C. Shiau, Yu-Tien Liu
Apr 12, 2002
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Influential Citations
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Journal
Biochemical and Biophysical Research Communications
Abstract
Abstract l -δ-(α-Aminoadipoyl)- l -cysteine- d -valine synthetase (ACVS) has been recently studied as a model enzyme for peptide synthetases. It was found that in the absence of α-aminoadipic acid but in the presence of several cysteine analogues it was incorporated into several analogue dipeptides upon incubation of the potential cysteine analogues with ACVS. [14C]Cysteine was incorporated into the[14C]cysteinyl-valine analogue dipeptides. Notably, [14C]valine incorporation in the presence of N-acylated cysteine analogues was observed. The α-aminoadipic acid activation site is influential, inhibitory or promotive, on the production of these putative dipeptide products. The production of dipeptide analogues, containing valine or analogues at the C-terminus, leads to the speculation that the biosynthetic direction of ACV could be from the C-terminus to the N-terminus.