Stereochemistry and accessibility of prosthetic groups in flavoproteins (original) (raw)

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. is a flavin analogue whose specific features make it well suited for probing stereospecificities of flavin coenzymes in enzymic reactions. Its shape and charge usually do not interfere with binding at active sites of enzymes; it can be transformed to the FMN and FAD levels, respectively, by the well-characterized riboflavin kinase/FAD synthetase from Brevibacterium ammoniagenes

Sign up for access to the world's latest research.

checkGet notified about relevant papers

checkSave papers to use in your research

checkJoin the discussion with peers

checkTrack your impact