RRC ID 54945
Author Okamura E, Hirai MY.
Title Novel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in Arabidopsis thaliana.
Journal Sci Rep
Abstract The proteinogenic amino acid L-serine is a precursor for various essential biomolecules in all organisms. 3-Phosphoglycerate dehydrogenase (PGDH) is the first committed enzyme of the phosphorylated pathway of L-serine biosynthesis, and is regulated by negative feedback from L-serine in bacteria and plants. In the present study, two Arabidopsis PGDH isoforms were inhibited by L-serine but were activated by L-amino acids such as L-homocysteine in vitro. Activation and inhibition by these amino acids was cooperative, suggesting an allosteric mechanism. Moreover, the half maximal effective concentration of L-homocysteine was 2 orders of magnitude lower than that of L-serine, suggesting greater regulatory potency. These are the first data to show that PGDH is activated by various biomolecules and indicate that serine biosynthesis is regulated by multiple pathways.
Volume 7(1)
Pages 3533
Published 2017-6-14
DOI 10.1038/s41598-017-03807-5
PII 10.1038/s41598-017-03807-5
PMID 28615699
PMC PMC5471267
MeSH Allosteric Regulation Arabidopsis / enzymology* Arabidopsis / metabolism* Arabidopsis Proteins / metabolism* Enzyme Activators / metabolism Enzyme Inhibitors / metabolism Gene Expression Regulation, Enzymologic* Gene Expression Regulation, Plant* Phosphoglycerate Dehydrogenase / metabolism* Serine / biosynthesis*
IF 4.011
Times Cited 10
Arabidopsis / Cultured plant cells, genes pda02295 pda04481