Role of the N-terminal region for the conformational stability of esterase 2 from Alicyclobacillus acidocaldarius

Biophysical Chemistry

Volumn 127, Issue 1-2, 2007, Pages 113-122

  Foglia, Fabrizia ^a   Mandrich, Luigi ^b   Pezzullo, Margherita ^b   Graziano, Giuseppe ^c   Barone, Guido ^a   Rossi, Mosè ^b   Manco, Giuseppe ^b   Del Vecchio, Pompea ^a  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

^c UNIVERSITY OF SANNIO   (Italy)

Author keywords

Conformational stability; Coupled domains; Independent or sequential two state transitions; Thermophilic esterase

Indexed keywords

ESTERASE II; HYDROLASE; UNCLASSIFIED DRUG;

ALICYCLOBACILLUS ACIDOCALDARIUS; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME STABILITY; FLUORESCENCE; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; TEMPERATURE; THERMODYNAMICS; THERMOPHILIC BACTERIUM;

BACILLUS; BACTERIAL PROTEINS; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; ESTERASES; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SPECTROPHOTOMETRY, ULTRAVIOLET; THERMODYNAMICS;

ALICYCLOBACILLUS ACIDOCALDARIUS;

EID: 33847240831     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2007.01.004     Document Type: Article

References (34)

1. Manco G., Adinolfi E., Pisani F.M., Carratore V., and Rossi M. Identification of an esterase from Bacillus acidocaldarius with sequence similarity to a hormone sensitive lipase subfamily. Prot. Peptide Letters 4 (1997) 375-382
2. Manco G., Adinolfi E., Pisani F.M., Ottolina G., Carrea G., and Manco G. Overexpression and properties of a new thermophilic and thermostable esterase from Bacillus acidocaldarius with sequence similarity to hormone-sensitive lipase subfamily. Biochem. J. 332 (1998) 203-212
3. Hemilä H., Koivula T.T., and Palva I. 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 1210 (1994) 249-253
4. Manco G., Febbraio F., Adinolfi E., and Rossi M. Homology modeling and active-site residues probing of the thermophilic Alicyclobacillus acidocaldarius esterase 2. Protein Sci. 8 (1999) 1789-1796
5. Manco G., Mandrich L., and Rossi M. Residues at the active site of the esterase 2 from Alicyclobacillus acidocaldarius involved in substrate specificity and catalytic activity at high temperature. J. Biol. Chem. 276 (2001) 37482-37490
6. Del Vecchio P., Graziano G., Granata V., Barone G., Mandrich L., Manco G., and Rossi M. Temperature- and denaturant-induced unfolding of two thermophilic esterases. Biochemistry 41 (2002) 1364-1371
7. Del Vecchio P., Graziano G., Granata V., Barone G., Mandrich L., Manco G., and Rossi M. Denaturing action of urea and guanidine hydrochloride towards two thermophilic esterases. Biochem. J. 367 (2002) 857-863
8. Mandrich L., Pezzullo M., Del Vecchio P., Barone G., Rossi M., and Manco G. Analysis of thermal adaptation in the HSL enzyme family. J. Mol. Biol. 335 (2004) 357-369
9. De Simone G., Galdiero S., Manco G., Lang D., Rossi M., and Pedone C. 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 (2000) 761-771
10. De Simone G., Mandrich L., Menchise V., Giordano V., Febbraio F., Rossi M., Pedone C., and Manco G. A substrate-induced switch in the reaction mechanism of thermophilic esterase. J. Biol. Chem. 279 (2004) 6815-6823
11. Mandrich L., Merone L., Pezzullo M., Cipolla L., Nicotra F., Rossi M., and Manco G. Role of the N-terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family. J. Mol. Biol. 345 (2005) 501-512
12. Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
13. Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-280
14. Venyaminov S.Y., and Yang J.T. Determination of protein secondary structure. In: Fasman G.D. (Ed). Circular Dichroism and the Conformational Analysis of Biomolecules (1996), Plenum Press, New York 69-107
15. Sreema N., and Woody R.W. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209 (1993) 32-44
16. Lobley A., Whitmore A.L., and Wallace B.A. Dichroweb: an interactive website for the analysis of secondary structure from circular dichroism data. Bioinformatics 18 (2002) 211-212
17. J.R. Lakowicz, Principles of Fluorescence Spectroscopy, Kluwer Academic and Plenum Publishers, New York, 1999.
18. Catanzano F., Giancola C., Graziano G., and Barone G. Temperature-induced denaturation of ribonuclease S: a thermodynamic study. Biochemistry 35 (1996) 13378-13385
19. Freire E., and Biltonen R.L. Statistical mechanical deconvolution of thermal transitions in macromolecules I. Theory and application to homogeneous systems. Biopolymers 17 (1978) 463-479
20. Privalov P.L. Stability of proteins: small globular proteins. Adv. Protein Chem. 33 (1979) 167-241
21. Zhou Y., Hall C.K., and Karplus M. The calorimetric criterion for a two-state process revisited. Protein Sci. 5 (1999) 1064-1074
22. Catanzano F., Gambuti A., Graziano G., and Barone G. Interaction with d-glucose and thermal denaturation of yeast hexokinase B: a DSC study. J. Biochem. 121 (1997) 568-577
23. Freire E. Statistical thermodynamic analysis of differential scanning calorimetry data: structural deconvolution of heat capacity function of proteins. Methods Enzymol. 240 (1994) 502-530
24. Gill S.J., Richey B., Bishop G., and Wyman J. Generalized binding phenomena in an allosteric macromolecule. Biophys. Chem. 21 (1985) 1-14
25. Becktel W.J., and Schellman J.A. Protein stability curves. Biopolymers 26 (1987) 1859-1877
26. Rees D.C., and Robertson A.D. Some thermodynamic implications for the thermostability of proteins. Protein Sci. 10 (2001) 1187-1194
27. Robertson A.D., and Murphy K.P. Protein structure and energetics of protein stability. Chem. Rev. 97 (1997) 1251-1267
28. Jaenicke R., and Bohm G. The stability of proteins in extreme environments. Curr. Opin. Struct. Biol. 8 (1998) 738-748
29. Dill K.A. Theory for the folding and stability of globular proteins. Biochemistry 24 (1985) 1501-1509
30. Privalov P.L. Thermodynamic problems of protein structure. Annu. Rev. Biophys. Biophys. Chem. 18 (1989) 47-69
31. Spassov V.Z., Karshikoff A.D., and Ladenstein R. The optimisation of protein-solvent interactions: thermostability and the role of hydrophobic and electrostatic interactions. Protein Sci. 4 (1995) 1516-1527
32. Brandts J.F., Hu C.Q., and Lin L.N. A simple model for proteins with interacting domains. Applications to scanning calorimetry data. Biochemistry 28 (1989) 8588-8596
33. Ramsay G., and Freire E. Linked thermal and solute perturbation analysis of cooperative domain interactions in proteins. Structural stability of diphteria toxin. Biochemistry 29 (1990) 8677-8683
34. Graziano G. Scaled particle theory study of the lengthscale dependence of cavity thermodynamics in different liquids. J. Phys. Chem., B 110 (2006) 11421-11426