Biology:Carboxypeptidase A2
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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[3]
References
- ↑ "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. doi:10.1074/jbc.270.12.6651. PMID 7896805.
- ↑ "Construction of a physical and transcript map flanking the imprinted MEST/PEG1 region at 7q32". Genomics 66 (2): 221–5. Aug 2000. doi:10.1006/geno.2000.6206. PMID 10860668.
- ↑ 3.0 3.1 "Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1358.
Further reading
- "Purification and properties of five different forms of human procarboxypeptidases.". Eur. J. Biochem. 179 (3): 609–16. 1989. doi:10.1111/j.1432-1033.1989.tb14590.x. PMID 2920728.
- "Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2.". Arch. Biochem. Biophys. 332 (1): 8–18. 1996. doi:10.1006/abbi.1996.0310. PMID 8806703.
- "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. doi:10.1093/emboj/16.23.6906. PMID 9384570.
- "Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2.". FEBS Lett. 420 (1): 7–10. 1998. doi:10.1016/S0014-5793(97)01476-2. PMID 9450539.
- "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. doi:10.1038/74092. PMID 10742178.
- "Changes in zinc ligation promote remodeling of the active site in the zinc hydrolase superfamily.". J. Mol. Biol. 314 (5): 1191–207. 2002. doi:10.1006/jmbi.2000.5161. PMID 11743734.
- "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. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "NMR solution structure of the activation domain of human procarboxypeptidase A2.". Protein Sci. 12 (2): 296–305. 2003. doi:10.1110/ps.0227303. PMID 12538893.
- "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. doi:10.1016/S0022-2836(03)00888-X. PMID 12948494.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design.". J. Mol. Biol. 366 (4): 1209–21. 2007. doi:10.1016/j.jmb.2006.11.080. PMID 17196978.
External links
- The MEROPS online database for peptidases and their inhibitors: M14.002
- Overview of all the structural information available in the PDB for UniProt: P48052 (Human Carboxypeptidase A2) at the PDBe-KB.
PDB gallery | |
|---|---|
|
 |  |
