Galactose Oxidase - an overview | ScienceDirect Topics
Galactose oxidase is a free radical metalloenzyme containing a novel metalloradical complex, comprised of a protein radical coordinated to a copper ion in the active site. The unusually stable protein radical is formed from the redox-active side chain of …
Oxidation with galactose oxidase: Multifunctional enzymatic …
Oct 1, 2015 · Galactose oxidase (EC 1.1.3.9) is a single copper metalloenzyme, having a molecular weight of 65–68 kDa. Galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group.
Galactose oxidase - ScienceDirect
Jan 1, 2002 · Galactose oxidase (GAOX) is an extraordinary copper metalloenzyme, combining the reactivity of a free radical ligand with a redox-active metal center in a unique catalytic complex, the free radical-coupled copper active site.
Catalytic Promiscuity of Galactose Oxidase: A Mild Synthesis of ...
Sep 3, 2018 · We report an unprecedented catalytically promiscuous activity of the copper-dependent enzyme galactose oxidase. The enzyme catalyses the one-pot conversion of alcohols into the related nitriles under mild reaction conditions in ammonium buffer, consuming ammonia as the source of nitrogen and dioxygen (from air at atmospheric pressure) as the ...
Catalytic Galactose Oxidase Models: Biomimetic Cu(II ... - Science
Biomimetic functional models of the mononuclear copper enzyme galactose oxidase are presented that catalytically oxidize benzylic and allylic alcohols to aldehydes with O 2 under mild conditions. The mechanistic fidelity between the models and the natural system is pronounced.
Structure and mechanism of galactose oxidase: catalytic role of ...
Provided by the Springer Nature SharedIt content-sharing initiative. Key words Galactose oxidase. Copper. Tyrosine free radical. Proton abstraction. The catalytic mechanism of the copper-containing enzyme galactose oxidase involves a protein radical on Tyr272, one of the equatorial copper ligands.
Galactose Oxidase Model Complexes: Catalytic Reactivities
Dec 25, 1996 · Marked Stabilization of Redox States and Enhanced Catalytic Activity in Galactose Oxidase Models Based on Transition Metal S-Methylisothiosemicarbazonates with −SR Group in Ortho Position to the Phenolic Oxygen.
Galactose oxidase - PubMed
Abstract. The free radical-coupled copper catalytic motif has emerged as the unifying feature of a new family of enzymes, the radical copper oxidases. Their highly evolved active sites include a novel amino acid modification, the Tyr-Cys dimer, that forms spontaneously through self-processing of the protein during its maturation.
Structure–function characterization reveals new catalytic …
Dec 18, 2015 · EPR spectroscopy and crystallographic analysis confirm a common active-site structure vis-à-vis the archetypal galactose 6-oxidase from Fusarium graminearum.
Electrochemical studies of galactose oxidase - Figueiredo - 2022 ...
Nov 8, 2021 · Galactose oxidase (GOase; E.C. 1.1.3.9) is a copper metalloenzyme found mainly in the fungi Gibberella fujikuroi, Fusarium graminearum, and the most extensively characterized Dactylium dendroides. GOase is categorized as a mononuclear type II copper-containing enzyme, and it is composed of a single polypeptide with a molecular mass of ca. 68 kDa
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