Carboxypeptidase A2

From Wikipedia, the free encyclopedia

Carboxypeptidase A2 (pancreatic)

PDB rendering based on 1aye.

Available structures: 1aye, 1dtd, 1o6x

Identifiers

Symbol(s)

CPA2;

External IDs

OMIM: 600688 MGI: 3617840 HomoloGene: 37541

Gene ontology
Molecular Function:	• carboxypeptidase activity • carboxypeptidase A activity • metallopeptidase activity • zinc ion binding • metal ion binding
Biological Process:	• proteolysis • vacuolar protein catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_001869 (mRNA)
NP_001860 (protein)

NM_001024698 (mRNA)
NP_001019869 (protein)

Location

Chr 7: 129.69 - 129.72 Mb

Chr 6: 30.49 - 30.51 Mb

Pubmed search

[1]

[2]

Carboxypeptidase A2 (pancreatic), also known as CPA2, is a human gene.^[1]

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^[1]

[edit] References

^ ^a ^b Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic).

[edit] Further reading

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. PMID 2920728.
Catasús L, Vendrell J, Avilés FX, et al. (1995). "The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis, and three-dimensional model.". J. Biol. Chem. 270 (12): 6651-7. PMID 7896805.
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. PMID 8806703.
García-Sáez I, Reverter D, Vendrell J, et al. (1998). "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. doi:10.1093/emboj/16.23.6906. PMID 9384570.
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. PMID 9450539.
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. PMID 10742178.
Hayashida S, Yamasaki K, Asada Y, et al. (2000). "Construction of a physical and transcript map flanking the imprinted MEST/PEG1 region at 7q32.". Genomics 66 (2): 221-5. doi:10.1006/geno.2000.6206. PMID 10860668.
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. PMID 11743734.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. doi:10.1073/pnas.242603899. PMID 12477932.
Jiménez MA, Villegas V, Santoro J, et al. (2003). "NMR solution structure of the activation domain of human procarboxypeptidase A2.". Protein Sci. 12 (2): 296-305. PMID 12538893.
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. PMID 12948494.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Dantas G, Corrent C, Reichow SL, et al. (2007). "High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design.". J. Mol. Biol. 366 (4): 1209-21. doi:10.1016/j.jmb.2006.11.080. PMID 17196978.