Catalysis of serine oligopeptidases is controlled by a gating filter mechanism

EMBO Reports

Volumn 1, Issue 3, 2000, Pages 277-281

  Fülöp, Vilmos ^a   Szeltner, Zoltán ^b   Polgár, László ^b  

^a UNIVERSITY OF WARWICK   (United Kingdom)

^b INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISULFIDE; GLUTATHIONE DISULFIDE; PROLYL ENDOPEPTIDASE; RECOMBINANT PROTEIN; SERINE PROTEINASE;

AMINO ACID SUBSTITUTION; ANIMAL; ARTICLE; BRAIN; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MUTATION; OXIDATION REDUCTION REACTION; PH; PROTEIN CONFORMATION; SWINE; TEMPERATURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SUBSTITUTION; ANIMALS; BRAIN; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; DISULFIDES; ENZYME STABILITY; GLUTATHIONE DISULFIDE; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MUTATION; OXIDATION-REDUCTION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY; SWINE; TEMPERATURE;

EID: 0034279642     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1093/embo-reports/kvd048     Document Type: Article

References (15)

1. Atack, J.R., Suman-Chauhan, N., Dawson, G. and Kulagowski, J.J. (1991) In vitro and in vivo inhibition of prolyl endopeptidase. Eur. J. Pharmacol., 205, 157-163.
2. Brünger, A.T. (1992a) X-PLOR: Version 3.1, A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT.
3. Brünger, A.T. (1992b) The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-474.
4. Chevalier, S., Goeltz, P., Thibault, P., Banville, D. and Gagnon, J. (1992) Characterization of prolyl oligopeptidase from Flavobacterium meningosepticum. J. Biol. Chem., 267, 8192-8199.
5. Cunningham, D.F. and O'Connor, B. (1997) Proline specific peptidases. Biochim. Biophys. Acta, 1343, 160-186.
6. Esnouf, R.M. (1997) An extensively modified version of MolScript that includes greatly enhanced colouring capabilities. J. Mol Graph., 15, 133-138.
7. Fülöp, V. and Jones, D.T. (1999) β-propellers: structural rigidity and functional diversity. Curr. Opin. Struct. Biol., 9, 715-721.
8. Fülöp, V., Böcskei, Z. and Polgár, L. (1998) Prolyl oligopeptidase: an unusual β-propeller domain regulates proteolysis. Cell, 94, 161-170.
9. Jones, T.A., Zou, J.Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47, 110-119.
10. Szeltner, Z., Renner, V. and Polgdr, L. (2000b) The non-catalytic β-propeller domain of prolyl oligopeptidase enhances the catalytic capability of the peptidase domain. J. Biol. Chem., 275, 15000-15005.
11. Welches, W.R., Brosnihan, K.B. and Ferrario, C.M. (1993) A comparison of the properties and enzymatic activities of three angiotensin processing enzymes: angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase. Life Sci., 52, 1461-1480.
12. Wilk, S. (1983) Prolyl endopeptidase. Life Sci., 33, 2149-2157.
13. Williams, R.S.B., Eames, M., Ryves, W.J., Viggars, J. and Harwood, A.J. (1999) Loss of a prolyl oligopeptidase confers resistance to lithium by elevation of inositol (1,4,5) trisphosphate. EMBO J., 18, 2734-2745.
14. Yoshimoto, T., Kado, K., Matsubara, F., Koriyama, N., Kaneto, H. and Tsuru, D. (1987) Specific inhibitors for prolyl endopeptidase and their antiamnesic effect. J. Pharmacobiodyn., 10, 730-735.
15. Yoshimoto, T., Kanatani, A., Shimoda, T., Inaoka, T., Kobubo, T. and Tsuru, D. (1991) Prolyl endopeptidase from Flavobaterium meningosepticum: cloning and sequencing of the enzyme gene. J. Biochem., 110, 873-878.