Microscopic rate-constants for substrate binding and acylation in cold-adaptation of trypsin I from Atlantic cod

FEBS Letters

Volumn 580, Issue 19, 2006, Pages 4639-4644

  Ásgeirsson, Bjarni ^a   Cekan, Pavol ^a  

^a UNIVERSITY OF ICELAND   (Iceland)

Author keywords

Cold adaptation; Gadus morhua; Kinetics; Psychrophilic; Rate constants; Serine proteinase

Indexed keywords

ANILIDE; TRYPSIN; TRYPSIN I; UNCLASSIFIED DRUG;

ACYLATION; ARTICLE; ATLANTIC COD; CATALYSIS; COLD ACCLIMATIZATION; DISSOCIATION CONSTANT; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; MICROSCOPY; PRIORITY JOURNAL; WATER TEMPERATURE;

ACYLATION; ADAPTATION, PHYSIOLOGICAL; ANIMALS; COLD; FISHES; HYDROLYSIS; KINETICS; SUBSTRATE SPECIFICITY; TRYPSIN;

BOS TAURUS; GADUS MORHUA;

EID: 33746887076     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.07.043     Document Type: Article

References (48)

1. Low P.S., and Somero G.N. Temperature adaptation of enzymes: a proposed molecular basis for the different catalytic efficiencies of enzymes from ectotherms and endotherms. Comp. Biochem. Physiol. B (1974) 307-312
2. Johnston I.A. Cold adaptation in marine organisms. Philos. Trans. R. Soc. Lond. B 326 (1990) 655-667
3. Feller G., and Gerday C. Psychrophilic enzymes: hot topics in cold adaptation. Nat. Rev. Microbiol. 1 (2003) 200-208
4. Somero G.N. Adaptation of enzymes to temperature: searching for basic "strategies". Comp. Biochem. Physiol. 139 (2004) 321-333
5. Ayala Y.M., and Di Cera E. A simple method for the determination of individual rate constants for substrate hydrolysis by serine proteases. Protein Sci. 9 (2000) 1589-1593
6. Bobofchak K.M., Pineda A.O., Mathews F.S., and Di Cera E. Energetic and structural consequences of perturbing Gly-193 in the oxyanion hole of serine proteases. J. Biol. Chem. 280 (2005) 25644-25650
7. Kraut J. Serine proteases: structure and mechanism of catalysis. Ann. Rev. Biochem. 46 (1977) 331-358
8. Neurath H. Evolution of proteolytic enzymes. Science 224 (1984) 350-357
9. Halfon S., and Craik C.S. Trypsin. In: Barrett A.J., Rawlings N.D., and Woessner J.F. (Eds). Handbook of Proteolytic Enzymes (1998), Academic Press, London 12-21
10. Lesk A.M., and Fordham W.D. Conservation and variability in the structures of serine proteinases of the chymotrypsin family. J. Mol. Biol. 258 (1996) 501-537
11. 15N NMR spectroscopy of hydrogen-bonding interactions in the active site of serine proteases: evidence for a moving histidine mechanism. Biochemistry 25 (1986) 7751-7759
12. Nakagawa S., Yu H.A., Karplus M., and Umeyama H. Active site dynamics of acyl-chymotrypsin. Proteins - Struct. Funct. Genet. 16 (1993) 172-194
13. Dufton M.J. Could domain movements be involved in the mechanism of trypsin-like serine proteases?. FEBS Lett. 271 (1990) 9-13
14. Perona J.J., and Craik C.S. Structural basis of substrate specificity in the serine proteases. Protein Sci. 4 (1995) 337-360
15. Simpson B.K., and Haard N.F. Purification and characterization of the trypsin from the Greenland cod (Gadus ogac). 1. Kinetic and thermodynamic characteristics. Can. J. Biochem. Cell Biol. 62 (1984) 894-900
16. Genicot S., Feller G., and Gerday C.H. Trypsin from antarctic fish (Paranotothenia magellanica Forster) as compared with trout (Salmo gairdneri) trypsin. Comp. Biochem. Physiol. B 90 (1988) 601-609
17. Ásgeirsson B., Fox J.W., and Bjarnason J.B. Purification and characterization of trypsin from the poikilotherm Gadus morhua. Eur. J. Biochem. 180 (1989) 85-94
18. Ásgeirsson B., and Bjarnason J.B. Structural and kinetic properties of chymotrypsin from Atlantic cod (Gadus morhua). Comparison with bovine chymotrypsin. Comp. Biochem. Physiol. B 99 (1991) 327-335
19. Outzen H., Berglund G.I., Smalås A.O., and Willassen N.P. Temperature and pH sensitivity of trypsins from Atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin. Comp. Biochem. Physiol. B 115 (1996) 33-45
20. Kristjánsson M.M., Ásgeirsson B., and Bjarnason J.B. Serine proteinases from cold-adapted organisms. Adv. Exp. Med. Biol. 415 (1997) 27-46
21. Ásgeirsson B., and Bjarnason J.B. Properties of elastase from Atlantic cod, a cold-adapted proteinase. Biochim. Biophys. Acta 1164 (1993) 91-100
22. Zerner B., and Bender M.L. The kinetic consequences of the acyl-enzyme mechanism for the reactions of specific substrates with chymotrypsin. J. Am. Chem. Soc. 86 (1964) 3669-3674
23. Osnes K.K., and Mohr V. On the purification and characterization of three anionic, serine-type peptide hydrolyses from antarctic krill, Euphausia superba. Comp. Biochem. Physiol. B 82 (1985) 607-619
24. Erlanger B.F., Edel F., and Cooper A.G. The action of chymotrypsin on two new chromogenic substrates. Arch. Biochem. Biophys. 210 (1966) 206-210
25. Lonhienne T., Gerday C., and Feller G. Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta 1543 (2000) 1-10
26. Zimmerman M., Ashe B., Yurewicz E.C., and Patel G. Sensitive assays for trypsin, elastase, and chymotrypsin using new fluorogenic substrates. Anal. Biochem. 78 (1977) 47-51
27. Corey D.R., and Craik C.S. An investigation into the minimum requirements for peptide hydrolysis by mutation of the catalytic triad of trypsin. J. Am. Chem. Soc. 114 (1992) 1784-1790
28. Higaki J.N., Haymore B.L., Chen S., Fletterick R.J., and Craik C.S. Regulation of serine protease activity by an engineered metal switch. Biochemistry 29 (1990) 8582-8586
29. Sahin-Toth M. Human cationic trypsinogen: role of Asn21 in zymogen activation and implications in hereditary pancreatitis. J. Biol. Chem. 275 (2000) 22750-22755
30. Kukor Z., Toth M., and Sahin-Toth M. Human anionic trypsinogen: properties of autocatalytic activation and degradation and implications in pancreatic diseases. Eur. J. Biochem. 270 (2003) 2047-2058
31. Schechter I., and Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27 (1967) 157-162
32. Stein R.L., and Strimpler A.M. P1 residue determines the operation of the catalytic triad of serine proteases during hydrolysis of acyl-enzymes. J. Am. Chem. Soc. 109 (1987) 4387-4390
33. Czapinska H., and Otlewski J. Structural and energetic determinants of the S1-site specificity in serine proteases. Eur. J. Biochem. 260 (1999) 571-595
34. Hedstrom L. Trypsin: a case study in the structural determinants of enzyme specificity. Biol. Chem. 377 (1996) 465-470
35. Hedstrom L. Serine protease mechanism and specificity. Chem. Rev. 102 (2002) 4501-4524
36. Krowarsch D., Dadlez M., Buczek O., Krokoszynska I., Smalås A.O., and Otlewski J. Interscaffolding additivity: binding of P1 variants of bovine pancreatic trypsin inhibitor to four serine proteases. J. Mol. Biol. 289 (1999) 175-186
37. Grzesiak A., Helland R., Smalas A.O., Krowarsch D., Dadlez M., and Otlewski J. Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases. J. Mol. Biol. 301 (2000) 205-217
38. Georlette D., Blaise V., Collins T., D'Amico S., Gratia E., Hoyoux A., Marx J.-C., Sonan G., Feller G., and Gerday C. Some like it cold: biocatalysis at low temperatures. FEMS Microbiol. Rev. 28 (2004) 25-42
39. Siddiqui K.S., and Cavicchioli R. Cold-adapted enzymes. Ann. Rev. Biochem. 75 (2006) 403-433
40. Leiros H.-K.S., Brandsdal B.O., Andersen O.A., Os V., Leiros I., Helland R., Otlewski J., Willassen N.P., and Smalås A.O. Trypsin specificity as elucidated by LIE calculations, X-ray structures, and association constant measurements. Protein Sci. 13 (2004) 1056-1070
41. Genicot S., Rentierdelrue F., Edwards D., Vanbeeumen J., and Gerday C. Trypsin and trypsinogen from an Antarctic fish: molecular basis of cold adaptation. Biochim. Biophys. Acta 1298 (1996) 45-57
42. Smalås A.O., Heimstad E.S., Hordvik A., Willassen N.P., and Male R. Cold adaption of enzymes: structural comparison between salmon and bovine trypsins. Protein - Struct. Funct. Genet. 20 (1994) 149-166
43. Russell R.J., Gerike U., Danson M.J., Hough D.W., and Taylor G.L. Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium. Structure 6 (1998) 351-361
44. Leiros H.-K.S., Willassen N.P., and Smalås A.O. Structural comparison of psychrophilic and mesophilic trypsins. Elucidating the molecular basis of cold-adaptation. Eur. J. Biochem. 267 (2000) 1039-1049
45. Gorfe A.A., Brandsdal B.O., Leiros H.K., Helland R., and Smalås A.O. Electrostatics of mesophilic and psychrophilic trypsin isoenzymes: qualitative evaluation of electrostatic differences at the substrate binding site. Proteins 40 (2000) 207-217
46. Heimstad E.S., Hansen L.K., and Smalås A.O. Comparative molecular dynamics simulation studies of salmon and bovine trypsins in aqueous solution. Protein Eng. 8 (1995) 379-388
47. Brandsdal B.O., Heimstad E.S., Sylte I., and Smalås A.O. Comparative molecular dynamics of mesophilic and psychrophilic protein homologues studied by 1.2 ns simulations. J. Biomol. Struct. Dyn. 17 (1999) 493-506
48. Graf L., Jancso A., Szilagyi L., Hegyi G., Pinter K., Naray-Szabo G., Hepp J., Medzihradszky K., and Rutter W.J. Electrostatic complementarity within the substrate-binding pocket of trypsin. Proc. Natl. Acad. Sci. USA 85 (1988) 4961-4965