Carboxypeptidase A2 Explained

Carboxypeptidase A2 is an enzyme that in humans is encoded by the CPA2 gene.^{[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

Further reading

• Pascual R, Burgos FJ, Salva M . Purification and properties of five different forms of human procarboxypeptidases. . Eur. J. Biochem. . 179 . 3 . 609–16 . 1989 . 2920728 . 10.1111/j.1432-1033.1989.tb14590.x . etal. free .
• Laethem RM, Blumenkopf TA, Cory M . Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2. . Arch. Biochem. Biophys. . 332 . 1 . 8–18 . 1996 . 8806703 . 10.1006/abbi.1996.0310 . etal.
• García-Sáez I, Reverter D, Vendrell J . The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen. . EMBO J. . 16 . 23 . 6906–13 . 1998 . 9384570 . 10.1093/emboj/16.23.6906 . 1170294 . etal.
• Reverter D, García-Sáez I, Catasús L . Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2. . FEBS Lett. . 420 . 1 . 7–10 . 1998 . 9450539 . 10.1016/S0014-5793(97)01476-2 . 7781802 . etal. free .
• Reverter D, Fernández-Catalán C, Baumgartner R . 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 . 2000 . 10742178 . 10.1038/74092 . 24225493 . etal.
• Wouters MA, Husain A . Changes in zinc ligation promote remodeling of the active site in the zinc hydrolase superfamily. . J. Mol. Biol. . 314 . 5 . 1191–207 . 2002 . 11743734 . 10.1006/jmbi.2000.5161 .
• Strausberg RL, Feingold EA, Grouse LH . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . etal. free .
• Jiménez MA, Villegas V, Santoro J . NMR solution structure of the activation domain of human procarboxypeptidase A2. . Protein Sci. . 12 . 2 . 296–305 . 2003 . 12538893 . 10.1110/ps.0227303 . 2312417 . etal.
• Dantas G, Kuhlman B, Callender D . A large scale test of computational protein design: folding and stability of nine completely redesigned globular proteins. . J. Mol. Biol. . 332 . 2 . 449–60 . 2003 . 12948494 . 10.1016/S0022-2836(03)00888-X . etal. 10.1.1.66.8110 .
• Gerhard DS, Wagner L, Feingold EA . The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 . etal.
• Dantas G, Corrent C, Reichow SL . High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design. . J. Mol. Biol. . 366 . 4 . 1209–21 . 2007 . 17196978 . 10.1016/j.jmb.2006.11.080 . 3764424. etal.

External links

• The MEROPS online database for peptidases and their inhibitors: M14.002

Notes and References

1. Catasus L, Vendrell J, Aviles FX, Carreira S, Puigserver A, Billeter M . The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis, and three-dimensional model . J Biol Chem . 270 . 12 . 6651–7 . Apr 1995 . 7896805 . 10.1074/jbc.270.12.6651. free .
2. Hayashida S, Yamasaki K, Asada Y, Soeda E, Niikawa N, Kishino T . Construction of a physical and transcript map flanking the imprinted MEST/PEG1 region at 7q32 . Genomics . 66 . 2 . 221–5 . Aug 2000 . 10860668 . 10.1006/geno.2000.6206 .
3. Web site: Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic).