By Rene A. Frenkel
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Extra info for Carnitine Biosynthesis, Metabolism, and Functions
Characterization of this + enzymatic activity showed that it requires F e 2 , a-ketoglutarate and ascorbate, thus this enzyme is similar to the dioxygenase that forms carnitine from TMAB (5) . The meta bolite of the mitochondrial incubations was shown to be 3hydroxy-6-N-trimethyllysine (HTML) by its behavior and that + of its periodate oxidation product on Dowex 50-H and Chelex + 100-Cu^ columns and migration during high voltage paper electrophoresis. The HTML so obtained was also shown to be an effective precursor of carnitine by its conversion to TMAB and carnitine by a crude rat liver homogenate.
7) identified hydroxytrimethy 1 lysine as a metabolite of trimethyllysine found in the urine of rats and suggested that it was an intermediate as shown. Attempts to isolate a system capable of hydroxylating trimethyllysine led to the discovery that mitochondria from both rat liver and kidney possess this capacity (8). Characterization of this + enzymatic activity showed that it requires F e 2 , a-ketoglutarate and ascorbate, thus this enzyme is similar to the dioxygenase that forms carnitine from TMAB (5) .
3) A n u m b e r of s c a v e n g e r s f o r the s u p e r o x i d e a n i o n h a v e been t e s t e d . T e t r a n i t r o m e t h a n e a n d nitro blue t e t r a z o l i u m w e r e i n h i b i t o r y , but these c o m p o u n d s a l s o r e d u c e d the a c t i v i t y if p r e i n c u b a t e d w i t h the e n z y m e in the c o l d . e. in a s i t u a t i o n when a u t o o x i d a t i o n m a y t a k e p l a c e . S i n c e a d r e n o c h r o m e s e e m s to d a m a g e the e n z y m e p r o t e i n the r e s u l t s are d i f f i c u l t to i n t e r p r e t e .