Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.95 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
Search for more literature for 1.1.1.95

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Escherichia coli

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Reaction

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

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli
NADH
-
 Escherichia coli