f Threonine Catabolism in Trypanosoma brucei
- Authors: D. J. LINSTEAD*, R. A. KLEIN, G. A. M. CROSS
- First Published Online: 01 August 1977, Microbiology 101: 243-251, doi: 10.1099/00221287-101-2-243
- Subject: Biochemistry
- Issue Published:
Summary: 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 18.104.22.168) and aminoacetone synthase (acetyl-CoA: glycine C-acetyltransferase, EC 22.214.171.124) 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.
Present address: Wellcome Research Laboratories, Langley Court, Beckenham, Kent BR3 3BS.
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