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Literature summary for 1.1.1.95 extracted from

  • Grant, G.A.; Schuller, D.J.; Banaszak, L.J.
    A model for the regulation of D-3-phosphoglycerate dehydrogenase, a Vmax-type allosteric enzyme (1996), Protein Sci., 5, 34-41.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
amino acids
-
Escherichia coli
L-serine allosteric inhibition, regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364 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 allosteric inhibition by L-serine, L-serine regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364, 1 serine binds per subunit 3-phosphohydroxypyruvate + NADH
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
3-phospho-D-glycerate + NAD+ = 3-phosphooxypyruvate + NADH + H+ regulation model with effector L-serine, member of the D-2-hydroxyacid dehydrogenases, D-isomer substrate specific, overview of related enzymes from other species Escherichia coli

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+ allosteric inhibition by L-serine, L-serine regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364, 1 serine binds per subunit 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
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