Stereocomplementary Bioreduction of α,β-Unsaturated Dicarboxylic Acids and Dimethyl Esters using Enoate Reductases: Enzyme- and Substrate-Based Stereocontrol
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A site-saturated mutagenesis study of pentaerythritol tetranitrate reductase reveals that residues 181 and 184 influence ligand binding, stereochemistry and reactivityThe Structure of Glycerol Trinitrate Reductase NerA fromAgrobacterium radiobacterReveals the Molecular Reason for Nitro- and Ene-Reductase Activity in OYE HomologuesResidues Controlling Facial Selectivity in an Alkene Reductase and Semirational Alterations to Create Stereocomplementary VariantsChemoenzymatic asymmetric synthesis of pregabalin precursors via asymmetric bioreduction of β-cyanoacrylate esters using ene-reductasesAsymmetric bioreduction of activated alkenes to industrially relevant optically active compounds.Structural insights into the ene-reductase synthesis of profens.Overcoming co-product inhibition in the nicotinamide independent asymmetric bioreduction of activated C=C-bonds using flavin-dependent ene-reductasesStructure-Based Insight into the Asymmetric Bioreduction of the C=C Double Bond of alpha,beta-Unsaturated Nitroalkenes by Pentaerythritol Tetranitrate Reductase.Asymmetric Reduction of Activated Alkenes by Pentaerythritol Tetranitrate Reductase: Specificity and Control of Stereochemical Outcome by Reaction Optimisation.NAD(P)H-independent asymmetric C=C bond reduction catalyzed by ene reductases by using artificial co-substrates as the hydrogen donor.Nitrile as Activating Group in the Asymmetric Bioreduction of β-Cyanoacrylic Acids Catalyzed by Ene-ReductasesFunctional characterization and stability improvement of a 'thermophilic-like' ene-reductase from Rhodococcus opacus 1CPAsymmetric bioreduction of activated carbon-carbon double bonds using Shewanella yellow enzyme (SYE-4) as novel enoate reductase.Alkene hydrogenation activity of enoate reductases for an environmentally benign biosynthesis of adipic acid.Unusual C=C bond isomerization of an α,β-unsaturated γ-butyrolactone catalysed by flavoproteins from the old yellow enzyme family.Better than Nature: Nicotinamide Biomimetics That Outperform Natural CoenzymesA thermophilic-like ene-reductase originating from an acidophilic iron oxidizer.Exploring De Novo metabolic pathways from pyruvate to propionic acid.Revealing Additional Stereocomplementary Pairs of Old Yellow Enzymes by Rational Transfer of Engineered Residues.Systematic methodology for the development of biocatalytic hydrogen-borrowing cascades: application to the synthesis of chiral α-substituted carboxylic acids from α-substituted α,β-unsaturated aldehydes.Nicotinamide-Dependent Ene Reductases as Alternative Biocatalysts for the Reduction of Activated AlkenesA surprising observation that oxygen can affect the product enantiopurity of an enzyme-catalysed reaction
P2860
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P2860
Stereocomplementary Bioreduction of α,β-Unsaturated Dicarboxylic Acids and Dimethyl Esters using Enoate Reductases: Enzyme- and Substrate-Based Stereocontrol
description
im Dezember 2007 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в грудні 2007
@uk
name
Stereocomplementary Bioreducti ...... Substrate-Based Stereocontrol
@en
Stereocomplementary Bioreducti ...... Substrate-Based Stereocontrol
@nl
type
label
Stereocomplementary Bioreducti ...... Substrate-Based Stereocontrol
@en
Stereocomplementary Bioreducti ...... Substrate-Based Stereocontrol
@nl
prefLabel
Stereocomplementary Bioreducti ...... Substrate-Based Stereocontrol
@en
Stereocomplementary Bioreducti ...... Substrate-Based Stereocontrol
@nl
P2093
P50
P356
P1433
P1476
Stereocomplementary Bioreducti ...... Substrate-Based Stereocontrol
@en
P2093
Clemens Stueckler
Eva Pointner
Heidemarie Ehammer
Kurt Faber
P304
P356
10.1021/OL7019185
P407
P577
2007-12-01T00:00:00Z