Xaa-Pro aminopeptidase

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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[edit]

  1. ^ Yaron, A.; Mlynar, D. (1968). "Aminopeptidase-P". Biochem. Biophys. Res. Commun. 32: 658–663. PMID 4878817. doi:10.1016/0006-291x(68)90289-1. 
  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.; Yaron, A. (1982). "Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and calf lung". Eur. J. Biochem. 125: 609–615. PMID 6749499. doi:10.1111/j.1432-1033.1982.tb06726.x. 
  4. ^ Orawski, A.T.; Susz, J.P.; Simmons, W.H. (1987). "Aminopeptidase-P from bovine lung - solubilization, properties, potential role in bradykinin degradation". Mol. Cell. Biochem. 75: 123–132. PMID 3627107. doi:10.1007/bf00229900. 
  5. ^ Hooper, N.M.; Hryszko, J.; Turner, A.J. (1990). "Purification and characterization of pig kidney aminopeptidase P". Biochem. J. 267: 509–515. PMC 1131318Freely accessible. PMID 2139778. doi:10.1042/bj2670509. 

External links[edit]