Properties of Choline Oxidase of Cylindrocarpon didymum M-1 |
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Authors: | Hideaki Yamada Nobuhiro Mori Yoshiki Tani |
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Institution: | Department of Agricultural Chemistry, Kyoto University, Kyoto |
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Abstract: | Choline oxidase from the cell-free extract of Cylindrocarpon didymum M-1 showed a molecular weight of 120,000 by the gel filtration method and 145,000 by the sedimentation velocity method. The enzyme exhibited an absorption spectrum characteristic of a flavoprotein with absorption maxima at 276, 370 and 454 nm and a shoulder at 470 nm. Anaerobic addition of choline as well as sodium dithionite to the enzyme produced a disappearance of the peak at 454 nm.Choline oxidase consists of two identical subunits, which have a molecular weight of 64,000, and contains two mol of FAD per mol of enzyme. The flavin was shown to be covalently bound to the protein.The enzyme was inactivated by Ag+, Hg2+, Cu2+ and Zn2+. The enzyme oxidized choline, betaine aldehyde and N, N-dimethylaminoethanol and apparent Km values were 1.3 mm, 5.8 mm and 14 mm, respectively. |
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