Publikation: Stereochemistry and accessibility of prosthetic groups in flavoproteins
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Using 8-demethyl-8-hydroxy-5-deaza-5-carabnaa logues of the appropriate flavin nucleotides, we determined the stereochemistry of interaction between coenzyme and substrate for several flavoproteins. The enzymes were D-amino acid oxidase, L-lactate oxidase, and D-lactate dehydrogenase, all three of which interact with pyruvate, as well as cyclohexanone monooxygenase and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase, which were both probed with nicotinamide nucleotides. L-Lactate oxidase and D-lactate dehydrogenase used the si face of the modified flavin ring while the other three enzymes showed re-side specificity. This selection of flavoenzymes includes FAD- and FMN-dependent enzymes, enzymes that follow a carbanion mechanism, and others that have hydride transfer as an integral part of their reaction pathway.
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MANSTEIN, Dietmar J., Vincent MASSEY, Sandro GHISLA, Emil F. PAI, 1988. Stereochemistry and accessibility of prosthetic groups in flavoproteins. In: Biochemistry. 1988, 27(7), pp. 2300-2305. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi00407a009BibTex
@article{Manstein1988Stere-8773, year={1988}, doi={10.1021/bi00407a009}, title={Stereochemistry and accessibility of prosthetic groups in flavoproteins}, number={7}, volume={27}, issn={0006-2960}, journal={Biochemistry}, pages={2300--2305}, author={Manstein, Dietmar J. and Massey, Vincent and Ghisla, Sandro and Pai, Emil F.} }
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