Characterization of Saccharomyces cerevisiae acyl-protein thioesterase 1, the enzyme responsible for G protein alpha subunit deacylation in vivo.

@article{Duncan2002CharacterizationOS,
  title={Characterization of Saccharomyces cerevisiae acyl-protein thioesterase 1, the enzyme responsible for G protein alpha subunit deacylation in vivo.},
  author={Joseph A Duncan and Alfred G. Gilman},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 35},
  pages={31740-52}
}
Thioacylation is a reversible lipid modification of proteins that plays a role in the regulation of signal transduction. Acyl-protein thioesterase 1 (APT1) was identified as an enzyme capable of deacylating some thioacylated proteins in vitro. Saccharomyces cerevisiae open reading frame YLR118c encodes an enzyme homologous to Rattus norvegicus APT1. We demonstrate that the catalytic activity of the protein encoded by the yeast open reading frame is similar to that of rat APT1, and we designate… CONTINUE READING

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