Henderson, LaVell M. published the artcileMammalian enzymes of trimethyllysine conversion to trimethylaminobutyrate, Application In Synthesis of 6249-56-5, the publication is Federation Proceedings (1982), 41(12), 2843-7, database is CAplus and MEDLINE.
The biosynthesis of carnitine proceeds from trimethyllysine (TML) by β-hydroxylation by liver or kidney mitochondrial TML-α-ketoglutarate dioxygenase (referred to as TML hydroxylase) which requires O2, α-ketoglutarate, Fe2+, and ascorbate. TML hydroxylase is rapidly inactivated by preincubation with Fe2+, but not Fe3+, suggesting that superoxide is involved in the hydroxylation. β-Hydroxyltrimethyllysine undergoes aldol cleavage to glycine and trimethylaminobutyraldehyde under the influence of serum hydroxymethyltransferase and possibly a specific aldolase. The next step, the aldehyde oxidation, is catalyzed by a specific NAD-dependent aldehyde dehydrogenase from liver cytosol. The product, trimethylaminobutyrate, is then hydroxylated by a cytosolic dioxygenase to carnitine. This enzyme, which has the same cofactor requirements as TML hydroxylase, is found in the liver of all species examined, but is absent from the kidney of some species.
Federation Proceedings published new progress about 6249-56-5. 6249-56-5 belongs to chlorides-buliding-blocks, auxiliary class Phase Transfer Catalyst,Inhibitor,Natural product, name is 3-Carboxy-N,N,N-trimethylpropan-1-aminium chloride, and the molecular formula is C7H16ClNO2, Application In Synthesis of 6249-56-5.
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