Home Ricerca Sedi Chi siamo Organigramma Personale Contatti Didattica Login Documenti EN
Progetti in evidenza
INCIPIT
(Link esterno)

ISTAPCA
(1204 visite)

Fondo Europeo Pesca
(614 visite)

Euro-BioImaging
(Link esterno)

Fondazione Veronesi
(Link esterno)

LightDyNAmics
(1080 visite)

 INMiND
(1179 visite)

Instruct-IT
(Link esterno)

 PRIN
(1320 visite)

 eHealthNet
(1083 visite)

Ponrec
(1025 visite)

MFAG Grant
(1126 visite)

MERIT
(Link esterno)


Collegamenti

Contiene: [X]      Estesa     Autori: [X]  Tipo di lavoro: [X]
Data iniziale: Data finale: [X]      Sede: Affiliazione IBB     
    
[Pulisci modulo]



Insight into the stereospecificity of short-chain Thermus thermophilus alcohol dehydrogenase showing pro-S hydride transfer and Prelog enantioselectivity (124 visite)

Pennacchio A, Giordano A, Esposito L, Langella E, Rossi M, Raia CA

Protein And Peptide Letters (ISSN: 0929-8665, 1875-5305), 2010 Apr; 17(4): 437-443.

Tipo di articolo: Journal Article, , Impact factor: 1.849, Impact factor a 5 anni: 1.45, Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77949957731&partnerID=40&md5=4f6b4e76221e675ce349d72852226469

Parole chiave: 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,

Affiliazioni: *** 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


Riferimenti: 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



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.
Nessun risultato.
Nessun risultato.

Contiene: [X]      Estesa     Autori: [X]  Tipo di lavoro: [X]
Data iniziale: Data finale: [X]      Sede: Affiliazione IBB     
    
[Pulisci modulo]


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 (119 visite)
And Life Sciencesjournal Of Chromatography B Analytical Technologies In The Biomedical, 2004 Feb 5; 800(1-2): 127-133.
Impact Factor: 1.403
Dettagli    Esporta in BibTeX    Esporta in EndNote



1 Records (1 escludendo Abstract e Conferenze).
Impact factor totale: 1.403 (1.403 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 1.339 (1.339 escludendo Abstract e Conferenze).







    Esporta in BibTeX    Esporta in EndNote

Ultima modifica di Marco Comerci in data Thursday 19 March 2015, 14:24:23
124 visite. Ultima visita in data Monday 10 December 2018, 5:30:39

Webmaster and developer: Marco Comerci
Per problemi e suggerimenti: adminibb.cnr.it
Ultimo aggiornamento: Tuesday 11 December 2018, 12:37:42