Abstract
Two ketoreductases from Candida glabrata were used for the asymmetric reduction of prochiral substituted acetophenones displayed different enantiopreference toward para-, meta-substituted and ortho-halogen substituted acetophenones with excellent enantioselectivity. Homology modeling and docking analysis were in conformity with this interested enantiopreference obtained from experimental tests. The reduction of a series of other substituted aryl ketones was also investigated using the two ketoreductases.
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Ankati H, Zhu D, Yang Y, Biehl ER, Hua L (2009) Asymmetric synthesis of both antipodes of β-hydroxy nitriles and β-hydroxy carboxylic acids via enzymatic reduction or sequential reduction/hydrolysis. J Org Chem 74:1658–1662
Bornscheuer UT, Huisman GW, Kazlauskas RJ, Lutz S, Moore JC, Robins K (2012) Engineering the third wave of biocatalysis. Nature 485:185–194
Ernst M, Kaup B, Müller M, Bringer-Meyer S, Sahm H (2005) Enantioselective reduction of carbonyl compounds by whole-cell biotransformation, combining a formate dehydrogenase and a (R)-specific alcohol dehydrogenase. Appl Microbiol Biot 66:629–634
Hall Ml, Bommarius AS (2011) Enantioenriched compounds via enzyme-catalyzed redox reactions. Chem Rev 111:4088–4110
Hollmann F, Arends IWCE, Holtmann D (2011) Enzymatic reductions for the chemist. Green Chem 13:2285–2314
Huisman GW, Liang J, Krebber A (2010) Practical chiral alcohol manufacture using ketoreductases. Curr Opin Chem Biol 14:122–129
Kamitori S, Iguchi A, Ohtaki A, Yamada M, Kita K (2005) X-ray structures of nadph-dependent carbonyl reductase from Sporobolomyces salmonicolor provide insights into stereoselective reductions of carbonyl compounds. J Mol Biol 352:551–558
Liang J, Lalonde J, Borup B, Mitchell V, Mundorff E, Trinh N, Kochrekar DA, Nair Cherat R, Pai GG (2009a) Development of a biocatalytic process as an alternative to the (−)-DIP-Cl-mediated asymmetric reduction of a key intermediate of montelukast. Org Proc Res Dev 14:193–198
Liang J, Mundorff E, Voladri R, Jenne S, Gilson L, Conway A, Krebber A, Wong J, Huisman G, Truesdell S, Lalonde J (2009b) Highly enantioselective reduction of a small heterocyclic ketone: biocatalytic reduction of tetrahydrothiophene-3-one to the corresponding (R)-alcohol. Org Process Res Dev 14:188–192
Ma SK, Gruber J, Davis C, Newman L, Gray D, Wang A, Grate J, Huisman GW, Sheldon RA (2010) A green-by-design biocatalytic process for atorvastatin intermediate. Green Chem 12:81–86
Ma H, Yang L, Ni Y, Zhang J, Li C-X, Zheng G-W, Yang H, Xu J-H (2012) Stereospecific reduction of methyl o-chlorobenzoylformate at 300 g l−1 without additional cofactor using a carbonyl reductase mined from Candida glabrata. Adv Synth Catal 354:1765–1772
Olsen JG, Pedersen L, Christensen CL, Olsen O, Henriksen A (2008) Barley aldose reductase: structure, cofactor binding, and substrate recognition in the aldo/keto reductase 4C family. Proteins 71:1572–1581
Prelog V (1964) Specification of the stereospecificity of some oxido-reductases by diamond lattice sections. Pure Appl Chem 9:119
Shen N-D, Ni Y, Ma H-M, Wang L-J, Li C-X, Zheng G-W, Zhang J, Xu J-H (2012) Efficient synthesis of a chiral precursor for angiotensin-converting enzyme (ace) inhibitors in high space–time yield by a new reductase without external cofactors. Org Lett 14:1982–1985
Wildeman S, Sonke T, Schoemaker H, May O (2007) Biocatalytic reductions: from lab curiosity to “first choice”. Acc Chem Res 40:1260–1266
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This work was financially supported by National Scientific Major Program (2010ZX09301-012) and Shenyang Municipal Scientific and Technology Research Fund (F11-243-1-00).
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Ping Liang and Bin Qin contributed equally to this study.
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Liang, P., Qin, B., Mu, M. et al. Prelog and anti-Prelog stereoselectivity of two ketoreductases from Candida glabrata . Biotechnol Lett 35, 1469–1473 (2013). https://doi.org/10.1007/s10529-013-1228-0
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DOI: https://doi.org/10.1007/s10529-013-1228-0