Baker's yeast reduction of 3-phenylthiomethyl-2-butenolide and its derivatives: Synthesis of versatile chiral C5-building blocks for terpenoid synthesis

Takabe, Kunihiko; Hiyoshi, Hidetaka; Sawada, Hiroyuki; Tanaka, Masaya; Miyazaki, Akira; Yamada, Takashi; Katagiri, Takao; Yoda, Hidemi

doi:10.1016/0957-4166(92)80016-p

Cited by 26 publications

(12 citation statements)

References 13 publications

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“…Old Yellow Enzymes (OYE) or ene-reductases (ER) are flavoproteins catalyzing the asymmetric reduction of activated C = C bonds through a trans-hydrogenation reaction ( Stürmer et al, 2007 ). Creating up to two stereogenic centers, OYEs are versatile biocatalysts for the biotransformation of cyclic and acyclic enones and enals, α,β-unsaturated dicarboxylic acids and esters, maleimides, terpenoids, nitroalkenes, steroids as well as nitrate esters and nitroaromatics ( Leuenberger et al, 1976 ; Takabe et al, 1992 ; Vaz et al, 1995 ; Kataoka et al, 2002 , 2004 ; Kurata et al, 2004 ; Chaparro-Riggers et al, 2007 ; Hall et al, 2007 ; Stückler et al, 2007 ; Nivinskas et al, 2008 ; Fryszkowska et al, 2009 ; Adalbjörnsson et al, 2010 ; Mueller et al, 2010 ; Opperman et al, 2010 ; Toogood et al, 2010 ). Especially with maleimides, relevant products like the anticonvulsant drugs ethosuximide, phensuximide, and methsuximide can be synthesized.…”

Section: Introductionmentioning

confidence: 99%

Functional characterization and stability improvement of a ‘thermophilic-like’ ene-reductase from Rhodococcus opacus 1CP

et al. 2015

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Ene-reductases (ERs) are widely applied for the asymmetric synthesis of relevant industrial chemicals. A novel ER OYERo2 was found within a set of 14 putative old yellow enzymes (OYEs) obtained by genome mining of the actinobacterium Rhodococcus opacus 1CP. Multiple sequence alignment suggested that the enzyme belongs to the group of ‘thermophilic-like’ OYEs. OYERo2 was produced in Escherichia coli and biochemically characterized. The enzyme is strongly NADPH dependent and uses non-covalently bound FMNH2 for the reduction of activated α,β-unsaturated alkenes. In the active form OYERo2 is a dimer. Optimal catalysis occurs at pH 7.3 and 37°C. OYERo2 showed highest specific activities (45-50 U mg-1) on maleimides, which are efficiently converted to the corresponding succinimides. The OYERo2-mediated reduction of prochiral alkenes afforded the (R)-products with excellent optical purity (ee > 99%). OYERo2 is not as thermo-resistant as related OYEs. Introduction of a characteristic intermolecular salt bridge by site-specific mutagenesis raised the half-life of enzyme inactivation at 32°C from 28 to 87 min and improved the tolerance toward organic co-solvents. The suitability of OYERo2 for application in industrial biocatalysis is discussed.

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Section: Introductionmentioning

confidence: 99%

Functional characterization and stability improvement of a ‘thermophilic-like’ ene-reductase from Rhodococcus opacus 1CP

et al. 2015

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“…As a result of the high instability of HMMF, we decided to synthesize EDHMF, which needs not be trapped. [31] Although the unsubstituted test compound 15a and the α-methyl analogue 16a were poorly converted by LTB 4 DH/PGR (ca. under standard conditions.…”

Section: Resultsmentioning

confidence: 99%

Nicotinamide‐Dependent Ene Reductases as Alternative Biocatalysts for the Reduction of Activated Alkenes

et al. 2012

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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 lycopersicum (tomato) exhibited a narrow substrate spectrum, progesterone 5β‐reductase (At5β‐StR) from Arabidopsis thaliana (thale cress) and leukotriene B4 12‐hydroxydehydrogenase (LTB4DH/PGR) from Rattus norvegicus (rat) appear to be promising candidates, in particular for the asymmetric bioreduction of open‐chain enals, nitroalkenes and α,β‐unsaturated γ‐butyrolactones. Competing nitro reduction and non‐enzymatic Weitz–Scheffer epoxidation were largely suppressed.

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“…A further example of yeast reduction of a sulfide‐functionalised compound is the reduction of 3‐(phenylthiomethyl)‐2‐butenolide ( 66 ) reported by Takabe 85. In this example the double bond is reduced in preference to the carbonyl group to afford 2‐(phenylthiomethyl)butanolide ( 67 ) in 41 % yield and 99 % ee (Scheme ).…”

Section: Baker's‐yeast‐mediated Resolution Of Keto Sulfidesmentioning

confidence: 99%

Baker's‐Yeast‐Mediated Reduction of Sulfur‐Containing Compounds

Deasy

Maguire

2014

Eur J Org Chem

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Both the efficiency and the stereoselectivity in baker's‐yeast‐mediated reduction of ketones are strongly influenced by both the presence and the position of sulfur substituents, or indeed by the use of sulfur‐containing additives. Interestingly the oxidation level of the sulfur substituent has a powerful impact on the outcome of the yeast reduction. It is apparent that use of the sulfone moiety as a substituent to influence the efficiency and stereoselectivity in ketone reduction is substantially more effective than use of the analogous sulfide and sulfoxide moieties.

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Baker's yeast reduction of 3-phenylthiomethyl-2-butenolide and its derivatives: Synthesis of versatile chiral C5-building blocks for terpenoid synthesis

Cited by 26 publications

References 13 publications

Functional characterization and stability improvement of a ‘thermophilic-like’ ene-reductase from Rhodococcus opacus 1CP

Functional characterization and stability improvement of a ‘thermophilic-like’ ene-reductase from Rhodococcus opacus 1CP

Nicotinamide‐Dependent Ene Reductases as Alternative Biocatalysts for the Reduction of Activated Alkenes

Baker's‐Yeast‐Mediated Reduction of Sulfur‐Containing Compounds

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