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Membrane Pro-X carboxypeptidase

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Membrane Pro-Xaa carboxypeptidase
Identifiers
EC no.3.4.17.16
CAS no.9075-64-3
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Membrane Pro-Xaa carboxypeptidase (EC 3.4.17.16, carboxypeptidase P, microsomal carboxypeptidase) is an enzyme. This enzyme catalyses the following chemical reaction

Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond

This is one of the renal brush border exopeptidases

References

  1. Dehm P, Nordwig A (December 1970). "The cleavage of prolyl peptides by kidney peptidases. Isolation of a microsomal carboxypeptidase from swine kidney". European Journal of Biochemistry. 17 (2): 372–7. doi:10.1111/j.1432-1033.1970.tb01175.x. PMID 5500406.
  2. Booth AG, Hubbard LM, Kenny AJ (May 1979). "Proteins of the kidney microvillar membrane. Immunoelectrophoretic analysis of the membrane hydrolases: identification and resolution of the detergent- and proteinase-solubilized forms". The Biochemical Journal. 179 (2): 397–405. doi:10.1042/bj1790397. PMC 1186637. PMID 486090.
  3. Hedeager-Sørensen S, Kenny AJ (July 1985). "Proteins of the kidney microvillar membrane. Purification and properties of carboxypeptidase P from pig kidneys". The Biochemical Journal. 229 (1): 251–7. doi:10.1042/bj2290251. PMC 1145174. PMID 4038259.

External links

Hydrolase: proteases (EC 3.4)
3.4.11-19: Exopeptidase
3.4.11
3.4.13
3.4.14
3.4.15
3.4.16
3.4.17
Metalloexopeptidases
Carboxypeptidase
A
A2
B
C
E
Glutamate II
Other/ungrouped
3.4.21-25: Endopeptidase
3.4.99: Unknown
Enzymes
Activity
Regulation
Classification
Kinetics
Types
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