Absolute stereochemistry of flavins in enzyme-catalyzed reactions

Manstein, Dietmar J.; Pai, Emil F.; Schopfer, Lawrence M.; Massey, Vincent

doi:10.1021/bi00370a012

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Absolute stereochemistry of flavins in enzyme-catalyzed reactions

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

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Pai, Emil F.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Manstein, D. J., Pai, E. F., Schopfer, L. M., & Massey, V. (1986). Absolute stereochemistry of flavins in enzyme-catalyzed reactions. Biochemistry, 25(22), 6807-6816. doi:10.1021/bi00370a012.

Cite as: https://hdl.handle.net/21.11116/0000-0006-9946-F

Abstract

The 8-demethyl-8-hydroxy-5-deaza-5-carba analogues of FMN and FAD have been synthesized. Several apoproteins of flavoenzymes were successfully reconstituted with these analogues. This and further tests established that these analogues could serve as general probes for flavin stereospecificity in enzyme-catalyzed reactions. The method used by us involved stereoselective introduction of label on one enzyme combined with transfer to and analysis on a second enzyme. Using as a reference glutathione reductase from human erythrocytes for which the absolute stereochemistry of catalysis is known from X-ray studies [Pai, E. F., & Schulz, G. E. (1983) J. Biol. Chem. 258, 1752-1758], we were able to determine the absolute stereospecificities of other flavoenzymes. We found that glutathione reductase (NADPH), general acyl-CoA dehydrogenase (acyl-CoA), mercuric reductase (NADPH), thioredoxin reductase (NADPH), p-hydroxybenzoate hydroxylase (NADPH), melilotate hydroxylase (NADH), anthranilate hydroxylase (NADPH), and glucose oxidase (glucose) all use the re face of the flavin ring when interacting with the substrates given in parentheses.