Novel Regulatory Mechanism of Serine Biosynthesis Associated with 3-phosphoglycerate Dehydrogenase in Arabidopsis Thaliana

Overview

Journal Sci Rep

Specialty Science

Date 2017 Jun 16

PMID 28615699

Citations 21

Authors

Eiji Okamura

Masami Yokota Hirai

Affiliations

Soon will be listed here.

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.

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