Carboxypeptidase A2

Handbook of Proteolytic Enzymes, Second Edition: Volume 1: Aspartic and Metallo Peptidases

Volumn 1, Issue , 2004, Pages 821-825

  Auld, David S ^a  

^a BOSTON COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 20444413866     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-079611-3.50249-4     Document Type: Chapter

References (35)

1. D.S. Auld (2001) Zinc coordination sphere in biochemical zinc sites. BioMetals 14 271-313.
2. D.S. Auld and B.L. Vallee (1970) Kinetics of carboxypeptidase A. II. Inhibitors of the hydrolysis of oligopeptides. Biochemistry 9 602-609.
3. T.J. Bazzone, M. Sokolovsky, L.B. Cueni and B.L. Vallee (1979) Single step isolation and resolution of pancreatic carboxypeptidase A and B. Biochemistry 18 4362-4366.
4. J.T. Bukrinsky, M.J. Bjerrum and A. Kadziola (1998) Native carboxypeptidase A in a new crystal environment reveals a different conformation of the important tyrosine 248. Biochemistry 37 16555-16564.
5. L. Catasús, J. Vendrell, F.X. Avilés, S. Carreira, A. Puigserver and M. Billeter (1995) The sequence and conformation of human pancreatic procarboxypeptidase A2. J. Biol. Chem. 270 6651-6657.
6. D.W. Christianson and W.N. Lipscomb (1989) Carboxypeptidase A. Acc. Chem. Res. 22 62-69.
7. E. Clauser, S.J. Gardell, C.S. Craik, R.J. MacDonald and W.J. Rutter (1988) Structural characterization of the rat carboxypeptidase A1 and B genes. Comparative analysis of the rat carboxypeptidase gene family. J. Biol. Chem. 263 17837-17845.
8. G.M. Clore, A.M. Gronenborn, M. Nilges and C.A. Ryan (1987) Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry 26 8012-8023.
9. M. Coll, A. Guasch, F.X. Avilés and R. Huber (1991) Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity. EMBO J. 10 1-9.
10. L.B. Cueni, T.J. Bazzone, J.F. Riordan and B.L. Vallee (1980) Affinity chromatographic sorting of carboxypeptidase A and its chemically modified derivatives. Anal. Biochem. 107 341-349.
11. Z. Faming, B. Kobe, C.-B. Stewart, W.J. Rutter and E.J. Goldsmith (1991) Structural evolution of an enzyme specificity. The structure of rat carboxypeptidase A2 at 1.9 Å resolution. J. Biol. Chem. 266 24606-24612.
12. A.M. Fernandez, V. Villegas, J.C. Martinez, N.A. Van Nuland, F. Conejero-Lara, F.X. Avilés, L. Serrano, V.V. Filimonov and P.L. Mateo (2000) Thermodynamic analysis of helix-engineered forms of the activation domain of human procarboxypeptidase A2. Eur. J. Biochem. 267 5891-5899.
13. I. Garcia-Saez, D. Reverter, J. Vendrell, F.X. Avilés and M. Coll (1997) The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen. EMBO J. 16 6906-6913.
14. S.J. Gardell, C.S. Craik, E. Clauser, E.J. Goldsmith, C.-B. Stewart, M. Graff and W.J. Rutter (1988) A novel rat carboxypeptidase, CPA2: characterization, molecular cloning, and evolutionary implications on substrate specificity in the carboxypeptidase gene family. J. Biol. Chem. 263 17828-17836.
15. A. Guasch, M. Coll, F.X. Avilés and R. Huber (1992) Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation. J. Mol. Biol. 224 141-157.
16. L.W. Harrison, D.S. Auld and B.L. Vallee (1975) Intramolecular arsanilazotyrosine-248 Zn complex of carboxypeptidase A: a monitor of catalytic events. Proc. Natl. Acad. Sci. USA 72 3930-3933.
17. R.M. Laethem, T.A. Blumenkopf, M. Cory, L. Elwell, C.P. Moxham, P.H. Ray, L.M. Walton and G.K. Smith (1996) Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2. Arch. Biochem. Biophys. 332 8-18.
18. S.A. Latt, D.S. Auld and B.L. Vallee (1972) Distance measurements at the active site of carboxypeptidase A during catalysis. Biochemistry 11 3015-3022.
19. S. Mangani, P. Carloni and P. Orioli (1992) Crystal structure of the complex between carboxypeptidase A and the biproduct analog inhibitor L-benzylsuccinate at 2.0 Å resolution. J. Mol. Biol. 223 573-578.
20. O. Oppezzo, S. Ventura, T. Bergman, J. Vendrell, H. Jornvall and F.X. Avilés (1994) Procarboxypeptidase in rat pancreas. Overall characterization and comparison of the activation processes. Eur. J. Biochem. 222 55-63.
21. R. Pascual, F.J. Burgos, M. Salva, F. Soriano, E. Mendez and F.X. Avilés (1989) Purification and properties of five different forms of human procarboxypeptidases. Eur. J. Biochem. 179 609-616.
22. F.A. Quiocho and W.N. Lipscomb (1971) Carboxypeptidase A: a protein and an enzyme. Adv. Protein Chem. 25 1-78.
23. D.C. Rees and W.N. Lipscomb (1982) Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 Å resolution. J. Mol Biol. 160 475-498.
24. D.C. Rees, M. Lewis and W.N. Lipscomb (1983) Refined crystal structure of carboxypeptidase A at 1.54 Å resolution. J. Mol. Biol. 168 367-387.
25. D. Reverter, I. Garcia-Saez, L. Catasús, J. Vendrell, M. Coll and F.X. Avilés (1997) Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2. FEBS Lett. 420 7-10.
26. D. Reverter, J. Vendrell, F. Canals, J. Horstmann, F.X. Avilés, H. Fritz and C.P. Sommerhoff (1998) A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis. Isolation, sequence analysis, cDNA cloning, recombinant expression, and characterization. J. Biol. Chem. 273 32927-32933.
27. D. Reverter, S. Ventura, V. Villegas, J. Vendrell and F.X. Avilés (1998) Overexpression of human procarboxypeptidase A2 in Pichia pastoris and detailed characterization of its activation pathway. J. Biol. Chem. 273 3535-3541.
28. D. Reverter, C. Fernandez-Catalan, R. Baumgartner, R. Pfander, R. Huber, W. Bode, J. Vendrell, T.A. Holak and F.X. Avilés (2000) Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2. Nature Struct. Biol. 7 322-328.
29. J.F. Riordan and B. Holmquist (1984) Carboxypeptidase A. H. Bergmeyer (Ed.) Methods of Enzymatic Analysis, 3rd edn, vol. V: Peptidases, Proteinases and Their Inhibitors Berlin: Verlag Chemie 43-60.
30. G. Scheele, D. Bartelt and W. Bieger (1981) Characterization of human exocrine pancreatic proteins by two dimensional isoelectric focusing/sodium dodecyl sulfate gel electrophoresis. Gastroenterology 80 461-473.
31. G.K. Smith, S. Banks, T.A. Blumenkopf, M. Cory, J. Humphreys, R.M. Laethem, J. Miller, C.P. Moxham, R. Mullin, P.H. Ray, L.M. Walton and L.A. Wolfe 3rd. (1997) Toward antibody-directed enzyme prodrug therapy with the T268G mutant of human carboxypeptidase A1 and novel in vivo stable prodrugs of methotrexate. J. Biol. Chem. 272 15804-15816.
32. K. Titani, L.H. Ericsson, K.A. Walsh and H. Neurath (1975) Amino acid sequence of bovine carboxypeptidase B. Proc. Natl. Acad. Sci. USA 72 1666-1670.
33. B.L. Vallee and D.S. Auld (1990) Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29 5647-5659.
34. J. Vendrell, E. Querol and F.X. Avilés (2000) Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties. Biochim. Biophys. Acta 1477 284-298.
35. V. Villegas, J.C. Martinez, F.X. Avilés and L. Serrano (1998) Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain. J. Mol. Biol. 283 1027-1036.