Carnitine biosynthesis. Purification of gamma-butyrobetaine hydroxylase from rat liver.

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Vaz FM, van Gool S, Ofman R, IJlst L, Wanders RJ

Carnitine biosynthesis. Purification of gamma-butyrobetaine hydroxylase from rat liver.

Adv Exp Med Biol. 1999;466:117-24.

PubMed ID
10709635 [ View in PubMed
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Abstract

gamma-Butyrobetaine hydroxylase catalyse the last step in carnitine biosynthesis, the formation of L-carnitine from gamma-butyrobetaine, a reaction dependent on Fe2+, alpha-ketoglutarate, ascorbate and oxygen. Initial attempts to purify the protein from rat liver showed that gamma-butyrobetaine hydroxylase is unstable. We, therefore, determined the influence of various compounds on the stability of gamma-butyrobetaine hydroxylase at different storage temperatures. The enzyme activity was best conserved by storing the protein at 4 degrees C in the presence of 200 g/l glycerol and 10 mM DTT. We subsequently purified the enzyme from rat liver to apparent homogeneity by liquid chromatography.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
Ascorbic acidGamma-butyrobetaine dioxygenaseProteinHumans
Unknown
Cofactor
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