Access

Format

Author / Creator

Subject

Recently added

Eresources

Language

Place of Publication

Dates

Location

Sub-series 1: Angus & Robertson book reviews in bound volumes, 1894-1970

Cytochrome P450 enzymes catalyze a broad set of C–H activation reactions, the most prominent being hydroxylation. This review provides an overview of the regioselectivity (CH
3
-terminal, in-chain, and carboxylate-terminal) and the optical purity of the hydroxylation products obtained from fatty acids as far as described, focusing on systems close to preparative application.
Graphical Abstract

Catalysis letters, 2018-03, Vol.148 (3), p.787-812

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

The oxidation of alcohols to the corresponding carbonyl or carboxyl compounds represents a convenient strategy for the selective introduction of electrophilic carbon centres into carbohydrate-based starting materials. The O2-dependent oxidation of prim-alcohols by flavin-containing alcohol oxidases often yields mixtures of aldehyde and carboxylic acid, which is due to “over-oxidation” of the aldehyde hydrate intermediate. In order to directly convert alcohols into carboxylic acids, rational engineering of 5-(hydroxymethyl)furfural oxidase was performed. In an attempt to improve the binding of the aldehyde hydrate in the active site to boost aldehyde-oxidase activity, two active-site residues were exchanged for hydrogen-bond-donating and -accepting amino acids. Enhanced over-oxidation was demonstrated and Michaelis–Menten kinetics were performed to corroborate these findings.

Molecules (Basel, Switzerland), 2017-12, Vol.22 (12), p.2205

Rational Engineering of a Flavoprotein Oxidase for Improved Direct Oxidation of Alcohols to Carboxylic Acids

The bioreduction and disproportionation of cyclohex-2-enone catalyzed by Old Yellow Enzyme 1 was investigated in presence of organic (co)solvents. Whereas the NADH-dependent bioreduction activity strongly decreased at elevated co-solvent concentrations due to the insolubility of the nicotinamide-cofactor, the NADH-free disproportionation was significantly improved in water-immiscible organic co-solvents at 90 % (v/v) with near-quantitative conversion. This positive effect was attributed to removal of the inhibiting co-product, phenol, from the enzyme’s active site. The best co-solvents show high lipophilicity (logP) and a high potential to solubilize phenol (Kₚₕₑₙₒₗ). As a predictive parameter, the ratio of logP/Kₚₕₑₙₒₗ should be preferably ≥100.

Biotechnology letters, 2014-06, Vol.36 (6), p.1329-1333

Bioreduction and disproportionation of cyclohex-2-enone catalyzed by ene-reductase OYE-1 in ‘micro-aqueous’ organic solvents

Export record to excel

Export this record

Export record to excel

Sub-series 1: Angus & Robertson book reviews in bound volumes, 1894-1970

Export this record

Export record to excel

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

Export this record

Export record to excel

Rational Engineering of a Flavoprotein Oxidase for Improved Direct Oxidation of Alcohols to Carboxylic Acids

Export this record

Export record to excel

Bioreduction and disproportionation of cyclohex-2-enone catalyzed by ene-reductase OYE-1 in ‘micro-aqueous’ organic solvents

Refine your search