The Acylaminoacyl Peptidase from Aeropyrum pernix K1 Thought to Be an Exopeptidase Displays Endopeptidase Activity

Journal of Molecular Biology

Volumn 368, Issue 2, 2007, Pages 509-520

  Kiss, András L ^a   Hornung, Balázs ^b   Rádi, Krisztina ^b   Gengeliczki, Zsolt ^b   Sztáray, Bálint ^b   Juhász, Tünde ^a   Szeltner, Zoltán ^a   Harmat, Veronika ^b   Polgár, László ^a  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b EÖTVÖS LORÁND UNIVERSITY   (Hungary)

Author keywords

inhibitor binding; kinetics; substrate specificity; thermophilic oligopeptidase; X ray crystallography

Indexed keywords

4 NITROPHENYLPHOSPHATASE; ACYLAMINOACYL PEPTIDASE; ALANINE; AMINO ACID; EXOPEPTIDASE; GENE PRODUCT; K1 PROTEIN; OLIGOPEPTIDE; PHENYLALANINE; PROTEINASE; UNCLASSIFIED DRUG;

AEROPYRUM; AEROPYRUM PERNIX; ARTICLE; BINDING SITE; CONFORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ELECTRICITY; ENZYME ACTIVITY; HYDROGEN BOND; HYDROPHOBICITY; LIGAND BINDING; NONHUMAN; PLASTICITY; PRIORITY JOURNAL; PROTEIN DEGRADATION;

AEROPYRUM PERNIX; MAMMALIA;

EID: 33947724046     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.02.025     Document Type: Article

References (35)

1. Jones W.M., Scaloni A., and Manning J.M. Acylaminoacyl-peptidase. Methods Enzymol. 244 (1994) 227-231
2. Rawlings N.D., Polgár L., and Barrett A.J. A new family of serine-type peptidases related to prolyl oligopeptidase. Biochem. J. 279 (1991) 907-908
3. Polgár L. The prolyl oligopeptidase family. Cell. Mol. Life Sci. 59 (2002) 349-362
4. Rosenblum J.S., and Kozarich J.W. Prolyl peptidases: a serine protease subfamily with high potential for drug discovery. Curr. Opin. Chem. Biol. 7 (2003) 496-504
5. Venalainen J.I., Juvonen R.O., and Mannisto P.T. Evolutionary relationships of the prolyl oligopeptidase family enzymes. Eur. J. Biochem. 271 (2004) 2705-2715
6. Fülöp V., Böcskei Z., and Polgár L. Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis. Cell 94 (1998) 161-170
7. Feese M., Scaloni A., Jones W.M., Manning J.M., and Remington S.J. Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase. J. Mol. Biol. 233 (1993) 546-549
8. Wright H., Kiss A.L., Szeltner Z., Polgár L., and Fülöp V. Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase. Acta Crystallog. sect. F 61 (2005) 942-944
9. Bartlam M., Wang G., Yang H., Gao R., Zhao X., Xie G., et al. Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1. Structure 12 (2004) 1481-1488
10. Bender M.L., and Kezdy J. Mechanism of action of proteolytic enzymes. Annu. Rev. Biochem. 34 (1965) 49-76
11. Blanchard J.S. Buffers for enzymes. Methods Enzymol. 104 (1984) 404-414
12. Kiss A.L., Szeltner Z., Fülöp V., and Polgár L. His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate. FEBS Letters 571 (2004) 17-20
13. Szeltner Z., Rea D., Renner V., Juliano L., Fülöp V., and Polgár L. Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding. J. Biol. Chem. 278 (2003) 48786-48793
14. Szeltner Z., Rea D., Renner V., Fülöp V., and Polgár L. Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site. J. Biol. Chem. 277 (2002) 42613-42622
15. Wang Q., Yang G., Liu Y., and Feng Y. Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic aeropyrum pernix K1 by single mutation. J. Biol. Chem 281 (2006) 18618-18625
16. Perrier J., Durand A., Giardina T., and Puigserver A. Catabolism of intracellular N-terminal acetylated proteins: involvement of acylpeptide hydrolase and acylase. Biochimie 87 (2005) 673-685
17. Aertgeerts K., Levin I., Shi L., Snell G.P., Jennings A., Prasad G.S., et al. Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha. J. Biol. Chem. 280 (2005) 19441-19444
18. Kobayashi K., and Smith J.A. Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction. J. Biol. Chem. 262 (1987) 11435-11445
19. Nashed N.T., Louis J.M., Sayer J.M., Wondrak E. M., Mora P.T., Oroszlan S., and Jerina D.M. Continuous spectrophotometric assay for retroviral proteases of HIV-1 and AMV. Biochem. Biophys. Res. Commun. 163 (1989) 1079-1085
20. Richards A.D., Phylip L.H., Farmerie W.G., Scarborough P.E., Alvarez A., Dunn B.M., et al. Sensitive, soluble chromogenic substrates for HIV-1 proteinase. J. Biol. Chem. 265 (1990) 7733-7736
21. Polgár L., Szeltner Z., and Boros I. Substrate-dependent mechanisms in the catalysis of human immunodeficiency virus protease. Biochemistry 33 (1994) 9351-9357
22. Polgár L. The catalytic triad of serine peptidases. Cell. Mol. Life Sci. 62 (2005) 2161-2172
23. Fülöp V., Szeltner Z., Renner V., and Polgár L. Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue. J. Biol. Chem. 276 (2001) 1262-1266
24. James M.N., Sielecki A.R., Brayer G.D., Delbaere L. T., and Bauer C.A. Structures of product and inhibitor complexes of Streptomyces griseus protease A at 1.8 Å resolution. A model for serine protease catalysis. J. Mol. Biol. 144 (1980) 43-88
25. Carter P., and Wells J.A. Functional interaction among catalytic residues in subtilisin BPN'. Proteins: Struct. Funct. Genet. 7 (1990) 335-342
26. Engel M., Hoffmann T., Wagner L., Wermann M., Heiser U., Kiefersauer R., et al. The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism. Proc. Natl Acad. Sci. USA 100 (2003) 5063-5068
27. Leatherbarrow R.J. Grafit, Version 5.0, Erithacus Software Ltd (2001), Horley, UK
28. Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 26 (1993) 795-800
29. Vagin A.A., and Treplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallog. 30 (1997) 1022-1025
30. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
31. Winn M., Isupov M., and Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallog. sect. D 57 (2001) 122-133
32. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
33. Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
34. Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
35. Berman H.M., Westbrook J., Feng Z., Gilliland G., Bhat T.N., Weissig H., et al. The Protein Data Bank. Nucl. Acids Res. 28 (2000) 235-242