Xaa-Pro aminopeptidase

Xaa-Pro aminopeptidase
Identifiers
EC number 3.4.11.9
CAS number 37288-66-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Xaa-Pro aminopeptidase (EC 3.4.11.9, X-Pro aminopeptidase, proline aminopeptidase, aminopeptidase P, aminoacylproline aminopeptidase) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide

This enzyme is Mn2+-dependent.

References

  1. ↑ Yaron A, Mlynar D (August 1968). "Aminopeptidase-P". Biochemical and Biophysical Research Communications. 32 (4): 658–63. doi:10.1016/0006-291x(68)90289-1. PMID 4878817.
  2. ↑ Yaron, A.; Berger, A. (1970). "Aminopeptidase-P". Methods Enzymol. 19: 522–534. doi:10.1016/0076-6879(70)19039-2.
  3. ↑ Fleminger G, Carmel A, Goldenberg D, Yaron A (July 1982). "Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and calf lung". European Journal of Biochemistry. 125 (3): 609–15. doi:10.1111/j.1432-1033.1982.tb06726.x. PMID 6749499.
  4. ↑ Orawski AT, Susz JP, Simmons WH (June 1987). "Aminopeptidase P from bovine lung: solubilization, properties, and potential role in bradykinin degradation". Molecular and Cellular Biochemistry. 75 (2): 123–32. doi:10.1007/bf00229900. PMID 3627107.
  5. ↑ Hooper NM, Hryszko J, Turner AJ (April 1990). "Purification and characterization of pig kidney aminopeptidase P. A glycosyl-phosphatidylinositol-anchored ectoenzyme". The Biochemical Journal. 267 (2): 509–15. doi:10.1042/bj2670509. PMC 1131318. PMID 2139778.
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