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Journal Article

Stereochemistry and accessibility of prosthetic groups in flavoproteins


Manstein,  Dietmar J.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Manstein, D. J., Massey, V., Ghisla, S., & Pai, E. F. (1988). Stereochemistry and accessibility of prosthetic groups in flavoproteins. Biochemistry, 27(7), 2300-2305. doi:10.1021/bi00407a009.

Cite as: https://hdl.handle.net/21.11116/0000-000A-7B4A-A
Using 8-demethyl-8-hydroxy-5-deaza-5-carba analogues 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.