Effect of selected Ser/Ala and Xaa/Pro mutations on the stability and catalytic properties of a cold adapted subtilisin-like serine proteinase

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1774, Issue 6, 2007, Pages 749-755

  Arnórsdóttir, Jóhanna ^a   Helgadóttir, Sunna ^a   Thorbjarnardóttir, Sigrídur H ^a   Eggertsson, Gudmundur ^a   Kristjánsson, Magnús M ^a  

^a UNIVERSITY OF ICELAND   (Iceland)

Author keywords

Cold adaptation; Kinetic properties; Proteinase K; Site directed mutagenesis; Stability; Subtilsin like; Vibrio proteinase

Indexed keywords

ALANINE; PROLINE; SERINE; SERINE PROTEINASE; SUBTILIN; SUBTILIN LIKE SERINE PROTEINASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CATALYST; COLD ACCLIMATIZATION; ENZYME ACTIVITY; ENZYME KINETICS; HIGH TEMPERATURE; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; VIBRIO;

ALANINE; AMINO ACIDS; CATALYSIS; COLD; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MUTATION; PROLINE; PROTEIN STRUCTURE, TERTIARY; SERINE; SUBTILISIN; TEMPERATURE; VIBRIO;

VIBRIO;

EID: 34249848371     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.03.015     Document Type: Article

References (42)

1. Smalås A.O., Leiros H.K., Os V., and Willassen N.P. Cold adapted enzymes. Biotechnol. Annu. Rev. 6 (2000) 1-57
2. 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
3. Kristjánsson M.M., and Ásgeirsson B. Properties of extremophilic enzymes and their importance in Food Science and technology. In: Whitaker J.R., Voragen A.G.J., and Wong D.W.S. (Eds). Handbook of Food Enzymology (2002), Marcel Dekker, Inc, New York 77-100
4. Hochachka P.W., and Somero G.N. Biochemical Adaptation (1984), Princeton Univ. Press, Princeton, NJ
5. Somero G.N. Proteins and temperature. Annu. Rev. Physiol. 57 (1995) 43-68
6. Fields P.A. Review: Protein function at thermal extremes: balancing stability and flexibility. Comp. Biochem. Physiol., A Mol. Integr. Physiol. 129 (2001) 417-431
7. Jaenicke R., and Böhm G. The stability of proteins in extreme environments. Curr. Opin. Struct. Biol. 8 (1998) 738-748
8. Zavodszky P., Kardos J., Svingor A., and Petsko G.A. Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 7406-7411
9. Arnórsdóttir J., Kristjánsson M.M., and Ficner R. Crystal structure of a subtilisin-like serine proteinase from a psychrotrophic Vibrio species reveals structural aspects of cold adaptation. FEBS J. 272 (2005) 832-845
10. Bae E., and Phillips Jr. G.N. Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases. J. Biol. Chem. 279 (2004) 28202-28208
11. Leiros I., Moe E., Lanes O., Smalas A.O., and Willassen N.P. The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features. Acta Crystallogr. Sect. D 59 (2003) 1357-1365
12. Van Petegem F., Collins T., Meuwis M.A., Gerday C., Feller G., and Van Beeumen J. The structure of a cold-adapted family 8 xylanase at 1.3 Å resolution. Structural adaptations to cold and investgation of the active site. J. Biol. Chem. 278 (2003) 7531-7539
13. Aghajari N., Van Petegem F., Villeret V., Chessa J.P., Gerday C., Haser R., and Van Beeumen J. Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. Proteins 50 (2003) 636-647
14. de Backer M., McSweeney S., Rasmussen H.B., Riise B.W., Lindley P., and Hough E. The 1.9 Å crystal structure of heat-labile shrimp alkaline phosphatase. J. Mol. Biol. 318 (2002) 1265-1274
15. Toyota E., Ng K.K., Kuninaga S., Sekizaki H., Itoh K., Tanizawa K., and James M.N. Crystal structure and nucleotide sequence of an anionic trypsin from chum salmon (Oncorhynchus keta) in comparison with Atlantic salmon (Salmo salar) and bovine trypsin. J. Mol. Biol. 324 (2002) 391-397
16. Kim S.Y., Hwang K.Y., Kim S.H., Sung H.C., Han Y.S., and Cho Y. Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum. J. Biol. Chem. 274 (1999) 11761-11767
17. Aghajari N., Feller G., Gerday C., and Haser R. Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level. Structure 6 (1998) 1503-1516
18. Alvarez M., Zeelens J.P., Mainfroid V., Rentier-Delrue F., Martial J.A., Wyns L., Wierenga R.K., and Maes D. Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. J. Biol. Chem. 273 (1998) 2199-2206
19. Russel R.J.M., Gerike U., Danson M.J., Hough D.W., and Taylor G.L. Structural adaptations of the cold active citrate-synthetase from an Antarctic bacterium. Structure 6 (1998) 351-361
20. Berglund G.I., Willassen N.P., Hordvik A., and Smalas A.O. Structure of native pancreatic elastase from North Atlantic salmon at 1.61 Å resolution. Acta Crystallogr., Sect. D 51 (1995) 925-937
21. Smalås A.O., Heimstad E.S., Hordvik A., Willassen N.P., and Male R. Cold adaptation of enzymes: structural comparison between salmon and bovine trypsins. Proteins 20 (1994) 149-166
22. Siddiqui K.S., and Cavicchioli R. Cold-adapted enzymes. Annu. Rev. Biochem. 75 (2006) 403-433
23. Sheridan P.P., Panasik N., Coombs J.M., and Brenchley J.E. Approaches for deciphering the structural basis of low temperature enzyme activity. Biochim. Biophys. Acta 1543 (2000) 417-433
24. Feller G., and Gerday C. Psychrophilic enzymes: hot topics in cold adaptation. Nat. Rev., Microbiol. 1 (2003) 200-208
25. Arnórsdóttir J., Smáradóttir R.B., Magnússon Ó.T., Eggertsson G., Thorbjarnardóttir S.H., and Kristjánsson M.M. Characterization of a cloned subtilisin-like serine proteinase from a psychrotrophic Vibrio species. Eur. J. Biochem. 269 (2002) 5536-5546
26. Betzel C., Gourinath S., Kumar P., Kaur P., Perbandt M., Eschenburg S., and Singh T.P. Structure of a serine protease proteinase K from Tritirachium album limber at 0.98 Å resolution. Biochemistry 40 (2001) 3080-3088
27. Kristjánsson M.M., Magnússon O.T., Gudmundsson H.M., Alfredsson G.A., and Matsuzawa H. Properties of a subtilisin-like proteinase from a psychrotrophic Vibrio species. Comparison with proteinase K and aqualysin I. Eur. J. Biochem. 260 (1999) 752-760
28. Vieille C., and Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 65 (2001) 1-43
29. Matthews B.W., Nicholson H., and Becktel W.J. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 6663-6667
30. Williams R.W., Chang A., Juretic D., and Loughran S. Secondary structure predictions and medium range interactions. Biochim. Biophys. Acta 916 (1987) 200-204
31. Peek K., Daniel R.M., Monk C., Parker L., and Coolbear T. Purification and characterization of a thermostable proteinase isolated from Thermus sp. strain Rt41A. Eur. J. Biochem. 207 (1992) 1035-1044
32. Mildvan A.S. Inverse thinking about double mutants of enzymes. Biochemistry 43 (2004) 14517-14520
33. Voorhorst W.G., Warner A., de Vos W.M., and Siezen R.J. Homology modelling of two subtilisin-like proteases from the hyperthermophilic archaea Pyrococcus furiosus and Thermococcus stetteri. Protein Eng. 10 (1997) 905-914
34. Szilagyi A., and Zavodszky P. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Structure 8 (2000) 493-504
35. Wintrode P.L., Miyazaki K., and Arnold F.H. Patterns of adaptation in a laboratory evolved thermophilic enzyme. Biochim. Biophys. Acta 1549 (2001) 1-8
36. Haney P.J., Badger J.H., Buldak G.L., Reich C.I., Woese C.R., and Olsen G.J. Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 3578-3583
37. Takano K., Yamagata Y., Kubota M., Funahashi J., Fujii S., and Yutani K. Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser → Ala mutants. Biochemistry 38 (1999) 6623-6629
38. Blaber M., Lindstrom J.D., Gassner N., Xu J., Heinz D.W., and Matthews B.W. Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala→Ser and Val→Thr substitutions in T4 lysozyme. Biochemistry 32 (1993) 11363-11373
39. Richardson J.M., Lopez M.M., and Makhatadze G.I. Enthalpy of helix-coil transition: missing link in rationalizing the thermodynamics of helix-forming propensities of the amino acid residues. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1413-1418
40. Blaber M., Zhang X.J., Lindstrom J.D., Pepiot S.D., Baase W.A., and Matthews B.W. Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. J. Mol. Biol. 235 (1994) 600-624
41. Larsen A.N., Moe E., Helland R., Gjellesvik D.R., and Willassen N.P. Characterization of a recombinantly expressed proteinase K-like enzyme from a psychrotrophic Serratia sp. FEBS J. 273 (2006) 47-60
42. Helland R., Larsen A.N., Smalas A.O., and Willassen N.P. The 1.8 Å crystal structure of a proteinase K-like enzyme from a psychrotroph Serratia species. Febs J. 273 (2006) 61-71