Asymmetric bioreduction of C=C bonds using enoate reductases OPR1, OPR3 and YqjM: enzyme-based stereocontrol

Melanie Hall, Clemens Stueckler, Heidemarie Ehammer, Eva Maria Pointner, Gustav Oberdorfer, Karl Gruber, Bernhard Hauer, Rainer Stuermer, Wolfgang Kroutil, Peter Macheroux, Kurt Faber

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Three cloned enoate reductases from the “old yellow enzyme” family of flavoproteins were investigated in the asymmetric bioreduction of activated alkenes. 12‐Oxophytodienoate reductase isoenzymes OPR1 and OPR3 from Lycopersicon esculentum (tomato), and YqjM from Bacillus subtilis displayed a remarkably broad substrate spectrum by reducing α,β‐unsaturated aldehydes, ketones, maleimides and nitroalkenes. The reaction proceeded with absolute chemoselectivity – only the conjugated CC bond was reduced, while isolated olefins and carbonyl groups remained intact – with excellent stereoselectivities (ees up to >99%). Upon reduction of a nitroalkene, the stereochemical outcome could be determined via choice of the appropriate enzyme (OPR1 versus OPR3 or YqjM), which furnished the corresponding enantiomeric nitroalkanes in excellent ee. Molecular modelling suggests that this “enzyme‐based stereocontrol” is caused by subtle differences within the active site geometries.
Original languageEnglish
Pages (from-to)411-418
JournalAdvanced Synthesis & Catalysis
Volume350
Issue number3
DOIs
Publication statusPublished - 2008

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Alkenes
Olefins
Oxidoreductases
Maleimides
Enzymes
Isoenzymes
NADPH Dehydrogenase
Flavoproteins
Stereoselectivity
Molecular modeling
Bacilli
Ketones
Aldehydes
Geometry
Substrates

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Asymmetric bioreduction of C=C bonds using enoate reductases OPR1, OPR3 and YqjM: enzyme-based stereocontrol. / Hall, Melanie; Stueckler, Clemens; Ehammer, Heidemarie; Pointner, Eva Maria; Oberdorfer, Gustav; Gruber, Karl; Hauer, Bernhard; Stuermer, Rainer; Kroutil, Wolfgang; Macheroux, Peter; Faber, Kurt.

In: Advanced Synthesis & Catalysis, Vol. 350, No. 3, 2008, p. 411-418.

Research output: Contribution to journalArticleResearchpeer-review

Hall, Melanie ; Stueckler, Clemens ; Ehammer, Heidemarie ; Pointner, Eva Maria ; Oberdorfer, Gustav ; Gruber, Karl ; Hauer, Bernhard ; Stuermer, Rainer ; Kroutil, Wolfgang ; Macheroux, Peter ; Faber, Kurt. / Asymmetric bioreduction of C=C bonds using enoate reductases OPR1, OPR3 and YqjM: enzyme-based stereocontrol. In: Advanced Synthesis & Catalysis. 2008 ; Vol. 350, No. 3. pp. 411-418.
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abstract = "Three cloned enoate reductases from the “old yellow enzyme” family of flavoproteins were investigated in the asymmetric bioreduction of activated alkenes. 12‐Oxophytodienoate reductase isoenzymes OPR1 and OPR3 from Lycopersicon esculentum (tomato), and YqjM from Bacillus subtilis displayed a remarkably broad substrate spectrum by reducing α,β‐unsaturated aldehydes, ketones, maleimides and nitroalkenes. The reaction proceeded with absolute chemoselectivity – only the conjugated CC bond was reduced, while isolated olefins and carbonyl groups remained intact – with excellent stereoselectivities (ees up to >99{\%}). Upon reduction of a nitroalkene, the stereochemical outcome could be determined via choice of the appropriate enzyme (OPR1 versus OPR3 or YqjM), which furnished the corresponding enantiomeric nitroalkanes in excellent ee. Molecular modelling suggests that this “enzyme‐based stereocontrol” is caused by subtle differences within the active site geometries.",
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AU - Hall, Melanie

AU - Stueckler, Clemens

AU - Ehammer, Heidemarie

AU - Pointner, Eva Maria

AU - Oberdorfer, Gustav

AU - Gruber, Karl

AU - Hauer, Bernhard

AU - Stuermer, Rainer

AU - Kroutil, Wolfgang

AU - Macheroux, Peter

AU - Faber, Kurt

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N2 - Three cloned enoate reductases from the “old yellow enzyme” family of flavoproteins were investigated in the asymmetric bioreduction of activated alkenes. 12‐Oxophytodienoate reductase isoenzymes OPR1 and OPR3 from Lycopersicon esculentum (tomato), and YqjM from Bacillus subtilis displayed a remarkably broad substrate spectrum by reducing α,β‐unsaturated aldehydes, ketones, maleimides and nitroalkenes. The reaction proceeded with absolute chemoselectivity – only the conjugated CC bond was reduced, while isolated olefins and carbonyl groups remained intact – with excellent stereoselectivities (ees up to >99%). Upon reduction of a nitroalkene, the stereochemical outcome could be determined via choice of the appropriate enzyme (OPR1 versus OPR3 or YqjM), which furnished the corresponding enantiomeric nitroalkanes in excellent ee. Molecular modelling suggests that this “enzyme‐based stereocontrol” is caused by subtle differences within the active site geometries.

AB - Three cloned enoate reductases from the “old yellow enzyme” family of flavoproteins were investigated in the asymmetric bioreduction of activated alkenes. 12‐Oxophytodienoate reductase isoenzymes OPR1 and OPR3 from Lycopersicon esculentum (tomato), and YqjM from Bacillus subtilis displayed a remarkably broad substrate spectrum by reducing α,β‐unsaturated aldehydes, ketones, maleimides and nitroalkenes. The reaction proceeded with absolute chemoselectivity – only the conjugated CC bond was reduced, while isolated olefins and carbonyl groups remained intact – with excellent stereoselectivities (ees up to >99%). Upon reduction of a nitroalkene, the stereochemical outcome could be determined via choice of the appropriate enzyme (OPR1 versus OPR3 or YqjM), which furnished the corresponding enantiomeric nitroalkanes in excellent ee. Molecular modelling suggests that this “enzyme‐based stereocontrol” is caused by subtle differences within the active site geometries.

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