Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 411-418 |
| Journal | Advanced Synthesis & Catalysis |
| Volume | 350 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2008 |
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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 journal › Article › Research › peer-review
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TY - JOUR
T1 - Asymmetric bioreduction of C=C bonds using enoate reductases OPR1, OPR3 and YqjM: enzyme-based stereocontrol
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
PY - 2008
Y1 - 2008
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 CC 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 CC 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.
U2 - 10.1002/adsc.200700458
DO - 10.1002/adsc.200700458
M3 - Article
VL - 350
SP - 411
EP - 418
JO - Advanced Synthesis & Catalysis
JF - Advanced Synthesis & Catalysis
SN - 1615-4150
IS - 3
ER -