Structural and catalytic response to temperature and cosolvents of carboxylesterase EST1 from the extremely thermoacidophilic archaeon Sulfolobus solfataricus P1

Biotechnology and Bioengineering

Volumn 80, Issue 7, 2002, Pages 784-793

  Sehgal, Amitabh C ^a   Tompson, Richele ^b   Cavanagh, John ^b   Kelly, Robert M ^a  

^a North Carolina State University   (United States)

^b NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

Conformational flexibility; DMSO; Enzyme activation; Thermostable

Indexed keywords

ACETONITRILE; CONFORMATIONS; MICROORGANISMS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; THERMAL EFFECTS;

COSOLVENTS; THERMAL ACTIVATION;

ENZYMES;

ACETONITRILE; CARBOXYLESTERASE; DIMETHYL SULFOXIDE; DIOXANE; N,N DIMETHYLFORMAMIDE; 1,4-DIOXANE; ACETONITRILE DERIVATIVE; DIOXANE DERIVATIVE; SOLVENT;

ARTICLE; CATALYSIS; CIRCULAR DICHROISM; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME STRUCTURE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SULFOLOBUS SOLFATARICUS; TEMPERATURE; BIOSYNTHESIS; CHEMISTRY; CLASSIFICATION; CONFORMATION; ENZYME ACTIVATION; ENZYME STABILITY; ENZYMOLOGY; EVALUATION; ISOLATION AND PURIFICATION; QUALITY CONTROL; SENSITIVITY AND SPECIFICITY; SPECIES DIFFERENCE; STRUCTURE ACTIVITY RELATION; SULFOLOBUS;

ACETONITRILES; CARBOXYLESTERASE; CARBOXYLIC ESTER HYDROLASES; CATALYSIS; DIMETHYL SULFOXIDE; DIMETHYLFORMAMIDE; DIOXANES; ENZYME ACTIVATION; ENZYME STABILITY; MOLECULAR CONFORMATION; QUALITY CONTROL; SENSITIVITY AND SPECIFICITY; SOLVENTS; SPECIES SPECIFICITY; STRUCTURE-ACTIVITY RELATIONSHIP; SULFOLOBUS; TEMPERATURE;

EID: 1842866795     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10433     Document Type: Article

References (59)

1. Adams MWW, Kelly RM. 1998. Finding and using hyperthermophilic enzymes. Trends Biotechnol 16:329-332.
2. Adams MWW, Kelly RM (editors). 2001. Methods in Enzymology. Vols 330, 331, and 334. Hyperthermophilic Enzymes, Part A, B, and C. San Diego: Academic Press.
3. Affleck R, Haynes CA, Clark DS. 1992. Solvent dielectric effects on protein dynamics. Proc Natl Acad Sci U S A 89:5167-5170.
4. Arroyo M, Torres R, de la Mata I, Castillon MP, Acebal C. 1999. Interaction of penicillin V acylase with organic solvents: Catalytic activity modulation on the hydrolysis of penicillin V. Enzyme Microb Technol 25:378-383.
5. Bauer MW, Kelly RM. 1998. The family 1 β-glucosidases from Pyrococcus furiosus and Agrobacterium faecalis share a common catalytic mechanism. Biochemistry 37:17170-17178.
6. Bhattacharjya S, Balaram P. 1997. Effects of organic solvents on protein structures: Observation of a structured helical core in hen egg-white lysozyme in aqueous dimethyl sulfoxide. Proteins 29:492-507.
7. Boross L, Kosary J, Stefanovits-Banyai E, Sisak C, Szajani B. 1998. Studies on kinetic parameters and stability of aminoacylase in nonconventional media. J Biotechnol 66:69-73.
8. Bradford M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principles of protein-dye binding. Anal Biochem 72:248-254.
9. Butler WL. 1979. Fourth-derivative spectra. Methods Enzymol 56:501-515.
10. Cady SG, Bauer MW, Callen W, Snead MA, Mathur EJ, Short JM, Kelly RM. 2001. β-endoglucanase from Pyrococcus furiosus. Methods Enzymol 330:346-354.
11. Cahill JE, Padera FG. 1980. Derivative analysis of UV-visible spectra. Am Lab 12:101-112.
12. Carrea G, Ottolina G, Riva S. 1995. Role of solvents in the control of enzyme selectivity in organic media. Trends Biotechnol 13:63-70.
13. Copeland RA. 1996. Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis. New York: VCH Publishers, Inc. 104 p.
14. Danson MJ, Hough DW, Russell RJM, Taylor GL, Pearl L. 1996. Enzyme thermostability and thermoactivity. Protein Eng 9:629-630.
15. De Simone G, Galdiero S, Manco G, Lang D, Rossi M, Pedone C. 2000. A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase. J Mol Biol 303:761-771.
16. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. 1995. NMRPipe - A multidimensional spectral processing system based on Unix Pipes. J Biomol NMR 6:277-293.
17. Dordick JS. 1989. Enzymatic catalysis in monophasic organic solvents. Enzyme Microb Technol 11:194-211.
18. Dunach M, Sabes M, Padros E. 1983. Fourth-derivative spectrophotometry analysis of tryptophan environment in proteins: Application to melittin, cytochrome c and bacteriorhodopsin. Eur J Biochem 134:123-128.
19. Eyring H, Steam AE. 1939. The application of the theory of absolute reaction rates to proteins. Chem Rev 24:253-270.
20. Gershenson A, Schauerte JA, Giver L, Arnold FH. 2000. Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases. Biochemistry 39:4658-4665.
21. Guo YZ, Clark DS. 2001. Activation of enzymes for nonaqueous biocatalysis by denaturing concentrations of urea. Biochim Biophys Acta Protein Struct Mol Enzymol 1546:406-411.
22. Gupta MN, Batra R, Tyagi R, Sharma A. 1997. Polarity index: The guiding solvent parameter for enzyme stability in aqueous-organic cosolvent mixtures. Biotechnol Prog 13:284-288.
23. Hemila H, Koivula TT, Palva I. 1994. Hormone-sensitive lipase is closely related to several bacterial proteins, and distantly related to acetylcholinesterase and lipoprotein-lipase: Identification of a superfamily of esterases and lipases. Biochim Biophys Acta - Lipids Lipid Metab 1210:249-253.
24. Jackson M, Mantsch HH. 1991. Beware of proteins in DMSO. Biochim Biophys Acta 1078:231-235.
25. Jaenicke R. 1996. Stability and folding of ultrastable proteins: Eye lens crystallins and enzymes from thermophiles. FASEB J 10:84-92.
26. Jensen WA, Armstrong JM. DeGiorgio J, Hearn MTW. 1997. Thermodynamic analysis of the stabilisation of pig heart mitochondrial malate dehydrogenase and maize leaf phosphoenolpyruvate carboxylase by different salts, amino acids and polyols. Biochim Biophys Acta Protein Struct Mol Enzymol 1338:186-198.
27. Kanaya S, Koyanagi T, Kanaya E. 1998. An esterase from Escherichia coli with a sequence similarity to hormone-sensitive lipase. Biochem J 332:75-80.
28. Khan AR, Nirasawa S, Kaneko S, Shimonishi T, Hayashi K. 2000. Characterization of a solvent resistant and thermostable aminopeptidase from the hyperthermophilic bacterium, Aquifex aeolicus. Enzyme Microb Technol 27:83-88.
29. Khmelnitsky YL, Mozhaev VV, Belova AB, Sergeeva MV, Martinek K. 1991. Denaturation capacity: A new quantitative criterion for selection of organic solvents as reaction media in biocatalysis. Eur J Biochem 198:31-41.
30. Klibanov AM. 1997. Why are enzymes less active in organic solvents than in water? Trends Biotechnol 15:97-101.
31. Kornblatt JA, Kornblatt MJ, Lange R, Mombelli E, Guillemette JG. 1999. The individual tyrosines of proteins: Their spectra may or may not differ from those in water or other solvents. Biochim Biophys Acta Protein Struct Mol Enzymol 1431:238-248.
32. Krejci E, Duval N, Chatonnet A, Vincens P, Massoulie J. 1991. Cholinesterase-like domains in enzymes and structural proteins: Functional and evolutionary relationships and identification of a catalytically essential aspartic acid. Proc Natl Acad Sci U S A 88:6647-6651.
33. Kujo C, Ohshima T. 1998. Enzymological characteristics of the hyperthermostable NAD-dependent glutamate dehydrogenase from the archaeon Pyrobaculum islandicum and effects of denaturants and organic solvents. Appl Environ Microbiol 64:2152-2157.
34. Laane C, Boeren S, Vos K, Veeger C. 1987. Rules for optimization of biocatalysis in organic solvents. Biotechnol Bioeng 30:81-87.
35. Laemmli UK. 1970. Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature 227:680-685.
36. Lai B, Cao AN, Lai LH. 2000. Organic cosolvents and hen egg white lysozyme folding. Biochim Biophys Acta - Protein Struct Mol Enzymol 1543:115-122.
37. Landenstein R, Antranikian G. 1998. Proteins from hyperthermophiles: Stability and enzymatic catalysis close to the boiling point of water. Adv Biochem Eng Biotechnol 61:37-85.
38. Lonhienne T, Gerday C, Feller G. 2000. Psychrophilic enzymes: Revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim Biophys Acta - Protein Struct Mol Enzymol 1543:1-10.
39. nd Edition. Menlo Park: Benjamin/Cummings. 289 p.
40. Manco G, Adinolfi E, Pisani FM, Ottolina G, Carrea G, Rossi M. 1998. Over-expression and properties of a new thermophilic and thermostable esterase from Bacillus acidocaldarius with sequence similarity to hormone-sensitive lipase subfamily. Biochem J 332:203-212.
41. Manco G, Giosue E, D'Auria S, Herman P, Carrea G, Rossi M. 2000. Cloning, over-expression, and properties of a new thermophilic and thermostable esterase with sequence similarity to hormone-sensitive lipase subfamily from the archaeon Archaeoglobusfulgidus. Arch Biochem Biophys 373:182-192.
42. Merz A, Knochel T, Jansonius JN, Kirschner K. 1999. The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges. J Mol Biol 288:753-763.
43. Miyazaki K, Wintrode PL, Grayling RA, Rubingh DN, Arnold FH. 2000. Directed evolution study of temperature adaptation in a psychrophilic enzyme. J Mol Biol 297:1015-1026.
44. Moore JC, Arnold FH. 1996. Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents. Nat Biotechnol 14:458-467.
45. Moreno JM, Fagain CO. 1997. Activity and stability of native and modified alanine aminotransferase in cosolvent systems and denaturants. J Mol Catal B - Enzym 2:271-279.
46. Mozhaev VV, Khmelnitsky YL, Sergeeva MV, Belova AB, Klyachko NL, Levashov AV, Martinek K. 1989. Catalytic activity and denaturation of enzymes in water organic cosolvent mixtures: α-Chymotrypsin and laccase in mixed water/alcohol, water/glycol, and water/formamide solvents. Eur J Biochem 184:597-602.
47. Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, Sussman JL, Verschueren KHG, Goldman A. 1992. The α/β-hydrolase fold. Protein Eng 5:197-211.
48. Padros E, Dunach M, Morros A, Sabes M, Manosa J. 1984. Fourthderivative spectrophotometry of proteins. Trends Biochem Sci 9:508-510.
49. Perutz MF. 1978. Electrostatic effects in proteins. Science 201:1187-1191.
50. Riva S, Sennino B, Zambianchi F, Danieli B, Panza L. 1997. Effect of organic cosolvents on the stability and activity of the β-1,4-galactosyltransferase from bovine colostrum. Carbohydr Res 305:525-531.
51. Sehgal AC, Callen W, Mathur EJ, Short JM, Kelly RM. 2001. Carboxylesterase from Sulfolobus solfataricus P1. Methods Enzymol 330:461-471.
52. Siddiqui KS, Shemsi AM, Anwar MA, Rashid MH, Rajoka MI. 1999. Partial and complete alteration of surface charges of carboxymethylcellulase by chemical modification: Thermostabilization in water-miscible organic solvent. Enzyme Microb Technol 24:599-608.
53. Sterner R, Kleemann GR, Szadkowski H, Lustig A, Hennig M, Kirschner K. 1996. Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer. Protein Sci 5:2000-2008.
54. Sterner R, Liebl W. 2001. Thermophilic adaptation of proteins. Crit Rev Biochem Mol Biol 36:39-106.
55. Vieille C, Zeikus GJ. 2001. Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65:1-43.
56. Wei YY, Contreras JA, Sheffield P, Osterlund T, Derewenda U, Kneusel RE, Matern U, Holm C, Derewenda ZS. 1999. Crystal structure of brefeldin A esterase, a bacterial homologue of the mammalian hormone-sensitive lipase. Nat Struct Biol 6:340-345.
57. Wintrode PL, Miyazaki K, Arnold FH. 2000. Cold adaptation of a mesophilic subtilisin-like protease by laboratory evolution. J Biol Chem 275:31635-31640.
58. Wood ANP, Fernandez-Lafuente R, Cowan DA. 1995. Characterization of a novel thermostable esterase as an industrial catalyst. Biotechnol Appl Biochem 21:313-322.
59. Zillig W, Stetter KO, Wunderl S, Schulz W, Priess H, Scholz I. 1980. The Sulfolobus-Caldariella group: Taxonomy on the basis of the structure of DNA-dependent RNA-polymerases. Arch Microbiol 125:259-269.