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Diversified amino acid-mediated allosteric regulation of phosphoglycerate dehydrogenase for serine biosynthesis in land plants.

Okamura, E., et al. · 2021 · Biochemical Journal   research

doi:10.1042/bcj20210191   PMID:34032263   PMC8238522

Linked genes (1)  1 core 0 peripheral

Gene ID Name Evidence / Role Function (this paper)
Mp8g16970 MpPGDH missing experimental subject Single-copy Marchantia phosphoglycerate dehydrogenase functionally characterized as recombinant protein; forms a homotetramer in vitro and shows allosteric regulation, inhibited by L-serine and activated by L-alanine, L-valine, L-methionine, L-homoserine, and L-homocysteine (lowest EC50). Represents a conserved amino acid-sensitive ancestral PGDH form, with no amino acid-insensitive isozyme in M. polymorpha.