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Journal Article

A biosynthetic pathway to isovaleryl-CoA in myxobacteria: the involvement of the mevalonate pathway

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Mahmud, T., Wenzel, S. C., Wan, E., Wen, K. W., Bode, H. B., Gaitatzis, N., et al. (2004). A biosynthetic pathway to isovaleryl-CoA in myxobacteria: the involvement of the mevalonate pathway. Chembiochem, 6(2), 322-30. doi:10.1002/cbic.200400261.

Cite as: https://hdl.handle.net/21.11116/0000-000A-0958-A
A biosynthetic shunt pathway branching from the mevalonate pathway and providing starter units for branched-chain fatty acid and secondary metabolite biosynthesis has been identified in strains of the myxobacterium Stigmatella aurantiaca. This pathway is upregulated when the branched-chain alpha-keto acid dehydrogenase gene (bkd) is inactivated, thus impairing the normal branched-chain amino acid degradation process. We previously proposed that, in this pathway, isovaleryl-CoA is derived from 3,3-dimethylacrylyl-CoA (DMA-CoA). Here we show that DMA-CoA is an isomerization product of 3-methylbut-3-enoyl-CoA (3MB-CoA). This compound is directly derived from 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) by a decarboxylation/ dehydration reaction resembling the conversion of mevalonate 5-diphosphate to isopentenyl diphosphate. Incubation of cell-free extracts of a bkd mutant with HMG-CoA gave product(s) with the molecular mass of 3MB-CoA or DMA-CoA. The shunt pathway most likely also operates reversibly and provides an alternative source for the monomers of isoprenoid biosynthesis in myxobacteria that utilize L-leucine as precursor.