Bj. Berger et al., AROMATIC AMINO-ACID TRANSAMINATION AND METHIONINE RECYCLING IN TRYPANOSOMATIDS, Proceedings of the National Academy of Sciences of the United Statesof America, 93(9), 1996, pp. 4126-4130
Although trypanosomatids are known to rapidly transaminate exogenous a
romatic amino acids ill vitro and in vivo, the physiological significa
nce of this reaction is not understood. In postmitochondrial supernata
nts prepared from Trypanosoma brucei brucei and Crithidia fasciculata,
we have found that aromatic amino acids were the preferred amino dono
rs for the transamination of alpha-ketomethiobutyrate to methionine. I
ntact C. fasciculata groan in the presence of [N-15]tyrosine were foun
d to contain detectable [N-15]methionine, demonstrating that this reac
tion occurs in situ in viable cells. This process is the final step in
the recycling of methionine from methylthioadenosine, a product of de
carboxylated S-adenosylmethionine from the polyamine synthetic pathway
. Mammalian liver, in contrast, preferentially used glutamine for this
reaction and utilized a narrower range of amino donors than seen with
the trypanosomalids. Studies with methylthioadenosine showed that thi
s compound was readily converted to methionine, demonstrating a fully
functional methionine-recycling pathway in trypanosomatids.