Carboxypeptidase A2
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| Carboxypeptidase A2 (pancreatic) | |||||||||||||
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 PDB rendering based on 1aye. | |||||||||||||
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| Identifiers | |||||||||||||
| Symbol | CPA2 | ||||||||||||
| External IDs | OMIM: 600688 MGI: 3617840 HomoloGene: 37541 ChEMBL: 4939 GeneCards: CPA2 Gene | ||||||||||||
| EC number | 3.4.17.15 | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 1358 | 232680 | |||||||||||
| Ensembl | ENSG00000158516 | ENSMUSG00000071553 | |||||||||||
| UniProt | P48052 | Q504N0 | |||||||||||
| RefSeq (mRNA) | NM_001869 | NM_001024698 | |||||||||||
| RefSeq (protein) | NP_001860 | NP_001019869 | |||||||||||
| Location (UCSC) | Chr 7: 129.91 – 129.93 Mb | Chr 6: 30.54 – 30.56 Mb | |||||||||||
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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
- ↑ Catasus L, Vendrell J, Aviles FX, Carreira S, Puigserver A, Billeter M (Apr 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.
- ↑ Hayashida S, Yamasaki K, Asada Y, Soeda E, Niikawa N, Kishino T (Aug 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.
- ↑ 3.0 3.1 "Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic)".
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. doi:10.1111/j.1432-1033.1989.tb14590.x. PMID 2920728.
- 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. PMC 1170294. 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. doi:10.1016/S0014-5793(97)01476-2. 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.
- 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. PMC 139241. 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. doi:10.1110/ps.0227303. PMC 2312417. 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. doi:10.1016/S0022-2836(03)00888-X. 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. PMC 528928. 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.
External links
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