Thermostable dehydrogenase

Machielsen, R., Uria, A.R., Kengen, S.W.M. and van der Oost, J. (2006) Production and characterization of a thermostable alcohol dehydrogenase that belongs to the aldo-keto reductase superfamily. Applied and Environmental Microbiology, 72 (1), 233-238. 

Monooxygenase Assays. Incubation media contained the following (final concentrations) 0.05M phosphate buffer, pH 7.A, glucose-6-phosphate (G-6-P, 2.3 mM), G-6-P dehydrogenase (3 units), NADP (0.23 mM), and KC1 (2.8 mM), and various tissue preparations. Substrates were added in small volumes (25 yl or less) of MeOH. Samples (1.1 ml) were shaken in a thermostated (usually at 22°C) water bath and reactions terminated by enzyme denaturation. Specific analytical procedures for aldrin epoxi-dation (13), 1 CH30-p-nitroanisole 0-demethylation (1A), and 3H-benzo(a)pyrene oxidation (15) have been described. 

Tanner, J J., R.M. Hecht, and K.L. Krause. 1996. Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceralde-hyde-3-phosphate dehydrogenase at 25 Angstroms Resolution. Biochemistry 35 2597-2609. 

Oka, M., Yang, Y.S., Nagata, S., Esaki, N., Tanaka, M., and Soda, K. 1989. Overproduction of thermostable leucine dehydrogenase of Bacillus stearothermophilus and its one-step purification from recombinant cells of Escherichia coli. Biotechnol. Appl. Biochem. 11 307-316. Sassenfeld, H.M. 1990. Engineering proteins for purification. Trends Biotechnol. 8 88-93. 

N. Esaki, H. Tanaka, and K. Soda, Gene cloning, purification, and characterization of the highly thermostable leudne dehydrogenase of Bacillus sp., /. Ferment. Biotechnol. 1990, 69, 199-203. 

T. Ohshima, S. Nagata, and K. Soda, Purification and Characterization of thermostable leucine dehydrogenase from Bacillus stearothermophilus, Arch. Microbiol. 1985a, 141, 407 4-11. 

T. Ohshima, C. Wandrey, M. Sugiura, and K. Soda, Screening of thermostable leucine and alanine dehydrogenases in thermophilic Bacillus strains, Biotechnol. Lett. 

T. Ohshima and K. Soda, Thermostable amino acid dehydrogenases applications and gene cloning, Trends Biotechnol. 1989a, 7, 210-214. 

E Keinan, EK Hafeli, KK Seth, RR Lamed. Thermostable enzymes in organic synthesis. 2. Asymmetric reduction of ketones with alcohol dehydrogenase from Ther-moanaerobium brockii. J Am Chem Soc 108 162-168, 1986. 

K Imada, M Sato, N Tanaka, YKatsube, Y Matsuura, T Oshima. Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution. J Mol Biol 222 725-738, 1991. 

The relative activity of the fragmentary enzyme to the wild-type enzyme was much higher than that of the clipped to the native DadB enzyme. This was explained by the assumption that the thermostable enzyme has more extensive hydrophobic interdomain interactions than the DadB enzyme with less thermostability.12 The importance of hydrophobic interdomain interactions for catalysis was pointed out by studies on lactate dehydrogenase.23,24 ... 

Johannes TW, Woodyer RD, Zhao H. Directed evolution of a thermostable phosphite dehydrogenase for NAD(P)H regeneration. 

Kirino H, Aoki M, Aoshima M, Hayashi Y, Ohba M, Yamagishi A, Wakagi T, Oshima T. Hydrophobic interaction at the subunit 30. interface contributes to the thermostability of 3-isopropyhnalate dehydrogenase from an extreme thermophile, Thermus ther-mophilus. Eur. J. Biochem. 1994 220 275-281. 31. 

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