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- W2021986906 abstract "L-delta-(alpha-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 alpha-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. [(14)C]Cysteine was incorporated into the[(14)C]cysteinyl-valine analogue dipeptides. Notably, [(14)C]valine incorporation in the presence of N-acylated cysteine analogues was observed. The alpha-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." @default.
- W2021986906 created "2016-06-24" @default.
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- W2021986906 date "2002-04-01" @default.
- W2021986906 modified "2023-09-26" @default.
- W2021986906 title "l-δ-(α-Aminoadipoyl)-l-cysteine-d-valine Synthetase: Production of Dipeptides Containing Valine Residue at Its C-Terminus" @default.
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- W2021986906 doi "https://doi.org/10.1006/bbrc.2002.6728" @default.
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