Carnitine Biosynthesis /3-HYDROXYLATION OF TRIMETHYLLYSINE BY AN a-KETOGLUTARATE-DEPENDENT MITOCHONDRIAL DIOXYGENASE*

نویسندگان

  • JAMES D. HULSE
  • STEVEN R. ELLIS
  • M. HENDERSON
چکیده

Rat liver mitochondria were found to hydroxylate E-Ntrimethyl+lysine to produce P-hydroxy-c-N-trimethyl-L-lysine, an intermediate in carnitine biosynthesis. The hydroxylating system requires a-ketoglutarate, Fez+, and ascorbate, but does not require NADPH nor NADH. No activity was found in the microsomal or soluble fractions of liver extracts. The hydroxylated a-amino acid was isolated and characterized by column chromatography using Dowex 50H+ and Chelex 100~CW+ resins and by high voltage paper electrophoresis. The enzymatically produced P-hydroxy-eN-trimethyl+lysine was shown to be periodate-sensitive and one periodation product was characterized as y-butyrobetaine aldehyde. The hydroxylated product was acted upon by crystalline serine transhydroxymethylase (EC 2.1.2.1) to yield y-butyrobetaine aldehyde and glycine. Conversion of about 40% of the l -N-trimethyl+lysine to phydroxy-•-N-trimethyl+lysine was accomplished by this system with little or no further metabolism.

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تاریخ انتشار 2002