Journal Article10.1016/J.MOLCATB.2015.06.006
Oxidation with galactose oxidase: Multifunctional enzymatic catalysis
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TL;DR: The various mono-, oligo- and polysaccharide derivatives that have been synthesized by galactose oxidase-catalyzed reactions, and the several either qualitative or quantitative analytical techniques utilized to follow of the reaction, determine the conversion, and identify the products are reviewed.
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Abstract: 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. The oxidation of alcohols to carbonyl compounds is one of the most important reactions in synthetic chemistry, thus enzymatic biocatalysis requiring only molecular oxygen as an oxidant is a valuable alternative to chemical reagents. We review here the various mono-, oligo- and polysaccharide derivatives that have been synthesized by galactose oxidase-catalyzed reactions, and the several either qualitative or quantitative analytical techniques utilized to follow of the reaction, determine the conversion, and identify the products. The optimal reaction conditions, the formation of side products, and the oxidation of substrates other than carbohydrates are discussed. Finally, we summarize engineering efforts of galactose oxidase that have improved recombinant enzyme expression and yield, or altered substrate specificity.
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Citations
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Recent advances in enzymatic oxidation of alcohols.
TL;DR: Different alcohol oxidation systems were used for the oxidation of primary and secondary alcohols, and biocatalyst with low enantioselectivity demonstrated an interesting feature for complete conversion of racemicsecondary alcohols through non-enantioseLECTive oxidation.
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Specific Identification of Glycoproteins Bearing the Tn Antigen in Human Cells
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References
Application of a very high-throughput digital imaging screen to evolve the enzyme galactose oxidase.
Simon Delagrave,Dennis J. Murphy,Jennifer L. Rittenhouse Pruss,Anthony M. Maffia,Barry L. Marrs,Edward J. Bylina,William J. Coleman,Christina L. Grek,Michael R. Dilworth,Mary M. Yang,Douglas C. Youvan +10 more
TL;DR: Digital imaging spectroscopy and a new solid-phase screening method are combined to screen enzyme variants on problematic substrates highly efficiently and it is shown here that the specific activity of the enzyme galactose oxidase can be improved using this technology.
Crystal structure of the precursor of galactose oxidase: An unusual self-processing enzyme
S.J. Firbank,M. Rogers,M. Rogers,Carrie M. Wilmot,David M. Dooley,Malcolm A. Halcrow,Peter F. Knowles,Michael J. McPherson,Simon E. V. Phillips +8 more
TL;DR: Structural alignment of the precursor and mature forms of galactose oxidase shows that five regions of main chain and some key residues of the active site differ significantly between the two forms.
Amperometric Biosensor Based on Galactose Oxidase Immobilized in Clay Matrix
TL;DR: In this paper, an amperometric galactose biosensor was developed by immobilizing GAOx within a laponite clay film coated on a Pt electrode surface, and the electrochemical assays were performed by potentiostating the GAOx/laponite bioelectrodes at + 0.6
Sensitive chemiluminescent imaging for chemoselective analysis of glycan expression on living cells using a multifunctional nanoprobe.
TL;DR: This novel sensitive chemiluminescent imaging method could be used for distinguishing cancer cells from normal cells and monitoring of dynamic carbohydrate expression on living cells, providing promising application in clinical diagnosis and treatment of cancer.