Threonine Catabolism in Trypanosoma brucei
Linstead, D. J. and Klein, R. A. and Cross, G. A. M.,, 101, 243-251 (1977),
doi = https://doi.org/10.1099/00221287-101-2-243,
publicationName = Microbiology Society,
issn = 1350-0872,
abstract= 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.,
language=,
type=