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Literature summary for 1.2.1.12 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
Search for more literature for 1.2.1.12

General Stability

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

Inhibitors

Inhibitors Comment Organism Structure
iodoacetate
-
 Homo sapiens

KM Value [mM]

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

Localization

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
 Homo sapiens
-

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

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