem Biophys Res Commun 32(4);658-63. PMID: 4878817

Yaron70: Yaron, A., Berger, A. (1970). "Aminopeptidase-P." Methods Enzymol.

Yoshimoto88: Yoshimoto T, Murayama N, Honda T, Tone H, Tsuru D (1988). "Cloning and expression of aminopeptidase P gene from Escherichia coli HB101 and characterization of expressed enzyme." J Biochem (Tokyo) 104(1);93-7. PMID: 2851590

Yoshimoto94: Yoshimoto T, Orawski AT, Simmons WH (1994). "Substrate specificity of aminopeptidase P from Escherichia coli: comparison with membrane-bound forms from rat and bovine lung." Arch Biochem Biophys 311(1);28-34. PMID: 8185318


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc13.