Asymmetric reduction of activated alkenes using an enoate reductase from Gluconobacter oxydans

Richter N, Gröger H, Hummel W (2011)
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 89(1): 79-89.

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Abstract
A recombinant enoate reductase from Gluconobacter oxydans was heterologously expressed, purified, characterised and applied in the asymmetric reduction of activated alkenes. In addition to the determination of the kinetic properties, the major focus of this work was to utilise the enzyme in the biotransformation of different interesting compounds such as 3,5,5-trimethyl-2-cyclohexen-1,4-dione (ketoisophorone) and (E/Z)-3,7-dimethyl-2,6-octadienal (citral). The reaction proceeded with excellent stereoselectivities (>99% ee) as well as absolute chemo-and regioselectivity, only the activated C-C bond of citral was reduced by the enoate reductase, while non-activated C-C bond and carbonyl moiety remained untouched. The described strategy can be used for the production of enantiomerically pure building blocks, which are difficult to prepare by chemical means. In general, the results show that the investigated enoate reductase is a promising catalyst for the use in asymmetric C-C bond reductions.
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Richter N, Gröger H, Hummel W. Asymmetric reduction of activated alkenes using an enoate reductase from Gluconobacter oxydans. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY. 2011;89(1):79-89.
Richter, N., Gröger, H., & Hummel, W. (2011). Asymmetric reduction of activated alkenes using an enoate reductase from Gluconobacter oxydans. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 89(1), 79-89.
Richter, N., Gröger, H., and Hummel, W. (2011). Asymmetric reduction of activated alkenes using an enoate reductase from Gluconobacter oxydans. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 89, 79-89.
Richter, N., Gröger, H., & Hummel, W., 2011. Asymmetric reduction of activated alkenes using an enoate reductase from Gluconobacter oxydans. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 89(1), p 79-89.
N. Richter, H. Gröger, and W. Hummel, “Asymmetric reduction of activated alkenes using an enoate reductase from Gluconobacter oxydans”, APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, vol. 89, 2011, pp. 79-89.
Richter, N., Gröger, H., Hummel, W.: Asymmetric reduction of activated alkenes using an enoate reductase from Gluconobacter oxydans. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY. 89, 79-89 (2011).
Richter, Nina, Gröger, Harald, and Hummel, Werner. “Asymmetric reduction of activated alkenes using an enoate reductase from Gluconobacter oxydans”. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 89.1 (2011): 79-89.
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10 Citations in Europe PMC

Data provided by Europe PubMed Central.

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PMID: 24835095
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Yin B, Cui D, Zhang L, Jiang S, Machida S, Yuan YA, Wei D., Proteins 82(11), 2014
PMID: 24825769
Carbon-carbon double-bond reductases in nature.
Huang M, Hu H, Ma L, Zhou Q, Yu L, Zeng S., Drug Metab. Rev. 46(3), 2014
PMID: 24750117
An ene reductase from Clavispora lusitaniae for asymmetric reduction of activated alkenes.
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PMID: 24564901
New generation of biocatalysts for organic synthesis.
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PMID: 24520044
Highly enantioselective reduction of α-methylated nitroalkenes.
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Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds.
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47 References

Data provided by Europe PubMed Central.


A, J Mol Catal B Enzym 38(), 2006
Stereospecific alkyne reduction: novel activity of old yellow enzymes.
Muller A, Sturmer R, Hauer B, Rosche B., Angew. Chem. Int. Ed. Engl. 46(18), 2007
PMID: 17387664
Asymmetric catalysis: science and opportunities (Nobel lecture).
Noyori R., Angew. Chem. Int. Ed. Engl. 41(12), 2002
PMID: 19746595

T, J Org Chem 60(), 1995
Enoate reductases of Clostridia. Cloning, sequencing, and expression.
Rohdich F, Wiese A, Feicht R, Simon H, Bacher A., J. Biol. Chem. 276(8), 2001
PMID: 11060310
The cloning and expression of a gene encoding Old Yellow Enzyme from Saccharomyces carlsbergensis.
Saito K, Thiele DJ, Davio M, Lockridge O, Massey V., J. Biol. Chem. 266(31), 1991
PMID: 1939123
Vinyl ketone reduction by three distinct Gluconobacter oxydans 621H enzymes.
Schweiger P, Gross H, Wesener S, Deppenmeier U., Appl. Microbiol. Biotechnol. 80(6), 2008
PMID: 18629490

AUTHOR UNKNOWN, 0

AUTHOR UNKNOWN, 0
The occurrence of a novel NADH dehydrogenase, distinct from the old yellow enzyme, in Gluconobacter strains.
Shinagawa E, Ano Y, Adachi O, Matsushita K., Biosci. Biotechnol. Biochem. 72(1), 2008
PMID: 18175896
Old Yellow Enzyme. The discovery of multiple isozymes and a family of related proteins.
Stott K, Saito K, Thiele DJ, Massey V., J. Biol. Chem. 268(9), 1993
PMID: 8454584
A homolog of old yellow enzyme in tomato. Spectral properties and substrate specificity of the recombinant protein.
Strassner J, Furholz A, Macheroux P, Amrhein N, Schaller A., J. Biol. Chem. 274(49), 1999
PMID: 10574986
Asymmetric bioreduction of activated C=C bonds using enoate reductases from the old yellow enzyme family.
Stuermer R, Hauer B, Hall M, Faber K., Curr Opin Chem Biol 11(2), 2007
PMID: 17353140

AF, J Catal 224(), 2004

O, Naturwissenschaften 20(), 1932

AUTHOR UNKNOWN, 0
'New uses for an Old Enzyme'--the Old Yellow Enzyme family of flavoenzymes.
Williams RE, Bruce NC., Microbiology (Reading, Engl.) 148(Pt 6), 2002
PMID: 12055282

Y, Agric Biol Chem 52(), 1988
Nitroreductase from Salmonella typhimurium: characterization and catalytic activity.
Yanto Y, Hall M, Bommarius AS., Org. Biomol. Chem. 8(8), 2010
PMID: 20449486

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