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Literature summary for 1.1.1.95 extracted from

  • Yoshida, K.; Ohtaka, K.; Hirai, M.Y.; Hisabori, T.
    Biochemical insight into redox regulation of plastidial 3-phosphoglycerate dehydrogenase from Arabidopsis thaliana (2020), J. Biol. Chem., 295, 14906-14915 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rosetta (DE3) pLysS competent cells Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Arabidopsis thaliana 9507
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-phospho-D-glycerate + NAD+ Arabidopsis thaliana
-
3-phosphooxypyruvate + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana O04130
-
-
Arabidopsis thaliana O49485
-
-
Arabidopsis thaliana Q9LT69
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-phospho-D-glycerate + NAD+
-
Arabidopsis thaliana 3-phosphooxypyruvate + NADH + H+
-
r

Synonyms

Synonyms Comment Organism
3-phosphoglycerate dehydrogenase
-
Arabidopsis thaliana
At1g17745
-
Arabidopsis thaliana
At3g19480
-
Arabidopsis thaliana
At4g34200
-
Arabidopsis thaliana
PGDH1
-
Arabidopsis thaliana
PGDH2
-
Arabidopsis thaliana
PGDH3
-
Arabidopsis thaliana

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the first committed step of Ser biosynthetic pathway in plastids. Activity of PGDH2 is not enhanced upon reduction by thioredoxin Arabidopsis thaliana
metabolism the enzyme catalyzes the first committed step of Ser biosynthetic pathway in plastids. Activity of PGDH3 is not enhanced upon reduction by thioredoxin Arabidopsis thaliana
metabolism the enzyme catalyzes the first committed step of Ser biosynthetic pathway in plastids. Isoform PGDH1 forms the intramolecular disulfide bond between Cys86 and Cys102, lowering PGDH enzyme activity. It is activated by cleavage of intramolecular disulfide bond. Some thioredoxin subtypes in plastids support PGDH1 reductive activation. PGDH1 is a redox-sensitive protein whose activity is enhanced upon reduction Arabidopsis thaliana