Results 61 to 70 of about 10,741 (164)

Single-domain flavoenzymes trigger lytic polysaccharide monooxygenases for oxidative degradation of cellulose

, 2016
The enzymatic conversion of plant biomass has been recently revolutionized by the discovery of lytic polysaccharide monooxygenases (LPMOs) that carry out oxidative cleavage of polysaccharides.
Berrin, Jean-Guy, J.-G., Rogniaux, Helene, Biaso, Frederic, Fanuel, Mathieu, Ropartz, David, D., Beccia, Maria Rosa, Record, Eric, Ropartz, David, Rogniaux-Bonaventure, Helene, H., Henrissat, Bernard, Garajova, Sonia, Garajova, Sona, Bennati-granier, Chloé, Guigliarelli, Bruno, Mathieu, Yann   +14 more
core   +1 more source

Glycerol dehydrogenase: Structure, specificity, and mechanism of a family III polyol dehydrogenase

, 2001
Background: Bacillus stearothermophilus glycerol dehydrogenase (GlyDH) (glycerol:NAD+ 2-oxidoreductase, EC 1.1.1.6) catalyzes the oxidation of glycerol to dihydroxyacetone (1,3-dihydroxypropanone) with concomitant reduction of NAD+ to NADH.
Baker PJ, Sveta Sedelnikova, Taylor R, Sedelnikova S, Baker, Patrick J., Rice DW, Muir, Nicola M., Gore, Michael G., Burke J, David W. Rice, Ruzheinikov, Sergey N., Bullough, Per A., Sedelnikova, Sveta, Sergey N. Ruzheinikov, Per A. Bullough, Patrick J. Baker, Gore MG, Burke, Jacky, Michael G. Gore, Muir NM, Bullough PA, Nicola M. Muir, Rice, David W., Robert Taylor, Ruzheinikov SN, Jacky Burke, Taylor, Robert   +26 more
core   +1 more source

An NADH dependent reductase for isolated enzyme and whole cell catalysis.

, 2006
Isolated enzymes and whole cell biocatalysts can both be applied for the synthesis of chiral hydroxy compounds. It is hypothesized that whole cells can easily be employed for such reactions using simple technology which is robust.
Shorrock, Vicky Jane, Shorrock, V.J.
core  

Asymmetric Chemoenzymatic Synthesis of Ramatroban Using Lipases and Oxidoreductases

, 2016
A chemoenzymatic asymmetric route for the preparation of enantiopure (R)-ramatroban has been developed for the first time. The action of lipases and oxidoreductases has been independently studied, and both were found as excellent biocatalysts for the ...
Eduardo Busto (1470310), Vicente Gotor (1566613), Vicente Gotor-Fernández (1616929)   +2 more
core   +1 more source

Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation

, 2012
Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H2O2 required by ligninolytic peroxidases for fungal degradation of lignin, the key step for carbon recycling in land ecosystems. O2 activation by Pleurotus eryngii AAO takes place
Hernández-Ortega, Aitor, Ferreira, Patricia, Martínez, Ángel T.   +2 more
core   +1 more source

Transcriptomic changes in barley leaves induced by alcohol ethoxylates indicate potential pathways of surfactant detoxification

Scientific Reports
Hardly anything is known regarding the detoxification of surfactants in crop plants, although they are frequently treated with agrochemical formulations.
Johanna Baales, Viktoria V. Zeisler-Diehl, Tino Kreszies, Alina Klaus, Frank Hochholdinger, Lukas Schreiber   +5 more
doaj   +1 more source

Development of a Thioredoxin-Based Cofactor Regeneration System for NADPH-Dependent Oxidoreductases

Nicotinamide cofactor-dependent oxidoreductases have become a valuable tool for the synthesis of high value chiral compounds. The feasibility of biocatalytic processes involving these enzymes stands and falls with the efficiency of the regeneration of ...
Ørtoft Kirkeby, Tanja, Kara, Selin, Loderer, Christoph, Zhang, Ningning, Müller, Beatrice   +4 more
core   +1 more source

Structure, function and redesign of vanillyl-alcohol oxidase [PDF]

, 2002
Vanillyl-alcohol oxidase (VAO) from Penicillium simplicissimum is an inducible flavoprotein involved in the biodegradation of lignin-derived aromatic compounds.
Mattevi, Andrea, Berkel, Willem J.H. van,, Fraaije, Marco W., Fraaije, Marco W.,, Berkel, Willem J.H. van, Mattevi, Andrea,, Heuvel, Robert H.H. van den,, Heuvel, Robert H.H. van den   +7 more
core   +1 more source

Structural insights into alcohol dehydrogenases catalyzing asymmetric reductions

, 2019
Alcohol dehydrogenases are a group of oxidoreductases that specifically use NAD(P)+ or NAD(P)H as cofactors for electron acceptance or donation and catalyze interconversion between alcohols and corresponding carbonyl compounds.
Yao Nie (475828), Yan Xu (14594), Jianhong An (231453)   +2 more
core   +1 more source

Inversion of stereospecificity of vanillyl-alcohol oxidase [PDF]

, 2000
Vanillyl-alcohol oxidase (VAO) is the prototype of a newly recognized family of structurally related oxidoreductases sharing a conserved FAD-binding domain.
Mattevi, Andrea, Ferrer, Miriam, Berkel, Willem J.H. van, Fraaije, M.W., van Berkel, W.J.H., Berkel, W.J.H., van, Mattevi, A., Berkel, Willem J.H. van,, van den Heuvel, R.H.H., Ferrer, M., Fraaije, Marco W., Fraaije, Marco W.,, Mattevi, Andrea,, Heuvel, R.H.H., van den, Ferrer, Miriam,, Heuvel, Robert H.H. van den,, Heuvel, Robert H.H. van den   +16 more
core   +1 more source