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Literature summary extracted from

  • Eby, D.; Kirtley, M.E.
    Isolation and characterization of glyceraldehyde-3-phosphate dehydrogenase from human erythrocyte membranes (1979), Arch. Biochem. Biophys., 198, 608-613.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.2.1.12 binding to erythrocyte membranes stabilizes the enzyme at 4°C Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.12 iodoacetate
-
Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.12 additional information
-
additional information
-
Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.1.12 membrane isolated from human erytrocyt ghosts Homo sapiens 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.12 36000
-
4 * 36000, SDS-PAGE Homo sapiens
1.2.1.12 144000
-
gel filtration Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.12 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.12
-
Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.12 erythrocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.12 D-glyceraldehyde 3-phosphate + arsenate + NAD+
-
Homo sapiens 3-phospho-D-glyceroyl arsenate + NADH
-
?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Homo sapiens 3-phospho-D-glyceroyl phosphate + NADH
-
?

Subunits

EC Number Subunits Comment Organism
1.2.1.12 tetramer 4 * 36000, SDS-PAGE Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.12 NAD+ contains 3.0-3.5 M of NAD+ bound per mol of tetramer Homo sapiens