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CPA1  -  carboxypeptidase A1 (pancreatic)

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Disease relevance of CPA1

 

High impact information on CPA1

  • Human mast cell carboxypeptidase resembled bovine carboxypeptidase A with respect to hydrolysis of synthetic dipeptides and angiotensin I, but was distinguished from carboxypeptidase A in its inability to hydrolyze des-Arg9 bradykinin [6].
  • Studies using pure enzymes showed that bovine carboxypeptidase A hydrolyzed the cholyl conjugates of the neutral L-alpha-amino acids with similar specificity as observed for the human pancreatic juice, whereas bovine carboxypeptidase B cleaved the basic amino acid conjugates [7].
  • Carboxypeptidase A digestion of isolated alpha chains liberated about 0.3 equivalent of tyrosine [8].
  • This pattern of selectivity might be attributable to a limited homology of a 11-amino acid sequence with sequences within the activation segments of CPA and CPB known to interact with residues within their active sites [1].
  • TCI appears as a hardly reversible, non-competitive, and potent inhibitor of CPA1 and CPA2 (Ki approximately 3 nM) and mast-cell CPA (Ki = 16 nM) and inactive on various other proteases [1].
 

Biological context of CPA1

  • Evolutionary trees built from the amino acid sequences of the known pancreatic carboxypeptidases show that CPA2 and carboxypeptidase A1 (CPA1) are the products of genes which duplicated before the mammalian radiation, and that bovine CPA is of the A1 type [9].
  • We also report the partial nucleotide sequence of the rat CPA1 gene [10].
  • Conserved sequences in the 5' flanking regions of the rat CPA1, CPA2, CPB, and other pancreas-specific genes have been identified [10].
  • At 5.5-A resolution, the multiple isomorphous replacement map was readily interpretable in terms of the known native carboxypeptidase A structure plus extra density around the active site [11].
  • The substrate specificities of CPA1 and CPA2 isolated from rat pancreas are similar to bovine CPA in that carboxyl-terminal amino acids with aromatic or branched aliphatic side chains are preferred [9].
 

Anatomical context of CPA1

 

Associations of CPA1 with chemical compounds

 

Regulatory relationships of CPA1

 

Other interactions of CPA1

  • Carboxypeptidase E is a member of the carboxypeptidase A and B gene family, with many of the putative active-site and substrate-binding residues conserved between these enzymes [21].
  • The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes [22].
  • Simple intrasequence difference (SID) analysis: an original method to highlight and rank sub-structural interfaces in protein folds. Application to the folds of bovine pancreatic trypsin inhibitor, phospholipase A2, chymotrypsin and carboxypeptidase A [3].
  • The distance of migration into the gel of PGs incubated overnight with cathepsin B, carboxypeptidase A, papain, plasmin, elastase, or cathepsin G varied with the size of the cleavage products [23].
  • This is confirmed by treatment of profilin (+Tyr) with carboxypeptidase A, which removes the C-terminal tyrosine (rapidly) and the penultimate glutamine residue (slowly), and thereby converts it to the other form as judged by chromatography on phosphocellulose [24].
 

Analytical, diagnostic and therapeutic context of CPA1

References

  1. Purification, cDNA cloning, functional expression, and characterization of a 26-kDa endogenous mammalian carboxypeptidase inhibitor. Normant, E., Martres, M.P., Schwartz, J.C., Gros, C. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  2. Phenylpropynal, a specific, irreversible, non-beta-lactam inhibitor of beta-lactamases. Schenkein, D.P., Pratt, R.F. J. Biol. Chem. (1980) [Pubmed]
  3. Simple intrasequence difference (SID) analysis: an original method to highlight and rank sub-structural interfaces in protein folds. Application to the folds of bovine pancreatic trypsin inhibitor, phospholipase A2, chymotrypsin and carboxypeptidase A. Pritchard, L., Cardle, L., Quinn, S., Dufton, M. Protein Eng. (2003) [Pubmed]
  4. Crystallization and properties of carboxypeptidase A gamma from porcine pancreas. Koide, A., Yoshizawa, M., Kurachi, K. Eur. J. Biochem. (1981) [Pubmed]
  5. The complete amino acid sequence of human brain-derived acidic fibroblast growth factor. Gimenez-Gallego, G., Conn, G., Hatcher, V.B., Thomas, K.A. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
  6. Human mast cell carboxypeptidase. Purification and characterization. Goldstein, S.M., Kaempfer, C.E., Kealey, J.T., Wintroub, B.U. J. Clin. Invest. (1989) [Pubmed]
  7. Pancreatic carboxypeptidase hydrolysis of bile acid-amino conjugates: selective resistance of glycine and taurine amidates. Huijghebaert, S.M., Hofmann, A.F. Gastroenterology (1986) [Pubmed]
  8. Modification of tubulin by tyrosylation in cells and extracts and its effect on assembly in vitro. Raybin, D., Flavin, M. J. Cell Biol. (1977) [Pubmed]
  9. A novel rat carboxypeptidase, CPA2: characterization, molecular cloning, and evolutionary implications on substrate specificity in the carboxypeptidase gene family. Gardell, S.J., Craik, C.S., Clauser, E., Goldsmith, E.J., Stewart, C.B., Graf, M., Rutter, W.J. J. Biol. Chem. (1988) [Pubmed]
  10. Structural characterization of the rat carboxypeptidase A1 and B genes. Comparative analysis of the rat carboxypeptidase gene family. Clauser, E., Gardell, S.J., Craik, C.S., MacDonald, R.J., Rutter, W.J. J. Biol. Chem. (1988) [Pubmed]
  11. Structure of potato inhibitor complex of carboxypeptidase A at 5.5-A resolution. Rees, D.C., Lipscomb, W.N. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  12. Purification and molecular characterization of two inhibitors of yeast proteinase B. Maier, K., Müller, H., Holzer, H. J. Biol. Chem. (1979) [Pubmed]
  13. Purification and characterization of carboxypeptidase A from rat skeletal muscle. Bodwell, J.E., Meyer, W.L. Biochemistry (1981) [Pubmed]
  14. Transmembrane topography of the mitochondrial phosphate carrier explored by peptide-specific antibodies and enzymatic digestion. Capobianco, L., Brandolin, G., Palmieri, F. Biochemistry (1991) [Pubmed]
  15. Comparative development and merozoite production of two isolates of Sarcocystis neurona and Sarcocystis falcatula in cultured cells. Speer, C.A., Dubey, J.P., Mattson, D.E. J. Parasitol. (2000) [Pubmed]
  16. The amino acid sequence of the activation peptide of bovine pro-carboxypeptidase A. Wade, R.D., Hass, G.M., Kumar, S., Walsh, K.A., Neurath, H. Biochimie (1988) [Pubmed]
  17. Zinc environment and cis peptide bonds in carboxypeptidase A at 1.75-A resolution. Rees, D.C., Lewis, M., Honzatko, R.B., Lipscomb, W.N., Hardman, K.D. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  18. Metorphamide: isolation, structure, and biologic activity of an amidated opioid octapeptide from bovine brain. Weber, E., Esch, F.S., Böhlen, P., Paterson, S., Corbett, A.D., McKnight, A.T., Kosterlitz, H.W., Barchas, J.D., Evans, C.J. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  19. Amino-acid sequence of bovine carboxypeptidase B. Titani, K., Ericsson, L.H., Walsh, K.A., Neurath, H. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  20. Immobilized carboxypeptidase A as a probe for studying the thermally induced unfolding of bovine pancreatic ribonuclease. Burgess, A.W., Weinstein, L.I., Gabel, D., Scheraga, H.A. Biochemistry (1975) [Pubmed]
  21. Regulation of carboxypeptidase E. Effect of pH, temperature and Co2+ on kinetic parameters of substrate hydrolysis. Greene, D., Das, B., Fricker, L.D. Biochem. J. (1992) [Pubmed]
  22. The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes. Bode, W., Greyling, H.J., Huber, R., Otlewski, J., Wilusz, T. FEBS Lett. (1989) [Pubmed]
  23. Agarose/polyacrylamide minislab gel electrophoresis of intact cartilage proteoglycans and their proteolytic degradation products. Varelas, J.B., Zenarosa, N.R., Froelich, C.J. Anal. Biochem. (1991) [Pubmed]
  24. The profilin--actin complex: further characterization of profilin and studies on the stability of the complex. Malm, B., Larsson, H., Lindberg, U. J. Muscle Res. Cell. Motil. (1983) [Pubmed]
  25. Isolation and structure of a C-terminally amidated nonopioid peptide, amidorphin-(8-26), from bovine striatum: a major product of proenkephalin in brain but not in adrenal medulla. Liebisch, D.C., Weber, E., Kosicka, B., Gramsch, C., Herz, A., Seizinger, B.R. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  26. Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: contribution of the fourth disulfide bond. Arolas, J.L., Popowicz, G.M., Bronsoms, S., Aviles, F.X., Huber, R., Holak, T.A., Ventura, S. J. Mol. Biol. (2005) [Pubmed]
  27. Novel bifunctional hyperthermostable carboxypeptidase/aminoacylase from Pyrococcus horikoshii OT3. Ishikawa, K., Ishida, H., Matsui, I., Kawarabayasi, Y., Kikuchi, H. Appl. Environ. Microbiol. (2001) [Pubmed]
  28. The ovine pancreatic protein which binds insulin-like growth factor binding protein-3 is procarboxypeptidase A. Fowke, P.J., Hodgkinson, S.C. J. Endocrinol. (1996) [Pubmed]
 
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