2012
DOI: 10.1002/ejoc.201200776
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Nicotinamide‐Dependent Ene Reductases as Alternative Biocatalysts for the Reduction of Activated Alkenes

Abstract: Four NAD(P)H‐dependent non‐flavin ene reductases have been investigated for their ability to reduce activated C=C bonds in an asymmetric fashion by using 20 structurally diverse substrates. In comparison with flavin‐dependent Old Yellow Enzyme homologues, a higher degree of electronic activation was required, because the best activities were obtained with enals and nitroalkenes rather than enones and carboxylic esters. Although FaEO from Fragaria x ananassa (strawberry) and its homologue SlEO from Solanum lyco… Show more

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Cited by 49 publications
(35 citation statements)
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“…Although NADPH is the preferred physiological coenzyme for OYE, the dependency on this commercially expensive compound can be circumvented by established recycling systems with dehydrogenases [12,18,[42][43][44][45], with alternative sources of hydride [46,47], or through a nicotinamide-independent disproportionation coupling reaction [48][49][50][51]. A highly promising and elegant alternative is the use of relatively inexpensive nicotinamide coenzyme biomimetics (NCBs) [52][53][54][55][56].…”
Section: Introductionmentioning
confidence: 99%
“…Although NADPH is the preferred physiological coenzyme for OYE, the dependency on this commercially expensive compound can be circumvented by established recycling systems with dehydrogenases [12,18,[42][43][44][45], with alternative sources of hydride [46,47], or through a nicotinamide-independent disproportionation coupling reaction [48][49][50][51]. A highly promising and elegant alternative is the use of relatively inexpensive nicotinamide coenzyme biomimetics (NCBs) [52][53][54][55][56].…”
Section: Introductionmentioning
confidence: 99%
“…Unlike in the case of substrate 1 a , a variety of ene‐reductases were able to reduce isomer 2 a at the expense of NADH by forming the expected saturated lactone 1 b in up to 75 % yield (Table 1, left). Whereas the most active enzyme (EBP1) showed only low stereoselectivity (20 % ee ), the “slow” proteins YqjM, OPR1 and YhdA gave ( R )‐ 1 b in up to >99 % ee 36. No switch in stereoselectivity could be detected, neither could any trace of CC‐isomerization product 1 a .…”
Section: Resultsmentioning
confidence: 98%
“…The chemoselective bioreduction of α,β-unsaturated alkenes represents an important tool in the synthesis of a lot of fine chemicals and pharmaceuticals [1][2][3]. Ene-reductases (ERs) belong to the flavin-containing "Old Yellow Enzyme" family (OYE, EC 1.6.99.1), which includes a class of I flavin-dependent oxidoreductases, which have been extensively studied for their ability to catalyze the asymmetric reduction of electronically activated C=C bonds, possessing electron-withdrawing substituents in the presence of cofactor-recycling systems for NAD(P)H [4][5][6][7][8][9][10][11][12][13][14]. Intracellular ER homologues from bacteria, yeasts, filamentous fungi and higher plants have been isolated and characterized since the 1990s [15][16][17][18][19][20][21][22][23][24][25].…”
Section: Introductionmentioning
confidence: 99%