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Literature summary for 1.2.1.12 extracted from

  • Speranza, M.L.; Gozzer, C.
    Purification and properties of NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from spinach leaves (1978), Biochim. Biophys. Acta, 522, 32-42.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.25
-
NAD+
-
Spinacia oleracea
0.4
-
D-glyceraldehyde 3-phosphate
-
Spinacia oleracea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
Cys content is higher than that found in analogous enzymes Spinacia oleracea
14000
-
x * 14000 + x * 37000, SDS-PAGE Spinacia oleracea
37000
-
x * 14000 + x * 37000, SDS-PAGE Spinacia oleracea
150000
-
-
Spinacia oleracea

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Spinacia oleracea

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Spinacia oleracea
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Spinacia oleracea

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 14000 + x * 37000, SDS-PAGE Spinacia oleracea

Cofactor

Cofactor Comment Organism Structure
NAD+ contains about 1.8 mol NAD+ per mol of enzyme Spinacia oleracea