Spermidine biosynthesis in Saccharomyces cerevisiae. Biosynthesis and processing of a proenzyme form of S-adenosylmethionine decarboxylase.

@article{Kashiwagi1990SpermidineBI,
  title={Spermidine biosynthesis in Saccharomyces cerevisiae. Biosynthesis and processing of a proenzyme form of S-adenosylmethionine decarboxylase.},
  author={Kiyoko Kashiwagi and Satish Kumar Taneja and Tina Y Liu and Celia White Tabor and Herbert Tabor},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 36},
  pages={
          22321-8
        }
}
We have cloned and sequenced the Saccharomyces cerevisiae gene for S-adenosylmethionine decarboxylase. This enzyme contains covalently bound pyruvate which is essential for enzymatic activity. We have shown that this enzyme is synthesized as a Mr 46,000 proenzyme which is then cleaved post-translationally to form two polypeptide chains: a beta subunit (Mr 10,000) from the amino-terminal portion and an alpha subunit (Mr 36,000) from the carboxyl-terminal portion. The protein was overexpressed in… CONTINUE READING
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