Synlett 2010(13): 2047-2048  
DOI: 10.1055/s-0030-1258509
© Georg Thieme Verlag Stuttgart ˙ New York

Alcohol Dehydrogenase

Zhen Yan*
School of Biotechnology and Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, 1800 Lihu Ave., Wuxi 214122, P. R. of China
Further Information

Publication History

Publication Date:
28 July 2010 (online)


Alcohol dehydrogenases (ADHs) can catalyze the reduction of carbonyl compounds, also referred to as carbony reductases, [¹] as well as the reverse reaction - the oxidation of the corresponding alcohols. [²] The most promising feature of ADHs is the strict recognition of the substrate which leads to very high chemo-, regio- and enantioselectivity. Although the demand for a stoichiometric amount of the expensive and unstable nicotinamide coenzyme NAD(P)H involved in ADHs catalyzing oxidoreductions is the major challenge for ADHs’ industrial application, many efficient coenzyme regeneration systems have been developed, [³] and the most common methods are known as enzyme-coupled and substrate-coupled approaches. ADHs are versatile biocatalysts in asymmetric synthesis of highly enantiomerical products, e.g. chiral alcohols, which are very important chiral building blocks for production of drugs, agrochemicals, and fine chemicals in chemical and pharmaceutical industry. [4]

ADHs from different species have been isolated and are commercially available in different preparations including purified enzymes, crude powders, and enzyme-­involving whole cells, and have been largely applied in the preparation of chiral alcohols and chiral hydroxyl compounds through asymmetric reactions. [5a,b]

ADHs catalyze the carbonyl reduction or the hydroxyl oxidation through hydride transfer between coenzyme and substrate (Scheme  [¹] ). Typically, the chiral products from ADHs catalyzing asymmetric reaction are optically active alcohols and corresponding chiral hydroxyl derivatives. Therefore, the applications of ADHs in organic synthesis mainly include asymmetric reduction of prochiral ketones, stereospecific oxidation of alcohols, resolution of racemic alcohols, and stereoinversion of chiral alcohol enantiomers.

Scheme 1 Principal reactions catalyzed by alcohol dehydrogenases


  • 1 Forrest GL. Gonzalez B. Chem. Biol. Interact.  2000,  129:  21 
  • 2 Reid MF. Fewson CA. Crit. Rev. Microbiol.  1994,  20:  13 
  • 3 Wichmann R. Vasic-Racki D. Adv. Biochem. Eng. Biotechnol.  2005,  92:  225 
  • 4 Panke S. Held M. Wubbolts M. Curr. Opin. Biotechnol.  2004,  15:  272 
  • 5a Moore JC. Pollard DJ. Kosjek B. Devine PN. Acc. Chem. Res.  2007,  40:  1412 
  • 5b De Wildeman SMA. Sonke T. Schoemaker HE. May O. Acc. Chem. Res.  2007,  40:  1260 
  • 6a Nakamura K. Yamanaka R. Matsuda T. Harada T. Tetrahedron: Asymmetry  2003,  14:  2659 
  • 6b Kizaki N. Yasohara Y. Hasegawa J. Wada M. Kataoka M. Shimizu S. Appl. Microbiol. Biot.  2001,  55:  590 
  • 7 Pollard D. Truppo M. Pollard J. Chen CY. Moore J. Tetrahedron: Asymmetry  2006,  17:  554 
  • 8 Musa MM. Ziegelmann-Fjeld KI. Vieile C. Zeikus JG. Phillips RS. J. Org. Chem.  2007,  72:  30 
  • 9 Pellissier H. Tetrahedron  2003,  59:  8291 
  • 10 Lüdeke S. Richter M. Müller M. Adv. Synth. Catal.  2009,  351:  253 
  • 11a Lee JM. Na Y. Han H. Chang S. Chem. Soc. Rev.  2004,  33:  302 
  • 11b Wasilke JC. Obrey SJ. Baker RT. Bazan GC. Chem. Rev.  2005,  105:  1001 
  • 12 Voss CV. Gruber CC. Faber K. Knaus T. Macheroux P. Kroutil W. J. Am. Chem. Soc.  2008,  130:  13969 
  • 13 Nie Y. Xu Y. Mu XQ. Org. Process Res. Dev.  2004,  8:  246 
  • 14 Edegger K. Mang H. Faber K. Gross J. Kroutil W.
    J. Mol. Catal. A: Chem.  2006,  251:  66