l-Threonine is catabolized by Trypanosoma brucei to give equimolar quantities of glycine and acetate. The pathway, which involves the two enzymes l-threonine dehydrogenase (EC 1.1.1.103) and aminoacetone synthase (acetyl-CoA: glycine C-acetyltransferase, EC 2.3.1.29) and subsequent hydrolysis of the acetyl-CoA, is most active in cultured trypanosomes but is also present in bloodstream forms. l-Threonine dehydrogenase from both culture and bloodstream forms of trypanosomes has an apparent molecular weight of between 28000 and 38000, and is sensitive to a wide range of sulphydryl reagents.
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