Submitochondrial localization of 6-N-trimethyllysine dioxygenase - implications for carnitine biosynthesis.

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van Vlies N, Ofman R, Wanders RJ, Vaz FM

Submitochondrial localization of 6-N-trimethyllysine dioxygenase - implications for carnitine biosynthesis.

FEBS J. 2007 Nov;274(22):5845-51. doi: 10.1111/j.1742-4658.2007.06108.x. Epub 2007 Oct 18.

PubMed ID

17944936 [ View in PubMed

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Abstract

The first enzyme of carnitine biosynthesis is the mitochondrial 6-N-trimethyllysine dioxygenase, which converts 6-N-trimethyllysine to 3-hydroxy-6-N-trimethyllysine. Using progressive membrane solubilization with digitonin and protease protection experiments, we show that this enzyme is localized in the mitochondrial matrix. Latency experiments with intact mitochondria showed that 3-hydroxy-6-N-trimethyllysine formation is limited by 6-N-trimethyllysine transport across the mitochondrial inner membrane. Because the subsequent carnitine biosynthesis enzymes are cytosolic, after production, 3-hydroxy-6-N-trimethyllysine must be transported out of the mitochondria by a putative mitochondrial 6-N-trimethyllysine/3-hydroxy-6-N-trimethyllysine transporter system. This transport system represents an additional step in carnitine biosynthesis that could have considerable implications for the regulation of carnitine biosynthesis.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Ascorbic acid	Trimethyllysine dioxygenase, mitochondrial	Protein	Humans	Unknown	Cofactor	Details