Functional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldarius(410 views) Mandrich L, Menchise V, Alterio V, De Simone G, Pedone C, Rossi M, Manco G
Istituto di Biochimica Delle Proteine, CNR, Via Pietro Castellino 111, 80131 Naples, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Naples, Italy
Bioindustry Park del Canavese, Via Ribes 5, 10010 Collerette Giacosa (To), Italy
Dipartimento Delle Scienze Biologiche, University of Naples Federico II, via Mezzocannone 16, 80134 Naples, Italy
References: Hemilä, H., Koivula, T.T., 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 (1994) Biochem Biophys Acta, 1210, pp. 249-25
Manco, G., Adinolfi, E., Pisani, F.M., Carratore, V., Rossi, M., Identification of an esterase from Bacillus acidocaldarius with sequence similarity to a hormone sensitive lipase subfamily (1997) Protein Pept Letters, 4, pp. 375-382
Osterlund, T., Structure-function relationships of hormone-sensitive lipase (2001) Eur J Biochem, 268, pp. 1899-1907
Probst, M.R., Beer, M., Beer, D., Jeno, P., Meyer, U.A., Gasser, R., Human liver arylacetamide deacetylase. Molecular cloning of a novel esterase involved in the metabolic activation of arylamine carcinogens with high sequence similarity to hormone-sensitive lipase (1994) J Biol Chem, 269, pp. 21650-21656
Manco, G., Carrea, G., Giosuè, E., Ottolina, G., Adamo, G., Rossi, M., Modification of the enantioselectivity of two homologous thermophilic carboxylesterases from Alicyclobacillus acidocaldarius and Archaeoglobus fulgidus by random mutagenesis and screening (2002) Extremophiles, 6, pp. 325-331
Manco, G., Febbraio, F., Adinolfi, E., Rossi, M., Homology modeling and active site residues probing of the thermophilic Alicyclobacillus acidocaldarius esterase 2 (1999) Prot Sci, 8, pp. 1789-1796
De Simone, G., Galdiero, S., Manco, G., Lang, D., Rossi, M., Pedone, C., A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase (2000) J Mol Biol, 303, pp. 761-771
De Simone, G., Mandrich, L., Menchise, V., Giordano, V., Febbraio, F., Rossi, M., Pedone, C., Manco, G., A substrate-induced switch in the reaction mechanism of a thermophilic esterase: Kinetic evidences and structural basis (2004) J Biol Chem, 279, pp. 6815-6823
Nardini, M., Dijkstra, B.W., Alpha/beta hydrolase fold enzymes: The family keeps growing (1999) Curr Opin Struct Biol, 9, pp. 732-737
Fischer, M., Pleiss, J., The lipase engineering database: A navigation and analysis tool for protein families (2003) Nucleic Acids Res, 31, pp. 319-321
Brzozowski, A.M., Derewenda, U., Derewenda, Z.S., Dodson, G.G., Lawson, D.M., Turkenburg, J.P., Bjorkling, R., Thim, L., A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex (1992) Nature, 351, pp. 491-494
Derewenda, U., Brzozowski, A.M., Lawson, D., Derewenda, Z.S., Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase (1992) Biochemistry, 31, pp. 1532-1541
Nicolas, A., Egmond, M., Verrips, C.T., de Vlieg, J., Longhi, S., Cambillau, C., Martinez, C., Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state (1996) Biochemistry, 35, pp. 398-410
Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Leatherbarrow RJ. Grafit Version 3.0. Staines, UK: Erithacus Softwere
1992Ayala, Y.M., Di Cera, E., A simple method for the determination of individual rate constants for substrate hydrolysis by serine proteases (2000) Protein Sci, 9, pp. 1589-1593
Brünger, A.T., Adams, P.D., Clore, G.M., De Lano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Warren, G.L., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr D Biol Crystallogr, 54, pp. 905-921
Navaza, J., AMoRe: An automated package for molecular replacement (1994) Acta Crystallogr A, 50, pp. 157-164
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr A, 47, pp. 110-119
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol, 276, pp. 307-326
Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., PRO-CHECK: A program to check the stereochemical quality of protein structures (1993) J Appl Crystallogr, 26, pp. 283-291
De Simone, G., Menchise, V., Alterio, V., Mandrich, L., Rossi, M., Manco, G., Pedone, C., The crystal structure of an EST2 mutant unveils structural insights on the H group of the carboxylesterase/lipase family (2004) J Mol Biol, 343, pp. 137-146
Derewenda, U., Swenson, L., Green, R., Wei, Y., Yamaguchi, S., Joerger, R., Haas, M.J., Derewenda, Z.S., Current progress in crystallographic studies of new lipases from filamentous fungi (1994) Protein Eng, 7, pp. 551-557
Kazlauskas, R.J., Elucidating structure-mechanism relationships in lipases: Prospects for predicting and engineering catalytic properties (1994) Trends Biotechnol, 12, pp. 464-472
Joerger, R.D., Haas, M.J., Alteration of chain length selectivity of a Rhizopus delemar lipase through site-directed mutagenesis (1994) Lipids, 29, pp. 377-384
Uppenberg, J., Hansen, M.T., Patkar, S., Jones, T.A., The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica (1994) Structure, 2, pp. 293-308
Harel, M., Quinn, D.M., Nair, H.K., Silman, I., Sussman, J.L., The structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase (1996) J Am Chem Soc, 118, pp. 2340-2346
Grochulski, P., Bouthillier, F., Kazlauskas, R.J., Serreqi, A.N., Schrag, J.D., Ziomek, E., Cygler, M., Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase (1994) Biochemistry, 33, pp. 3494-3500
Whiting, A.K., Peticolas, W.L., Details of the acyl-enzyme intermediate and the oxyanion hole in serine protease catalysis (1994) Biochemistry, 33, pp. 552-561
Hemil, H., Koivula, T. T., 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 (1994) Biochem Biophys Acta, 1210, pp. 249-25
Probst, M. R., Beer, M., Beer, D., Jeno, P., Meyer, U. A., Gasser, R., Human liver arylacetamide deacetylase. Molecular cloning of a novel esterase involved in the metabolic activation of arylamine carcinogens with high sequence similarity to hormone-sensitive lipase (1994) J Biol Chem, 269, pp. 21650-21656
Brzozowski, A. M., Derewenda, U., Derewenda, Z. S., Dodson, G. G., Lawson, D. M., Turkenburg, J. P., Bjorkling, R., Thim, L., A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex (1992) Nature, 351, pp. 491-494
Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
1992Ayala, Y. M., Di Cera, E., A simple method for the determination of individual rate constants for substrate hydrolysis by serine proteases (2000) Protein Sci, 9, pp. 1589-1593
Br nger, A. T., Adams, P. D., Clore, G. M., De Lano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Warren, G. L., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr D Biol Crystallogr, 54, pp. 905-921
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., Improved methods for building protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr A, 47, pp. 110-119
Laskowski, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M., PRO-CHECK: A program to check the stereochemical quality of protein structures (1993) J Appl Crystallogr, 26, pp. 283-291
Kazlauskas, R. J., Elucidating structure-mechanism relationships in lipases: Prospects for predicting and engineering catalytic properties (1994) Trends Biotechnol, 12, pp. 464-472
Joerger, R. D., Haas, M. J., Alteration of chain length selectivity of a Rhizopus delemar lipase through site-directed mutagenesis (1994) Lipids, 29, pp. 377-384
Whiting, A. K., Peticolas, W. L., Details of the acyl-enzyme intermediate and the oxyanion hole in serine protease catalysis (1994) Biochemistry, 33, pp. 552-561
Functional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldarius