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Literature summary 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)

EC Number Cloned (Comment) Organism
1.1.1.95 diverse mutants expressed in Escherichia coli Escherichia coli

Protein Variants

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

Inhibitors

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.95 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.95 diverse mutants expressed in Escherichia coli Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.95 3-phospho-D-glycerate + NAD+ = 3-phosphooxypyruvate + NADH + H+ model for catalytic mechanism Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.95 3-phosphoglycerate + NAD+
-
 Escherichia coli 3-phosphohydroxypyruvate + NADH
-
 r

Subunits

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