Structural analysis of a stereochemical modification of flavin adenine dinucleotide in alcohol oxidase from methylotrophic yeasts
作者： Richard M Kellogg , Wim Kruizinga , Leonid V Bystrykh , Lubbert Dijkhuizen , Wim Harder
DOI: 10.1016/S0040-4020(01)92193-3
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摘要: Abstract Alcohol oxidase (MOX), a major peroxisomal protein of methanol-utilizing yeasts, contains two different forms flavin adenine dinucleotide, one which is identical with natural FAD whereas the other (mFAD) stereochemical modification coenzyme. This modifictaion occurs spontaneously (but not FADH) bound to alcohol oxidase. mFAD was degraded diphosphatase provide authentic AMP and mFMN. The latter further phosphtase m-riboflavin. Analysis by 1H 13C NMR spectroscopy revealed that isoalloxazide rings were intact modified structurally. However, significant differences observed in proton spectra sugar chains attached isoalloxazine ring (ribitol case FAD). Similar observations made for mFMN Most striking COSY virtual absence coupling between protons 2′ 3′ chain ring, this strong materials. nature 1a′ 1b′ material. All these are consistent hypothesis cofactor absolute configuration carbon has changed from R S. indicates presence an arabityl rather than ribitol present FAD. A possible mechanism conversion suggested.
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