MarpolBase - Identification and Biochemical Characterization of the Serine Biosynthetic Enzyme 3-Phosphoglycerate Dehydrogenase in Marchantia polymorpha.

Identification and Biochemical Characterization of the Serine Biosynthetic Enzyme 3-Phosphoglycerate Dehydrogenase in Marchantia polymorpha.

Akashi, H., et al. · 2018 · Frontiers in Plant Science research

Gene ID	Name	Evidence / Role	Function (this paper)
Mp8g16970	MpPGDH missing	experimental subject	Marchantia 3-phosphoglycerate dehydrogenase; cDNA cloned and expressed in serine-auxotrophic E. coli, restoring growth without Ser to confirm function. Biochemically characterized: forms a homotetramer, optimal pH 9.0, Km/Vmax determined, stabilized by phosphate, inhibited cooperatively by L-serine (to 40%) and activated by several amino acids. Acts as the committed serine-biosynthesis enzyme studied here.
Mp1g15430	MpPSAT missing	sequence background	Phosphoserine aminotransferase identified as a single-copy gene by BLAST, deduced protein 67% identical to AtPSAT1; not functionally or biochemically tested.
Mp2g10500	MpPSP missing	sequence background	Phosphoserine phosphatase identified as a single-copy gene by BLAST, deduced protein 57% identical to AtPSP; not functionally or biochemically tested.