Premium
Asymmetric Bioreduction of CC Bonds using Enoate Reductases OPR1, OPR3 and YqjM: Enzyme‐Based Stereocontrol
Author(s) -
Hall Mélanie,
Stueckler Clemens,
Ehammer Heidemarie,
Pointner Eva,
Oberdorfer Gustav,
Gruber Karl,
Hauer Bernard,
Stuermer Rainer,
Kroutil Wolfgang,
Macheroux Peter,
Faber Kurt
Publication year - 2008
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.200700458
Subject(s) - chemistry , biocatalysis , substrate (aquarium) , stereochemistry , bacillus subtilis , enzyme , double bond , reductase , chemoselectivity , conjugated system , enantioselective synthesis , enantiomeric excess , organic chemistry , catalysis , reaction mechanism , oceanography , polymer , biology , bacteria , genetics , geology
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 ( ee s 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.