Gene Symbol: CPA2
Description: carboxypeptidase A2
Alias: carboxypeptidase A2, carboxypeptidase A2 (pancreatic)
Species: human
Products:     CPA2

Top Publications

  1. Garcia Saez I, Reverter D, Vendrell J, Aviles F, Coll M. The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen. EMBO J. 1997;16:6906-13 pubmed
    ..The derived structural features explain the intrinsic activity of A1/A2 pro-enzymes for small substrates. ..
  2. Dantas G, Kuhlman B, Callender D, Wong M, Baker D. A large scale test of computational protein design: folding and stability of nine completely redesigned globular proteins. J Mol Biol. 2003;332:449-60 pubmed
    ..These encouraging results indicate that the computational protein design methods can, with significant reliability, identify amino acid sequences compatible with a target protein backbone. ..
  3. Masrati G, Dwivedi M, Rimon A, Gluck Margolin Y, Kessel A, Ashkenazy H, et al. Broad phylogenetic analysis of cation/proton antiporters reveals transport determinants. Nat Commun. 2018;9:4205 pubmed publisher
    ..CPAs are commonly divided into two main groups, CPA1 and CPA2, and are further characterized by two main phenotypes: ion selectivity and electrogenicity...
  4. Lyons P, Fricker L. Substrate specificity of human carboxypeptidase A6. J Biol Chem. 2010;285:38234-42 pubmed publisher for CPA enzymes shows a gradient of specificity across the subfamily, from the very restricted specificity of CPA2 to the very broad activity of CPA4...
  5. Song Y, Wang Q, Wang D, Junqiang Li -, Yang J, Li H, et al. Label-Free Quantitative Proteomics Unravels Carboxypeptidases as the Novel Biomarker in Pancreatic Ductal Adenocarcinoma. Transl Oncol. 2018;11:691-699 pubmed publisher
    ..the dysregulation of a set of four proteins in the carboxypeptidase family: carboxypeptidase A1 (CPA1), A2 (CPA2), B1 (CPB1), and chymotrypsin C (CTRC)...
  6. Son S, Kim H, Yun H, Kim D, Ullah S, Kim S, et al. (E)-2-Cyano-3-(substituted phenyl)acrylamide analogs as potent inhibitors of tyrosinase: A linear β-phenyl-α,β-unsaturated carbonyl scaffold. Bioorg Med Chem. 2015;23:7728-34 pubmed publisher
    ..Results from the docking simulation indicated that CPA2 could bind directly to the active site of mushroom tyrosinase and the binding affinity of CPA2 for tyrosinase might ..
  7. Liu C, Yang W, Devidas M, Cheng C, Pei D, Smith C, et al. Clinical and Genetic Risk Factors for Acute Pancreatitis in Patients With Acute Lymphoblastic Leukemia. J Clin Oncol. 2016;34:2133-40 pubmed publisher the genome-wide association study, but a rare nonsense variant rs199695765 in CPA2, encoding carboxypeptidase A2, was highly associated with pancreatitis (hazard ratio, 587; 95% CI, 66.8 to 5166; P = 9.0 × 10(-9))...
  8. Ait Bahadou S, Ouijja A, Karfach A, Tahiri A, Lahlali R. New potential bacterial antagonists for the biocontrol of fire blight disease (Erwinia amylovora) in Morocco. Microb Pathog. 2018;117:7-15 pubmed publisher
    ..and ACBP2), Serratia (HC4), Brevibacterium (SF3, SF4, SF7, and SF15), Pseudomonas (SP9), and Bacillus (CPa12, CPa2, HF6, JB2, LMR2, SF14, SF16, SP10, SP13, and SP18)...
  9. Chintapalli V, Kato A, Henderson L, Hirata T, Woods D, Overend G, et al. Transport proteins NHA1 and NHA2 are essential for survival, but have distinct transport modalities. Proc Natl Acad Sci U S A. 2015;112:11720-5 pubmed publisher
    ..Under salt stress, knockdown of either gene decreases survival, demonstrating a key role for the CPA2 family in ion homeostasis...

More Information


  1. Reverter D, Fernandez Catalan C, Baumgartner R, Pfänder R, Huber R, Bode W, et al. Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2. Nat Struct Biol. 2000;7:322-8 pubmed
    ..The structures of LCI free and bound to carboxypeptidase A2 (CPA2)have been determined by NMR and X-ray crystallography, respectively...
  2. Szmola R, Bence M, Carpentieri A, Szabo A, Costello C, Samuelson J, et al. Chymotrypsin C is a co-activator of human pancreatic procarboxypeptidases A1 and A2. J Biol Chem. 2011;286:1819-27 pubmed publisher
    Human digestive carboxypeptidases CPA1, CPA2, and CPB1 are secreted by the pancreas as inactive proenzymes containing a 94-96-amino acid-long propeptide...
  3. D Silva N, Donini A, O Donnell M. The roles of V-type H+-ATPase and Na+/K+-ATPase in energizing K+ and H+ transport in larval Drosophila gut epithelia. J Insect Physiol. 2017;98:284-290 pubmed publisher
    ..gradients established by the VA in the latter regions, consistent with the presence of a Cation-Proton Antiporter (CPA2) identified in other insect epithelia...
  4. Szabo A, Pilsak C, Bence M, Witt H, Sahin Toth M. Complex Formation of Human Proelastases with Procarboxypeptidases A1 and A2. J Biol Chem. 2016;291:17706-16 pubmed publisher
    ..CELA2A, CELA3A, and CELA3B; chymotrypsinogens CTRB1, CTRB2, CTRC, and CTRL1; and procarboxypeptidases CPA1, CPA2, and CPB1...
  5. Yang Y, Jin L, Zhang J, Wang J, Zhao X, Wu G, et al. High HSF4 expression is an independent indicator of poor overall survival and recurrence free survival in patients with primary colorectal cancer. IUBMB Life. 2017;69:956-961 pubmed publisher
    ..COL11A2, CLPS, and ARSA and colocalized with PTGER1, ADRB1, PEX12, CLPS, PSEN2, KCNJ5, CPA1, ARSA, PNLIP, IRX4, CPA2, IDUA, BCKDHA, and CTRL. We hypothesized that HSF4 might exert its oncogenic effects in CRC via some of these genes...
  6. Pustovalova Y, Kukić P, Vendruscolo M, Korzhnev D. Probing the Residual Structure of the Low Populated Denatured State of ADA2h under Folding Conditions by Relaxation Dispersion Nuclear Magnetic Resonance Spectroscopy. Biochemistry. 2015;54:4611-22 pubmed publisher
    ..CPMG RD data analysis thus allowed a detailed structural characterization of the ADA2h denatured state under folding conditions not previously achieved for this protein. ..
  7. Catasus L, Vendrell J, Aviles F, 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. 1995;270:6651-7 pubmed
    ..Ten structures of human carboxypeptidase A2 were determined on the basis of each of the two known crystal structures...
  8. Pascual R, Burgos F, Salva M, Soriano F, Mendez E, Aviles F. Purification and properties of five different forms of human procarboxypeptidases. Eur J Biochem. 1989;179:609-16 pubmed
    ..N-terminal extended sequence analysis carried out on these proenzymes confirm that they constitute different isologous forms. ..
  9. Laethem R, Blumenkopf T, Cory M, Elwell L, Moxham C, Ray P, et al. Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2. Arch Biochem Biophys. 1996;332:8-18 pubmed
    ..of a human pancreatic cDNA library with cDNA probes that encoded either rat carboxypeptidase A1 (rCPA1) or carboxypeptidase A2 (rCPA2) was used to clone the human prepro-CPA homologs...
  10. Cerdà Costa N, de la Arada I, Aviles F, Arrondo J, Villegas S. Influence of aggregation propensity and stability on amyloid fibril formation as studied by Fourier transform infrared spectroscopy and two-dimensional COS analysis. Biochemistry. 2009;48:10582-90 pubmed publisher
  11. Wouters M, Husain A. Changes in zinc ligation promote remodeling of the active site in the zinc hydrolase superfamily. J Mol Biol. 2001;314:1191-207 pubmed
    ..Some residues important to the catalytic mechanism are not conserved amongst members. We discuss how molecules acting in trans may have facilitated the mutation of catalytically important residues in the active site in this group. ..
  12. Yin Z, Yang C, Long C, Li A. Influence of surface properties of RO membrane on membrane fouling for treating textile secondary effluent. Environ Sci Pollut Res Int. 2017;24:16253-16262 pubmed publisher
    ..on membrane fouling, the performances of three commercial polyamide thin-film composite RO membranes (BW30-4040, CPA2-4040, and RE-4040-FEN) with different roughness and hydrophilicity were investigated for treating textile SE...
  13. Nakano E, Geisz A, Masamune A, Niihori T, Hamada S, Kume K, et al. Variants in pancreatic carboxypeptidase genes CPA2 and CPB1 are not associated with chronic pancreatitis. Am J Physiol Gastrointest Liver Physiol. 2015;309:G688-94 pubmed publisher
    ..Besides CPA1, there are two other human pancreatic carboxypeptidases (CPA2 and CPB1). Here we examined whether CPA2 and CPB1 alterations are associated with CP in Japan and Germany...
  14. Jiménez M, Villegas V, Santoro J, Serrano L, Vendrell J, Aviles F, et al. NMR solution structure of the activation domain of human procarboxypeptidase A2. Protein Sci. 2003;12:296-305 pubmed
    ..0 and 298K is 4.9 +/- 0.3 kcal.mole(-1), in good agreement with the values determined by thermal or denaturant unfolding studies. ..
  15. 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. 2000;66:221-5 pubmed
    ..This integrated physical and transcript map provides a valuable resource for identification of an imprinted gene(s) in this region as well as a candidate gene(s) for autistic disorder. ..
  16. Dantas G, Corrent C, Reichow S, Havranek J, Eletr Z, Isern N, et al. High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design. J Mol Biol. 2007;366:1209-21 pubmed
  17. Reverter D, Garcia Saez I, Catasus L, Vendrell J, Coll M, Aviles F. Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2. FEBS Lett. 1997;420:7-10 pubmed
    ..The hydrolytic action of carboxypeptidase A2 on peptide substrates with different lengths and residues at the C-terminus was analysed, and a preference ..