Alcohol dehydrogenase from

Alcohol dehydrogenase-catalyzed reduction of ketones is a convenient method for the production of chiral alcohols. HLAD, the most thoroughly studied enzyme, has a broad substrate specificity and accommodates a variety of substrates (Table 11). It efficiendy reduces all simple four- to nine-membered cycHc ketones and also symmetrical and racemic cis- and trans-decalindiones (167). Asymmetric reduction of aUphatic acycHc ketones (C-4—C-10) (103,104) can be efficiendy achieved by alcohol dehydrogenase isolated from Thermoanaerohium hrockii (TBADH) (168). The enzyme is remarkably stable at temperatures up to 85°C and exhibits high tolerance toward organic solvents. Alcohol dehydrogenases from horse Hver and T. hrockii... 

Figure 8.2 Reduction of ketone with alcohol dehydrogenase from Thermoanaerobacter brockii using glucose-6-sulfate as a hydrogen source [3],...

A ruthenium complex [RuCl2(TPPTS)2]2 was used for regeneration of NADP+ to NADPH withhydrogen. Thus, 2-heptanonewas reduced with alcohol dehydrogenase from Thermoanaerobacter brockii in the presence of the mthenium complex, NAD P, and hydrogen at 60°C to (S)-2-heptanol in 40 % ee. Turnover number was reported to be 18 (Figure 8.6) [5cj. 

P Diketones can also be reduced diastereoselectively. Thus, a recombinant alcohol dehydrogenase from I. brevis (recLBADH) overexpressed in E. coli was used for... 

Hensgens CMH, J Vonck, J Van Beeumen, EFJ van Bruggen, TA Hansen (1993) Purification and characterization of an oxygen-labile, NAD-dependent alcohol dehydrogenase from Desulfovibrio gigas. J Bacterial 175 2859-2863. 

This pathway is supported by the demonstration of benzyl alcohol dehydrogenase, benzaldehyde dehydrogenase, benzoyl-CoA ligase, and benzoyl-CoA reductase activities in cell extracts (Biegert and Fuchs 1995). The benzyl alcohol dehydrogenase from benzyl alcohol-grown cells was similar in many of its properties to those from the aerobic bacteria Acinetobacter calcoaceticus and Pseudomonas putida (Biegert et al. 1995). 

Biegert T, U Altenschmidt, C Eckerskorn, G Euchs (1995) Purification and properties of benzyl alcohol dehydrogenase from a denitrifying Thauera sp. Arch Microbiol 163 418-423. 

Oubrie A, Rozeboom HJ, Kalk KH, Huizinga EG, Dijkstra BW. 2002. Crystal structure of qui-nohemoprotein alcohol dehydrogenase from Comamonas testosteroni Structural basis for substrate oxidation and electron transfer. J Biol Chem 211 3727-3732. 

Co-for-Zn substitution in alcohol dehydrogenase from Saccharomyces cerevisiae revealed a 100-fold increase in activity and a higher resistance of the modified protein to the inhibitory action of other divalent transition metals,1208 making the Co-modified enzyme suitable for biotechnological applications. 

DeTemino, D.M., Hartmeier, W. and Ansorge-Schumacher, M.B. (2005) Entrapment of the alcohol dehydrogenase from Lactobacillus kefir in polyvinyl alcohol for the synthesis of chiral hydrophobic alcohols in organic solvents. Enzyme and Microbial Technology, 36 (1), 3-9. 

A series of ethynyl ketones and ethynylketoesters were reduced enantioselectively to the corresponding nonracemic propargyl alcohols using a secondary alcohol dehydrogenase from... 

Weckbecker, A. and Hummel, W. (2006) Cloning, expression, and characterization of an (/ (-specific alcohol dehydrogenase from Lactobacillus kefir. Biocatalysis and Biotransformation, 24 (5), 380-389. 

Musa, M.M., Ziegelmann-Fjeld, K.I., Vieille, C. et al. (2007) Asymmetric reduction and oxidation of aromatic ketones and alcohols using W110A secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus. The Journal of Organic Chemistry, 72 (1), 30-34. 

B. Groen, J. Frank Jr, and J.A. Duine, Quinoprotein alcohol dehydrogenase from ethanol-grown Pseudomonas aeruginosa. Biochem. J. 223, 921-924 (1984). 

A. Oubrie, H.J. Rozeboom, K.H. Kalk, E.G. Huizinga, and B.W. Dijkstra, Crystal structure of qui-nohemoprotein alcohol dehydrogenase from Comamonas testosteroni. J. Biol. Chem. Til, 3727-3732 (2002). 

J. Razumiene, M. Niculescu, A. Ramanavicius, V. Laurinavicius, and E. Csoregi, Direct bioelectrocatalysis at carbon electrodes modified with quinohemoprotein alcohol dehydrogenase from Gluconobacter sp. 33. Electroanalysis 14, 43—49 (2002). 

Because the direct electrochemical oxidation of NAD(P)H has to take place at an anode potential of + 900 mV vs NHE or more, only rather oxidation-stable substrates can be transformed without loss of selectivity—thus limiting the applicability of this method. The electron transfer between NADH and the anode may be accellerated by the use of a mediator. At the same time, electrode fouling which is often observed in the anodic oxidation of NADH can be prevented. Synthetic applications have been described for the oxidation of 2-hexene-l-ol and 2-butanol to 2-hexenal and 2-butanone catalyzed by yeast alcohol dehydrogenase (YADH) and the alcohol dehydrogenase from Thermoanaerobium brockii (TBADH) repectively with indirect electrochemical... 

Y. Shibusawa, T. Fujiwara, H. Shindo and Y. Ito, Purification of alcohol dehydrogenase from bovine liver crude extract by dye-ligand affinity counter current chromatography. J. Chromatogr.B, 799 (2004) 239-244. 

G. B. Strambini, Singular oxygen effects on the room-temperature phosphorescence of alcohol dehydrogenase from horse liver, Biophys. J. 43, 127-130 (1983). 

N. Barboy and J. Feitelson, Quenching of tryptophan phosphorescence in alcohol dehydrogenase from horse liver and its temperature dependence, Photochem. Photobiol. 41, 9-13 (1985). 

Xerogel-encapsulated WHOA Secondary Alcohol Dehydrogenase from Thermoanaerohacter ethanolicus... 

Musa, M., Ziegelman-Fjeld, K., Vieille, C., Zeikus, J. and Phillips, R., Xerogel-encapsulated WHOA secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus performs asymmetric reduction of hydrophobic ketones in organic solvents. Angew. Chem. Int. Ed., 2007, 46, 3091-3094. 

Flatanaka T, Kawahara T, Asahi N, Tsuji M (1995) Effects of the structure of poly(vinyl alcohol) on the dehydrogenation reaction by poly(vinyl alcohol) dehydrogenase from Pseudomonas sp. 113P3 T. Biosci Biotechnol Biochem 59 1229-1231... 

Mori T, Sakimoto M et al (1998) Secondary alcohol dehydrogenase from a vinyl alcohol oligomer-degrading Geotrichum fermentans stabilization with Triton X-100 and activity toward polymers with polymerization degrees less than 20. World J Microbiol Biotechnoi 14 349-356... 

---