Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1973 Nov;135(3):563–565. doi: 10.1042/bj1350563

Inhibition of 3-phosphoglycerate dehydrogenase from Pisum sativum by purine nucleotides (Short Communication)

J Colin Slaughter 1
PMCID: PMC1165863  PMID: 4772281

Abstract

The inhibition of 3-phosphoglycerate dehydrogenase from etiolated pea epicotyls by purine nucleoside di- and tri-phosphates is linear, competitive with regard to NADH, and the nucleotides are mutually exclusive in their binding. Free ATP and ADP are more effective inhibitors than are the respective magnesium complexes.

Full text

PDF
563

Selected References

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

  1. Purich D. L., Fromm H. J. Studies on factors influencing enzyme responses to adenylate energy charge. J Biol Chem. 1972 Jan 10;247(1):249–255. [PubMed] [Google Scholar]
  2. Slaughter J. C., Davies D. D. Inhibition of 3-phosphoglycerate dehydrogenase by l-serine. Biochem J. 1968 Oct;109(5):749–755. doi: 10.1042/bj1090749. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Slaughter J. C., Davies D. D. The isolation and characterization of 3-phosphoglycerate dehydrogenase from peas. Biochem J. 1968 Oct;109(5):743–748. doi: 10.1042/bj1090743. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES