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Literature summary for 1.1.1.95 extracted from

  • Grant, G.A.; Hu, Z.; Xu, X.L.
    Amino acid residue mutations uncouple cooperative effects in Escherichia coli D-3-phosphoglycerate dehydrogenase (2001), J. Biol. Chem., 276, 17844-17850.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
diverse mutants expressed in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information diverse mutants with different interaction between the 3 binding domains of each of 4 subunits and modified kinetics Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
L-serine sigmoidal binding curve with mutant G294V/G336V, mutants with decreased sensitivity to serine Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
diverse mutants expressed in Escherichia coli Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
3-phospho-D-glycerate + NAD+ = 3-phosphooxypyruvate + NADH + H+ model for catalytic mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-phosphoglycerate + NAD+
-
Escherichia coli 3-phosphohydroxypyruvate + NADH
-
r

Subunits

Subunits Comment Organism
More subunit structure with substrate binding domain, coenzyme binding domain and regulatory domain, active sites Escherichia coli