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Carboxypeptidase A2 is an enzyme that in humans is encoded by the CPA2gene.[1][2][3]
Three different forms of human pancreatic procarboxypeptidase A have been isolated. The A1 and A2 forms are monomeric proteins with different biochemical properties. The A2 form of pancreatic procarboxypeptidase acts on aromatic C-terminal residues[3]
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Pascual R, Burgos FJ, Salva M, et al. (1989). "Purification and properties of five different forms of human procarboxypeptidases". Eur. J. Biochem. 179 (3): 609–16. doi:10.1111/j.1432-1033.1989.tb14590.x. PMID2920728.
Laethem RM, Blumenkopf TA, Cory M, et al. (1996). "Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2". Arch. Biochem. Biophys. 332 (1): 8–18. doi:10.1006/abbi.1996.0310. PMID8806703.
Reverter D, García-Sáez I, Catasús L, et al. (1998). "Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2". FEBS Lett. 420 (1): 7–10. doi:10.1016/S0014-5793(97)01476-2. PMID9450539.
Reverter D, Fernández-Catalán C, Baumgartner R, et al. (2000). "Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2". Nat. Struct. Biol. 7 (4): 322–8. doi:10.1038/74092. PMID10742178.
Wouters MA, Husain A (2002). "Changes in zinc ligation promote remodeling of the active site in the zinc hydrolase superfamily". J. Mol. Biol. 314 (5): 1191–207. doi:10.1006/jmbi.2000.5161. PMID11743734.
Dantas G, Kuhlman B, Callender D, et al. (2003). "A large scale test of computational protein design: folding and stability of nine completely redesigned globular proteins". J. Mol. Biol. 332 (2): 449–60. doi:10.1016/S0022-2836(03)00888-X. PMID12948494.