An investigation of the role of the copper in galactose oxidase.
Galactose oxidase is a metalloenzyme containing a single copper atom per molecule. The mechanism of action of galactose oxidase is studied in this paper by investigating substrate specificity and activation by peroxidase, and probing the copper site by electron spin resonance (ESR) spectroscopy. Line-shape simulation of ESR spectra are also reported and a comparison is made between observed and simulated spectra for galactose oxidase. A comparison is also reported for the enzyme from various commercial sources and enzyme isolated from a fungus in this laboratory. The results of this investigation suggest that the copper is in an environment of four in-plane nitrogens with axial symmetry.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D001487:Basidiomycota / Q000201:enzymology*; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D003201:Computers; D003300:Copper / Q000378:metabolism*; D004187:Disaccharides / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D004789:Enzyme Activation; D005692:Galactose Oxidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008433:Mathematics; D008667:Metalloproteins / Q000378:metabolism; D010544:Peroxidases / Q000494:pharmacology; D011124:Polyporaceae / Q000201:enzymology*; D013329:Structure-Activity Relationship
D004187:Disaccharides; D008667:Metalloproteins; D003300:Copper; D000429:Alcohol Oxidoreductases; D005692:Galactose Oxidase; D010544:Peroxidases