Insight into the stereospecificity of short-chain Thermus thermophilus alcohol dehydrogenase showing pro-S hydride transfer and Prelog enantioselectivity (520 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2010 Apr; 17(4): 437-443.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.849, 5-year impact factor: 1.45
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77949957731&partnerID=40&md5=4f6b4e76221e675ce349d72852226469
Keywords: Bacillus Stearothermophilus, Cofactor Stereospecificity, Enantioselectivity, Prelog Rule, Short-Chain Dehydrogenase Reductase, Thermus Thermophilus, 2 Propanol, Alcohol Dehydrogenase, Bacterial Protein, Deuterium, Nicotinamide Adenine Dinucleotide, Article, Chemical Structure, Chemistry, Enzymology, Metabolism, Nuclear Magnetic Resonance, Protein Conformation, Stereoisomerism, 2-Propanol, Models, Molecular, Biomolecular, Geobacillus Stearothermophilus,
Affiliations:
*** IBB - CNR ***
Istituto di Biochimica delle Proteine, CNR, Via P. Castellino 111, I-80131, NA, Italy
Istituto di Chimica Biomolecolare, CNR, Comprensorio Olivetti, Edificio 70, Via Campi Flegrei 34, I-80078 Pozzuoli (NA), Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134, NA, Italy
References:
You, K.S., Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions (1985) CRC Crit. Rev. Biochem, 17 (4), pp. 313-45
Creighton, D.J., Murthy, N.S.R.K., In Stereochemistry of EnzymeCatalyzed Reaction at Carbon
Academic Press, London (1990) The Enzymes, 19, pp. 323-421
Toseland, C.P., McSparron, H.M., Flower, D.R., DSD-An integrated, web accessible database of Dehydrogenase Enzyme Stereospecificities (2005) Bmc Bioinformatics, 6, pp. 283-289
Prelog, V., Specification of the stereospecificity of some oxidoreductase by diamond lattice sections (1964) Pure Appl. Chem, 9 (1), pp. 119-130
Faber, K., (2004) In Biotransformations In Organic Chemistry, pp. 177-219. , 5th Ed. Springer-Verlag, Berlin Heidelberg, Germany
Schlieben, N.H., Niefind, K., Muller, J., Riebel, B., Hummel, W., Schomburg, D., Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity (2005) J. Mol. Biol, 349 (4), pp. 801-813
Eklund, H., Plapp, B.V., Samama, J.P., Brändén, C.-I., Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase (1982) J. Biol. Chem, 257 (23), pp. 14349-14358
Weinhold, E.G., Glasfeld, A., Ellington, A.D., Benner, S.A., Structural determinants of stereospecificity in yeast alcohol dehydrogenase (1991) Proc. Natl. Acad. Sci. Usa, 88 (19), pp. 8420-8424
Korkhin, Y., Kalb, A.J., Peretz, M., Bogin, O., Burstein, Y., Frolow, F., NADP-dependent bacterial alcohol dehydrogenases: Crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii (1998) J. Mol. Biol., 278 (5), pp. 967-981. , Gilboa
Peters, J., Minuth, T., Kula, M.R., A novel NADH-dependent carbonyl reductase with an extremely broad substrate range from Candida parapsilosis: Purification and characterization (1993) Enzyme Microb. Technol, 15 (11), pp. 950-958
Itoh, N., Mizuguchi, N., Mabuchi, M., Production of chiral alcohols by enantioselective reduction with NADH-dependent phenylacetaldehyde reductase from Corynebacterium strain, ST-10 (1999) J. Mol. Cat. B: Enzym, 6 (1-2), pp. 41-50
Velonia, K., Tsigos, I., Bouriotis, V., Smonou, I., Stereospecificity of hydrogen transfer by the NAD(+)-linked alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123 (1999) Bioorg. Med. Chem. Lett, 9 (1), pp. 65-68
Trincone, A., Lama, L., Rella, R., D'auria, S., Raia, C.A., Nicolaus, B., Determination of hydride transfer stereospecificity of NADH-dependent alcohol-aldehyde/ketone oxidoreductase from Sulfolobus solfataricus (1990) Biochim. Biophys. Acta, 1041 (1), pp. 94-96
Ladenstein, R., Winberg, J.-O., Benach, J., Medium- and shortchain dehydrogenase/reductase gene and protein families: Structure-function relationships in short-chain alcohol dehydrogenases (2008) Cell. Mol. Life Sci, 65 (24), pp. 3918-3935
Dutler, H., Prelog, V., van der Baan, J.L., Hochuli, E., Kis, Z., Taylor, K.E., Dihydroxyacetone reductase from Mucor javanicus. 1. Isolation and properties (1977) Eur. J. Biochem, 75 (2), pp. 423-432
Bradshaw, C.W., Hummel, W., Wong, C.H., Lactobacillus kefir alcohol dehydrogenase: A useful catalyst for synthesis (1992) J. Org. Chem, 57 (5), pp. 1532-1536
Bradshaw, C.W., Fu, H., Shen, G.J., Wong, C.H., A Pseudomonas sp. alcohol dehydrogenase with broad substrate specificity and unusual stereospecificity for organic synthesis (1992) J. Org. Chem, 57 (5), pp. 1526-1532
Inoue, K., Makino, Y., Itoh, N., Production of (R)-chiral alcohols by a hydrogen-transfer bioreduction with NADH-dependent Leifsonia alcohol dehydrogenase (2005) Tetrahedron Asymmetry, 16 (15), pp. 2539-2549
Höffken, H.W., Duong, M., Friedrich, T., Breuer, M., Hauer, B., Reinhardt, R., Rabus, R., Heider, J., Crystal structure and enzyme kinetics of the (S)-specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain EbN1 (2006) Biochemistry, 45 (1), pp. 82-93
Almarsson, Ö., Bruice, T.C., Evaluation of the factors influencing reactivity and stereospecificity in NAD(P)H dependent dehydrogenase enzymes (1993) J. Am. Chem. Soc, 115 (6), pp. 2125-2138
Hummel, W., New alcohol dehydrogenases for the synthesis of chiral compounds (1997) Adv. Biochem. Eng. Biotechnol, 58 (1), pp. 145-184
Nakamura, K., Yamanaka, R., Matsuda, T., Harada, T., Recent developments in asymmetric reduction of ketones with biocatalysts (2003) Tetrahedron Asymmetry, 14 (18), pp. 2659-2681
de Wildeman, S.M., Sonke, T., Schoemaker, H.E., May, O., Biocatalytic reductions: From lab curiosity to first choice (2007) Acc. Chem. Res, 40 (12), pp. 1260-1266
Pennacchio, A., Pucci, B., Secundo, F., la Cara, F., Rossi, M., Raia, C.A., Purification and Characterization of a Novel Recombinant Highly Enantioselective, Short-Chain NAD(H)-dependent Alcohol Dehydrogenase from Thermus thermophilus. Appl. Environ (2008) Microbiol, 74 (13), pp. 3949-3958
Raia, C.A., Giordano, A., Rossi, M., Alcohol dehydrogenase from Sulfolobus solfataricus (2001) Methods Enzymol, 331, pp. 176-195
Fiorentino, G., Cannio, R., Rossi, M., Bartolucci, S., Decreasing the stability and changing the substrate specificity of the Bacillus stearothermophilus alcohol dehydrogenase by single amino acid replacements (1998) Protein Eng, 11 (11), pp. 925-930
Asada, Y., Endo, S., Inoue, Y., Mamiya, H., Hara, A., Kunishima, N., Matsunaga, T., Biochemical and structural characterization of a short-chain dehydrogenase/reductase of Thermus thermophilus HB8. A hyperthermostable aldose-1-dehydrogenase with broad substrate specificity (2009) Chem. Biol. Interact, 178 (1-3), pp. 117-126
Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Belew, R.K., Olson, A.J., Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function (1998) J. Comput. Chem, 19 (14), pp. 1639-1662
Ceccarelli, C., Liang, Z.X., Strickler, M., Prehna, G., Goldstein, B.M., Klinman, J.P., Bahnson, B.J., Crystal structure and amide H/D exchange of binary complexes of alcohol dehydrogenase from Bacillus stearothermophilus: Insight into thermostability and cofactor binding (2004) Biochemistry, 43 (18), pp. 5266-5277
Zhang, X., Bruice, T.C., Temperature-dependent structure of the E•S complex of Bacillus stearothermophilus alcohol dehydrogenase (2007) Biochemistry, 46 (3), pp. 837-843
Jeong, S.S., Gready, J.E., A method of preparation and purification of (4R)-deuterated-reduced nicotinamide adenine dinucleotide phosphate (1994) Anal. Biochem, 221 (2), pp. 273-277
Schneider-Bernlöhr, H., Adolph, H.-W., Zeppezauer, M., Coenzyme stereospecificity of Alcohol/Polyol Dehydrogenases: Conservation of Protein Types vs. Functional Constraints (1986) J. Am. Chem. Soc, 108 (18), pp. 5573-5576
Kwiecie, R.A., Ayadi, F., Nemmaoui, Y., Silvestre, V., Zhang, B.L., Robins, R.J., Probing stereoselectivity and pro-chirality of hydride transfer during short-chain alcohol dehydrogenase activity: A combined quantitative 2H NMR and computational approach (2009) Arch. Biochem. Biophys, 482 (1-2), pp. 42-51
Humphrey, W., Dalke, A., Schulten, K., VMD: Visual molecular dynamics (1996) J. Mol. Graph, 14 (1), pp. 33-38
You, K. S., Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions (1985) CRC Crit. Rev. Biochem, 17 (4), pp. 313-45
Creighton, D. J., Murthy, N. S. R. K., In Stereochemistry of EnzymeCatalyzed Reaction at Carbon
Toseland, C. P., McSparron, H. M., Flower, D. R., DSD-An integrated, web accessible database of Dehydrogenase Enzyme Stereospecificities (2005) Bmc Bioinformatics, 6, pp. 283-289
Schlieben, N. H., Niefind, K., Muller, J., Riebel, B., Hummel, W., Schomburg, D., Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity (2005) J. Mol. Biol, 349 (4), pp. 801-813
Weinhold, E. G., Glasfeld, A., Ellington, A. D., Benner, S. A., Structural determinants of stereospecificity in yeast alcohol dehydrogenase (1991) Proc. Natl. Acad. Sci. Usa, 88 (19), pp. 8420-8424
Bradshaw, C. W., Hummel, W., Wong, C. H., Lactobacillus kefir alcohol dehydrogenase: A useful catalyst for synthesis (1992) J. Org. Chem, 57 (5), pp. 1532-1536
Bradshaw, C. W., Fu, H., Shen, G. J., Wong, C. H., A Pseudomonas sp. alcohol dehydrogenase with broad substrate specificity and unusual stereospecificity for organic synthesis (1992) J. Org. Chem, 57 (5), pp. 1526-1532
H ffken, H. W., Duong, M., Friedrich, T., Breuer, M., Hauer, B., Reinhardt, R., Rabus, R., Heider, J., Crystal structure and enzyme kinetics of the (S) -specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain EbN1 (2006) Biochemistry, 45 (1), pp. 82-93
Almarsson, ., Bruice, T. C., Evaluation of the factors influencing reactivity and stereospecificity in NAD (P) H dependent dehydrogenase enzymes (1993) J. Am. Chem. Soc, 115 (6), pp. 2125-2138
de Wildeman, S. M., Sonke, T., Schoemaker, H. E., May, O., Biocatalytic reductions: From lab curiosity to first choice (2007) Acc. Chem. Res, 40 (12), pp. 1260-1266
Raia, C. A., Giordano, A., Rossi, M., Alcohol dehydrogenase from Sulfolobus solfataricus (2001) Methods Enzymol, 331, pp. 176-195
Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., Olson, A. J., Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function (1998) J. Comput. Chem, 19 (14), pp. 1639-1662
Jeong, S. S., Gready, J. E., A method of preparation and purification of (4R) -deuterated-reduced nicotinamide adenine dinucleotide phosphate (1994) Anal. Biochem, 221 (2), pp. 273-277
Schneider-Bernl hr, H., Adolph, H. -W., Zeppezauer, M., Coenzyme stereospecificity of Alcohol/Polyol Dehydrogenases: Conservation of Protein Types vs. Functional Constraints (1986) J. Am. Chem. Soc, 108 (18), pp. 5573-5576
Kwiecie, R. A., Ayadi, F., Nemmaoui, Y., Silvestre, V., Zhang, B. L., Robins, R. J., Probing stereoselectivity and pro-chirality of hydride transfer during short-chain alcohol dehydrogenase activity: A combined quantitative 2H NMR and computational approach (2009) Arch. Biochem. Biophys, 482 (1-2), pp. 42-51
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2010 Apr; 17(4): 437-443.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.849, 5-year impact factor: 1.45
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77949957731&partnerID=40&md5=4f6b4e76221e675ce349d72852226469
Keywords: Bacillus Stearothermophilus, Cofactor Stereospecificity, Enantioselectivity, Prelog Rule, Short-Chain Dehydrogenase Reductase, Thermus Thermophilus, 2 Propanol, Alcohol Dehydrogenase, Bacterial Protein, Deuterium, Nicotinamide Adenine Dinucleotide, Article, Chemical Structure, Chemistry, Enzymology, Metabolism, Nuclear Magnetic Resonance, Protein Conformation, Stereoisomerism, 2-Propanol, Models, Molecular, Biomolecular, Geobacillus Stearothermophilus,
Affiliations:
*** IBB - CNR ***
Istituto di Biochimica delle Proteine, CNR, Via P. Castellino 111, I-80131, NA, Italy
Istituto di Chimica Biomolecolare, CNR, Comprensorio Olivetti, Edificio 70, Via Campi Flegrei 34, I-80078 Pozzuoli (NA), Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134, NA, Italy
References:
You, K.S., Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions (1985) CRC Crit. Rev. Biochem, 17 (4), pp. 313-45
Creighton, D.J., Murthy, N.S.R.K., In Stereochemistry of EnzymeCatalyzed Reaction at Carbon
Academic Press, London (1990) The Enzymes, 19, pp. 323-421
Toseland, C.P., McSparron, H.M., Flower, D.R., DSD-An integrated, web accessible database of Dehydrogenase Enzyme Stereospecificities (2005) Bmc Bioinformatics, 6, pp. 283-289
Prelog, V., Specification of the stereospecificity of some oxidoreductase by diamond lattice sections (1964) Pure Appl. Chem, 9 (1), pp. 119-130
Faber, K., (2004) In Biotransformations In Organic Chemistry, pp. 177-219. , 5th Ed. Springer-Verlag, Berlin Heidelberg, Germany
Schlieben, N.H., Niefind, K., Muller, J., Riebel, B., Hummel, W., Schomburg, D., Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity (2005) J. Mol. Biol, 349 (4), pp. 801-813
Eklund, H., Plapp, B.V., Samama, J.P., Brändén, C.-I., Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase (1982) J. Biol. Chem, 257 (23), pp. 14349-14358
Weinhold, E.G., Glasfeld, A., Ellington, A.D., Benner, S.A., Structural determinants of stereospecificity in yeast alcohol dehydrogenase (1991) Proc. Natl. Acad. Sci. Usa, 88 (19), pp. 8420-8424
Korkhin, Y., Kalb, A.J., Peretz, M., Bogin, O., Burstein, Y., Frolow, F., NADP-dependent bacterial alcohol dehydrogenases: Crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii (1998) J. Mol. Biol., 278 (5), pp. 967-981. , Gilboa
Peters, J., Minuth, T., Kula, M.R., A novel NADH-dependent carbonyl reductase with an extremely broad substrate range from Candida parapsilosis: Purification and characterization (1993) Enzyme Microb. Technol, 15 (11), pp. 950-958
Itoh, N., Mizuguchi, N., Mabuchi, M., Production of chiral alcohols by enantioselective reduction with NADH-dependent phenylacetaldehyde reductase from Corynebacterium strain, ST-10 (1999) J. Mol. Cat. B: Enzym, 6 (1-2), pp. 41-50
Velonia, K., Tsigos, I., Bouriotis, V., Smonou, I., Stereospecificity of hydrogen transfer by the NAD(+)-linked alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123 (1999) Bioorg. Med. Chem. Lett, 9 (1), pp. 65-68
Trincone, A., Lama, L., Rella, R., D'auria, S., Raia, C.A., Nicolaus, B., Determination of hydride transfer stereospecificity of NADH-dependent alcohol-aldehyde/ketone oxidoreductase from Sulfolobus solfataricus (1990) Biochim. Biophys. Acta, 1041 (1), pp. 94-96
Ladenstein, R., Winberg, J.-O., Benach, J., Medium- and shortchain dehydrogenase/reductase gene and protein families: Structure-function relationships in short-chain alcohol dehydrogenases (2008) Cell. Mol. Life Sci, 65 (24), pp. 3918-3935
Dutler, H., Prelog, V., van der Baan, J.L., Hochuli, E., Kis, Z., Taylor, K.E., Dihydroxyacetone reductase from Mucor javanicus. 1. Isolation and properties (1977) Eur. J. Biochem, 75 (2), pp. 423-432
Bradshaw, C.W., Hummel, W., Wong, C.H., Lactobacillus kefir alcohol dehydrogenase: A useful catalyst for synthesis (1992) J. Org. Chem, 57 (5), pp. 1532-1536
Bradshaw, C.W., Fu, H., Shen, G.J., Wong, C.H., A Pseudomonas sp. alcohol dehydrogenase with broad substrate specificity and unusual stereospecificity for organic synthesis (1992) J. Org. Chem, 57 (5), pp. 1526-1532
Inoue, K., Makino, Y., Itoh, N., Production of (R)-chiral alcohols by a hydrogen-transfer bioreduction with NADH-dependent Leifsonia alcohol dehydrogenase (2005) Tetrahedron Asymmetry, 16 (15), pp. 2539-2549
Höffken, H.W., Duong, M., Friedrich, T., Breuer, M., Hauer, B., Reinhardt, R., Rabus, R., Heider, J., Crystal structure and enzyme kinetics of the (S)-specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain EbN1 (2006) Biochemistry, 45 (1), pp. 82-93
Almarsson, Ö., Bruice, T.C., Evaluation of the factors influencing reactivity and stereospecificity in NAD(P)H dependent dehydrogenase enzymes (1993) J. Am. Chem. Soc, 115 (6), pp. 2125-2138
Hummel, W., New alcohol dehydrogenases for the synthesis of chiral compounds (1997) Adv. Biochem. Eng. Biotechnol, 58 (1), pp. 145-184
Nakamura, K., Yamanaka, R., Matsuda, T., Harada, T., Recent developments in asymmetric reduction of ketones with biocatalysts (2003) Tetrahedron Asymmetry, 14 (18), pp. 2659-2681
de Wildeman, S.M., Sonke, T., Schoemaker, H.E., May, O., Biocatalytic reductions: From lab curiosity to first choice (2007) Acc. Chem. Res, 40 (12), pp. 1260-1266
Pennacchio, A., Pucci, B., Secundo, F., la Cara, F., Rossi, M., Raia, C.A., Purification and Characterization of a Novel Recombinant Highly Enantioselective, Short-Chain NAD(H)-dependent Alcohol Dehydrogenase from Thermus thermophilus. Appl. Environ (2008) Microbiol, 74 (13), pp. 3949-3958
Raia, C.A., Giordano, A., Rossi, M., Alcohol dehydrogenase from Sulfolobus solfataricus (2001) Methods Enzymol, 331, pp. 176-195
Fiorentino, G., Cannio, R., Rossi, M., Bartolucci, S., Decreasing the stability and changing the substrate specificity of the Bacillus stearothermophilus alcohol dehydrogenase by single amino acid replacements (1998) Protein Eng, 11 (11), pp. 925-930
Asada, Y., Endo, S., Inoue, Y., Mamiya, H., Hara, A., Kunishima, N., Matsunaga, T., Biochemical and structural characterization of a short-chain dehydrogenase/reductase of Thermus thermophilus HB8. A hyperthermostable aldose-1-dehydrogenase with broad substrate specificity (2009) Chem. Biol. Interact, 178 (1-3), pp. 117-126
Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Belew, R.K., Olson, A.J., Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function (1998) J. Comput. Chem, 19 (14), pp. 1639-1662
Ceccarelli, C., Liang, Z.X., Strickler, M., Prehna, G., Goldstein, B.M., Klinman, J.P., Bahnson, B.J., Crystal structure and amide H/D exchange of binary complexes of alcohol dehydrogenase from Bacillus stearothermophilus: Insight into thermostability and cofactor binding (2004) Biochemistry, 43 (18), pp. 5266-5277
Zhang, X., Bruice, T.C., Temperature-dependent structure of the E•S complex of Bacillus stearothermophilus alcohol dehydrogenase (2007) Biochemistry, 46 (3), pp. 837-843
Jeong, S.S., Gready, J.E., A method of preparation and purification of (4R)-deuterated-reduced nicotinamide adenine dinucleotide phosphate (1994) Anal. Biochem, 221 (2), pp. 273-277
Schneider-Bernlöhr, H., Adolph, H.-W., Zeppezauer, M., Coenzyme stereospecificity of Alcohol/Polyol Dehydrogenases: Conservation of Protein Types vs. Functional Constraints (1986) J. Am. Chem. Soc, 108 (18), pp. 5573-5576
Kwiecie, R.A., Ayadi, F., Nemmaoui, Y., Silvestre, V., Zhang, B.L., Robins, R.J., Probing stereoselectivity and pro-chirality of hydride transfer during short-chain alcohol dehydrogenase activity: A combined quantitative 2H NMR and computational approach (2009) Arch. Biochem. Biophys, 482 (1-2), pp. 42-51
Humphrey, W., Dalke, A., Schulten, K., VMD: Visual molecular dynamics (1996) J. Mol. Graph, 14 (1), pp. 33-38
You, K. S., Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions (1985) CRC Crit. Rev. Biochem, 17 (4), pp. 313-45
Creighton, D. J., Murthy, N. S. R. K., In Stereochemistry of EnzymeCatalyzed Reaction at Carbon
Toseland, C. P., McSparron, H. M., Flower, D. R., DSD-An integrated, web accessible database of Dehydrogenase Enzyme Stereospecificities (2005) Bmc Bioinformatics, 6, pp. 283-289
Schlieben, N. H., Niefind, K., Muller, J., Riebel, B., Hummel, W., Schomburg, D., Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity (2005) J. Mol. Biol, 349 (4), pp. 801-813
Weinhold, E. G., Glasfeld, A., Ellington, A. D., Benner, S. A., Structural determinants of stereospecificity in yeast alcohol dehydrogenase (1991) Proc. Natl. Acad. Sci. Usa, 88 (19), pp. 8420-8424
Bradshaw, C. W., Hummel, W., Wong, C. H., Lactobacillus kefir alcohol dehydrogenase: A useful catalyst for synthesis (1992) J. Org. Chem, 57 (5), pp. 1532-1536
Bradshaw, C. W., Fu, H., Shen, G. J., Wong, C. H., A Pseudomonas sp. alcohol dehydrogenase with broad substrate specificity and unusual stereospecificity for organic synthesis (1992) J. Org. Chem, 57 (5), pp. 1526-1532
H ffken, H. W., Duong, M., Friedrich, T., Breuer, M., Hauer, B., Reinhardt, R., Rabus, R., Heider, J., Crystal structure and enzyme kinetics of the (S) -specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain EbN1 (2006) Biochemistry, 45 (1), pp. 82-93
Almarsson, ., Bruice, T. C., Evaluation of the factors influencing reactivity and stereospecificity in NAD (P) H dependent dehydrogenase enzymes (1993) J. Am. Chem. Soc, 115 (6), pp. 2125-2138
de Wildeman, S. M., Sonke, T., Schoemaker, H. E., May, O., Biocatalytic reductions: From lab curiosity to first choice (2007) Acc. Chem. Res, 40 (12), pp. 1260-1266
Raia, C. A., Giordano, A., Rossi, M., Alcohol dehydrogenase from Sulfolobus solfataricus (2001) Methods Enzymol, 331, pp. 176-195
Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., Olson, A. J., Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function (1998) J. Comput. Chem, 19 (14), pp. 1639-1662
Jeong, S. S., Gready, J. E., A method of preparation and purification of (4R) -deuterated-reduced nicotinamide adenine dinucleotide phosphate (1994) Anal. Biochem, 221 (2), pp. 273-277
Schneider-Bernl hr, H., Adolph, H. -W., Zeppezauer, M., Coenzyme stereospecificity of Alcohol/Polyol Dehydrogenases: Conservation of Protein Types vs. Functional Constraints (1986) J. Am. Chem. Soc, 108 (18), pp. 5573-5576
Kwiecie, R. A., Ayadi, F., Nemmaoui, Y., Silvestre, V., Zhang, B. L., Robins, R. J., Probing stereoselectivity and pro-chirality of hydride transfer during short-chain alcohol dehydrogenase activity: A combined quantitative 2H NMR and computational approach (2009) Arch. Biochem. Biophys, 482 (1-2), pp. 42-51
Insight into the stereospecificity of short-chain Thermus thermophilus alcohol dehydrogenase showing pro-S hydride transfer and Prelog enantioselectivity
The stereochemistry of the hydride transfer in reactions catalyzed by NAD(H)-dependent alcohol dehydrogenase from Thermus thermophilus HB27 was determined by means of 1H-NMR spectroscopy. The enzyme transfers the pro-S hydrogen of [4R-2H]NADH and exhibits Prelog specificity. Enzyme-substrate docking calculations provided structural details about the enantioselectivity of this thermophilic enzyme. These results give additional insights into the diverse active site architectures of the largely versatile short-chain dehydrogenase superfamily enzymes. A feasible protocol for the synthesis of [4R-2H]NADH with high yield was also set up by enzymatic oxidation of 2-propanol-d8 catalyzed by Bacillus stearothermophilus alcohol dehydrogenase. © 2010 Bentham Science Publishers Ltd.
The stereochemistry of the hydride transfer in reactions catalyzed by NAD(H)-dependent alcohol dehydrogenase from Thermus thermophilus HB27 was determined by means of 1H-NMR spectroscopy. The enzyme transfers the pro-S hydrogen of [4R-2H]NADH and exhibits Prelog specificity. Enzyme-substrate docking calculations provided structural details about the enantioselectivity of this thermophilic enzyme. These results give additional insights into the diverse active site architectures of the largely versatile short-chain dehydrogenase superfamily enzymes. A feasible protocol for the synthesis of [4R-2H]NADH with high yield was also set up by enzymatic oxidation of 2-propanol-d8 catalyzed by Bacillus stearothermophilus alcohol dehydrogenase. © 2010 Bentham Science Publishers Ltd.
Insight into the stereospecificity of short-chain Thermus thermophilus alcohol dehydrogenase showing pro-S hydride transfer and Prelog enantioselectivity
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Insight into the stereospecificity of short-chain Thermus thermophilus alcohol dehydrogenase showing pro-S hydride transfer and Prelog enantioselectivity
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Amino Acids (ISSN: 1438-2199, 0939-4451, 1438-2199electronic), 2010 May; 38(5): 1301-1309.
Impact Factor: 4.106
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Cucinotta V, Giuffrida A, Grasso G, Maccarrone G, Messina M, Vecchio G
* High selectivity in new chiral separations of dansyl amino acids by cyclodextrin derivatives in electrokinetic chromatography (290 views)
J Chromatogr A (ISSN: 0021-9673, 0021-9673linking), 2007; 1155(2): 172-179.
Impact Factor: 3.641
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Cucinotta V, Giuffrida A, La Mendola D, Maccarrone G, Puglisi A, Rizzarelli E, Vecchio G
* 3-Amino Derivative Of Beta-Cyclodextrin: Thermodynamics Of Copper (ii) Complexes And Exploitation Of Its Enantioselectivity In The Separation Of Amino Acid Racemates By Ligand Exchange Capillary Electrophoresis (350 views)
And Life Sciencesjournal Of Chromatography B Analytical Technologies In The Biomedical, 2004 Feb 5; 800(1-2): 127-133.
Impact Factor: 1.403
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Formaggio F, Bonchio M, Crisma M, Peggion C, Mezzato S, Polese A, Barazza A, Antonello S, Maran F, Broxterman QB, Kaptein B, Kamphuis J, Vitale RM, Saviano M, Benedetti E, Toniolo C
* Nitroxyl peptides as catalysts of enantioselective oxidations (498 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2002; 8(1): [d]84-93.
Impact Factor: 4.238
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* Probing Molecular Interactions between Human Carbonic Anhydrases (hCAs) and a Novel Class of Benzenesulfonamides (386 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2017 May 25; 60(10): 4316-4326.
Impact Factor: 6.253
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Roviello GN, Gröschel S, Pedone C, Diederichsen U
* Synthesis of novel MMT/acyl-protected nucleo alanine monomers for the preparation of DNA/alanyl-PNA chimeras (572 views)
Amino Acids (ISSN: 1438-2199, 0939-4451, 1438-2199electronic), 2010 May; 38(5): 1301-1309.
Impact Factor: 4.106
View Export to BibTeX Export to EndNote
Cucinotta V, Giuffrida A, Grasso G, Maccarrone G, Messina M, Vecchio G
* High selectivity in new chiral separations of dansyl amino acids by cyclodextrin derivatives in electrokinetic chromatography (290 views)
J Chromatogr A (ISSN: 0021-9673, 0021-9673linking), 2007; 1155(2): 172-179.
Impact Factor: 3.641
View Export to BibTeX Export to EndNote
Cucinotta V, Giuffrida A, La Mendola D, Maccarrone G, Puglisi A, Rizzarelli E, Vecchio G
* 3-Amino Derivative Of Beta-Cyclodextrin: Thermodynamics Of Copper (ii) Complexes And Exploitation Of Its Enantioselectivity In The Separation Of Amino Acid Racemates By Ligand Exchange Capillary Electrophoresis (350 views)
And Life Sciencesjournal Of Chromatography B Analytical Technologies In The Biomedical, 2004 Feb 5; 800(1-2): 127-133.
Impact Factor: 1.403
View Export to BibTeX Export to EndNote
Formaggio F, Bonchio M, Crisma M, Peggion C, Mezzato S, Polese A, Barazza A, Antonello S, Maran F, Broxterman QB, Kaptein B, Kamphuis J, Vitale RM, Saviano M, Benedetti E, Toniolo C
* Nitroxyl peptides as catalysts of enantioselective oxidations (498 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2002; 8(1): [d]84-93.
Impact Factor: 4.238
View Export to BibTeX Export to EndNote
5 Records (5 excluding Abstracts).
Total impact factor: 19.641 (19.641 excluding Abstracts).
Total 5 year impact factor: 20.125 (20.125 excluding Abstracts).
Total impact factor: 19.641 (19.641 excluding Abstracts).
Total 5 year impact factor: 20.125 (20.125 excluding Abstracts).
520 views. Last view on Saturday 03 June 2023, 14:40:30
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