Abstract
The final step in the biosynthesis of l-carnitine in humans is catalysed by the 2-oxoglutarate and ferrous iron dependent oxygenase, γ-butyrobetaine hydroxylase (BBOX). 1H and 19F NMR studies inform on the BBOX mechanism including by providing evidence for cooperativity between monomers in substrate/some inhibitor binding. The value of the 19F NMR methods is demonstrated by their use in the design of new BBOX inhibitors.
Highlights
The final step in the biosynthesis of L-carnitine in humans is catalysed by the 2-oxoglutarate and ferrous iron dependent oxygenase, c-butyrobetaine hydroxylase (BBOX). 1H and 19F NMR studies inform on the BBOX mechanism including by providing evidence for cooperativity between monomers in substrate/some inhibitor binding
Carnitine plays a crucial role in lipid metabolism by enabling long-chain fatty acid transport into mitochondria for b-oxidation.[3,4]
Definitive evidence for its effects, and the biological modes of action of Mildronate, are lacking; it is proposed to cause a change in metabolism from mitochondrial fatty acid b-oxidation towards peroxisomal metabolism and glycolysis, via reduction of carnitine levels, due to inhibition of BBOX and of carnitine uptake.[9]
Summary
The final step in the biosynthesis of L-carnitine in humans is catalysed by the 2-oxoglutarate and ferrous iron dependent oxygenase, c-butyrobetaine hydroxylase (BBOX). 1H and 19F NMR studies inform on the BBOX mechanism including by providing evidence for cooperativity between monomers in substrate/some inhibitor binding. 1H and 19F NMR studies inform on the BBOX mechanism including by providing evidence for cooperativity between monomers in substrate/some inhibitor binding.
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