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Volumn 46, Issue 21, 2007, Pages 3934-3937

Asymmetric bioreduction of activated alkenes using cloned 12-oxophytodienoate reductase isoenzymes OPR-1 and OPR-3 from Lycopersicon esculentum (tomato): A striking change of stereoselectivity

Author keywords

Asymmetric catalysis; Carbonyl compounds; Enzymes; Oxidoreductases; Reduction

Indexed keywords

ASYMMETRIC CATALYSIS; CARBONYL COMPOUNDS; ENONES; NITROALKENE; OXIDOREDUCTASES; STEREOISOMERS;

EID: 34250782749     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200605168     Document Type: Article
Times cited : (155)

References (60)
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    • The family of flavin-dependent old yellow enzymes represents a quite heterogeneous group of proteins that have been shown to reduce not only conjugated enals, enones, α,β-unsaturated carboxylic acids, and nitroalkenes, but also to reductively cleave nitroesters, and reduce aromatic nitro groups and electron-deficient aromatics; see Ref, 5
    • The family of flavin-dependent old yellow enzymes represents a quite heterogeneous group of proteins that have been shown to reduce not only conjugated enals, enones, α,β-unsaturated carboxylic acids, and nitroalkenes, but also to reductively cleave nitroesters, and reduce aromatic nitro groups and electron-deficient aromatics; see Ref. [5].
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    • General procedures for the asymmetric bioreduction of compounds 1a-7a, for the recycling of cofactors using FDH, GDH, and G6PDH, the sources of enzymes and substrates, as well as analytical procedures and proof of absolute configuration of products are given in the Supporting Information.
    • General procedures for the asymmetric bioreduction of compounds 1a-7a, for the recycling of cofactors using FDH, GDH, and G6PDH, the sources of enzymes and substrates, as well as analytical procedures and proof of absolute configuration of products are given in the Supporting Information.
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    • In contrast to carbonyl reductases that show a rather pronounced preference for either NADH or NADPH, enoate reductases seem to be less specific: their preference for NADH over NADPH may vary significantly, with a ratio of relative activities that range from 0.02:1 to 10:1; see: a R. E. Williams, D. A. Rathbone, N. S. Scrutton, N. C. Bruce, Appl. Environ. Microbiol. 2004, 70, 3566-3574;
    • In contrast to carbonyl reductases that show a rather pronounced preference for either NADH or NADPH, enoate reductases seem to be less specific: their preference for NADH over NADPH may vary significantly, with a ratio of relative activities that range from 0.02:1 to 10:1; see: a) R. E. Williams, D. A. Rathbone, N. S. Scrutton, N. C. Bruce, Appl. Environ. Microbiol. 2004, 70, 3566-3574;
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    • This value is derived from the difference in energies for the destruction of the stereoselectivity for (R)-7b (99, ee, which amounts to 3.14 kcalM-1) and the generation of stereoselectivity in the opposite direction to (S)-7b 93, ee, which amounts to 1.96 kcalM -1
    • -1).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.