Functional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldarius (410 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2008 Jun; 71(4): 1721-1731.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.419, 5-year impact factor: 4.019
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-44349174350&partnerID=40&md5=2f6dc5b338e70245557922223751d466
Keywords: Carboxylesterase, Oxyanion Loop, Ph-Activity Profile, Reaction Mechanism, Thermophilicity, 4 (2 Hydroxyethyl) 1 Piperazineethanesulfonic Acid, Mutant Protein, Alicyclobacillus Acidocaldarius, Article, Catalysis, Hydrogen Bond, Molecular Mechanics, Nonhuman, Priority Journal, Protein Function, Protein Structure, Temperature, Thermostability, Three Dimensional Imaging, Binding Sites, Carboxylic Ester Hydrolases, Crystallography, X-Ray, Enzyme Stability, Glycine, Hydrogen Bonding, Hydrogen-Ion Concentration, Hydrolysis, Kinetics, Models, Mutation, Protein Binding, Secondary, Serine, Substrate Specificity, Water, X-Ray Diffraction,
Affiliations:
*** IBB - CNR ***
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
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2008 Jun; 71(4): 1721-1731.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.419, 5-year impact factor: 4.019
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-44349174350&partnerID=40&md5=2f6dc5b338e70245557922223751d466
Keywords: Carboxylesterase, Oxyanion Loop, Ph-Activity Profile, Reaction Mechanism, Thermophilicity, 4 (2 Hydroxyethyl) 1 Piperazineethanesulfonic Acid, Mutant Protein, Alicyclobacillus Acidocaldarius, Article, Catalysis, Hydrogen Bond, Molecular Mechanics, Nonhuman, Priority Journal, Protein Function, Protein Structure, Temperature, Thermostability, Three Dimensional Imaging, Binding Sites, Carboxylic Ester Hydrolases, Crystallography, X-Ray, Enzyme Stability, Glycine, Hydrogen Bonding, Hydrogen-Ion Concentration, Hydrolysis, Kinetics, Models, Mutation, Protein Binding, Secondary, Serine, Substrate Specificity, Water, X-Ray Diffraction,
Affiliations:
*** IBB - CNR ***
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
Recent mutagenic and molecular modelling studies suggested a role for glycine 84 in the putative oxyanion loop of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius. A 114 times decrease of the esterase catalytic activity of the G84S mutant was observed, without changes in the thermal stability. The recently solved three-dimensional (3D) structure of EST2 in complex with a HEPES molecule permitted to demonstrate that G84 (together with G83 and A156) is involved in the stabilization of the oxyanion through a hydrogen bond from its main chain NH group. The structural data in this case did not allowed us to rationalize the effect of the mutation, since this hydrogen bond was predicted to be unaltered in the mutant. Since the mutation could shed light on the role of the oxyanion loop in the HSL family, experiments to elucidate at the mechanistic level the reasons of the observed drop in k cat were devised. In this work, the kinetic and structural features of the G84S mutant were investigated in more detail. The optimal temperature and pH for the activity of the mutated enzyme were found significantly changed (T = 65°C and pH = 5.75). The catalytic constants KM and V max were found considerably altered in the mutant, with ninefold increased KM and 14-fold decreased Vmax, at pH 5.75. At pH 7.1, the decrease in kcat was much more dramatic. The measurement of kinetic constants for some steps of the reaction mechanism and the resolution of the mutant 3D structure provided evidences that the observed effects were partly due to the steric hindrance of the S84-OH group towards the ester substrate and partly to its interference with the nucleophilic attack of a water molecule on the second tetrahedral intermediate. © 2007 Wiley-Liss, Inc.
Recent mutagenic and molecular modelling studies suggested a role for glycine 84 in the putative oxyanion loop of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius. A 114 times decrease of the esterase catalytic activity of the G84S mutant was observed, without changes in the thermal stability. The recently solved three-dimensional (3D) structure of EST2 in complex with a HEPES molecule permitted to demonstrate that G84 (together with G83 and A156) is involved in the stabilization of the oxyanion through a hydrogen bond from its main chain NH group. The structural data in this case did not allowed us to rationalize the effect of the mutation, since this hydrogen bond was predicted to be unaltered in the mutant. Since the mutation could shed light on the role of the oxyanion loop in the HSL family, experiments to elucidate at the mechanistic level the reasons of the observed drop in k cat were devised. In this work, the kinetic and structural features of the G84S mutant were investigated in more detail. The optimal temperature and pH for the activity of the mutated enzyme were found significantly changed (T = 65°C and pH = 5.75). The catalytic constants KM and V max were found considerably altered in the mutant, with ninefold increased KM and 14-fold decreased Vmax, at pH 5.75. At pH 7.1, the decrease in kcat was much more dramatic. The measurement of kinetic constants for some steps of the reaction mechanism and the resolution of the mutant 3D structure provided evidences that the observed effects were partly due to the steric hindrance of the S84-OH group towards the ester substrate and partly to its interference with the nucleophilic attack of a water molecule on the second tetrahedral intermediate. © 2007 Wiley-Liss, Inc.
Functional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldarius
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Functional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldarius
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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 (950 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2004 Oct 8; 343(1): 137-146.
Impact Factor: 5.542
View Export to BibTeX Export to EndNote
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 (409 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2004 Feb 20; 279(8): 6815-6823.
Impact Factor: 6.355
View Export to BibTeX Export to EndNote
De Simone G, Menchise V, Manco G, Mandrich L, Sorrentino N, Lang D, Rossi M, Pedone C
* The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus (435 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2001 Nov 30; 314(3): 507-518.
Impact Factor: 5.826
View Export to BibTeX Export to EndNote
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 (624 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2000 Nov 10; 303(5): 761-771.
Impact Factor: 5.388
View Export to BibTeX Export to EndNote
De Simone G, Manco G, Galdiero S, Lombardi A, Rossi M, Pavone V
Crystallization and preliminary X-ray diffraction studies of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius (407 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 1999 Jul; 55(7): 1348-1349.
Impact Factor: 2.935
View Export to BibTeX Export to EndNote
* The crystal structure of an EST2 mutant unveils structural insights on the H group of the carboxylesterase/lipase family (950 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2004 Oct 8; 343(1): 137-146.
Impact Factor: 5.542
View Export to BibTeX Export to EndNote
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 (409 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2004 Feb 20; 279(8): 6815-6823.
Impact Factor: 6.355
View Export to BibTeX Export to EndNote
De Simone G, Menchise V, Manco G, Mandrich L, Sorrentino N, Lang D, Rossi M, Pedone C
* The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus (435 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2001 Nov 30; 314(3): 507-518.
Impact Factor: 5.826
View Export to BibTeX Export to EndNote
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 (624 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2000 Nov 10; 303(5): 761-771.
Impact Factor: 5.388
View Export to BibTeX Export to EndNote
De Simone G, Manco G, Galdiero S, Lombardi A, Rossi M, Pavone V
Crystallization and preliminary X-ray diffraction studies of the carboxylesterase EST2 from Alicyclobacillus acidocaldarius (407 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 1999 Jul; 55(7): 1348-1349.
Impact Factor: 2.935
View Export to BibTeX Export to EndNote
5 Records (5 excluding Abstracts).
Total impact factor: 26.046 (26.046 excluding Abstracts).
Total 5 year impact factor: 17.821 (17.821 excluding Abstracts).
Total impact factor: 26.046 (26.046 excluding Abstracts).
Total 5 year impact factor: 17.821 (17.821 excluding Abstracts).
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