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Literature summary extracted from

  • Schuller, D.J.; Grant, G.A.; Banaszak, L.J.
    The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase (1995), Nat. Struct. Biol., 2, 69-76.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.95
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.95 44000
-
 4 * 44000, SDS-PAGE, each subunit is divided into 3 separate domains Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.95 3-phosphoglycerate + NAD+ Escherichia coli first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate 3-phosphohydroxypyruvate + NADH
-
 r

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.95
-
 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
1.1.1.95 3-phosphoglycerate + NAD+ first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate Escherichia coli 3-phosphohydroxypyruvate + NADH
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.95 tetramer 4 * 44000, SDS-PAGE, each subunit is divided into 3 separate domains Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.95 NAD+
-
 Escherichia coli
1.1.1.95 NADH
-
 Escherichia coli