From Wikipedia, the free encyclopedia
(Redirected from X-Pro aminopeptidase)
Xaa-Pro aminopeptidase
Identifiers
EC no. 3.4.11.9
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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. Vol. 19. pp. 522–534. doi: 10.1016/0076-6879(70)19039-2. ISBN  978-0-12-181881-4.
  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. S2CID  37892547.
  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.
From Wikipedia, the free encyclopedia
(Redirected from X-Pro aminopeptidase)
Xaa-Pro aminopeptidase
Identifiers
EC no. 3.4.11.9
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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. Vol. 19. pp. 522–534. doi: 10.1016/0076-6879(70)19039-2. ISBN  978-0-12-181881-4.
  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. S2CID  37892547.
  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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