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. 1968 Oct;109(5):749–755. doi: 10.1042/bj1090749

Inhibition of 3-phosphoglycerate dehydrogenase by l-serine

J C Slaughter 1,*, D D Davies 1
PMCID: PMC1187025  PMID: 5696864

Abstract

1. l-Serine was shown to be a highly specific inhibitor of 3-phosphoglycerate dehydrogenase. 2. 3-Phosphoglycerate dehydrogenase is cold-labile with respect to its catalytic activity and to sensitivity to serine. 3. l-Serine protects the catalytic site as well as the inhibitor site. 4. Glycerol protects the catalytic site as well as the inhibitor site. 5. Serine acts as a `classical' non-competitive inhibitor of fresh preparations of 3-phosphoglycerate dehydrogenase. 6. `Aged' preparations when assayed at pH6·5 show sigmoid inhibition curves at saturating substrate concentrations. 7. A generalized model is advanced to account for the variation of the catalytic activity and the inhibitory effect of l-serine with time and conditions. 8. The possibility that the sigmoid kinetics of inhibition observed are an artifact of isolation is discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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