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Literature summary for 1.2.1.13 extracted from

  • Yonuschot, G.R.; Ortwerth, B.J.; Koeppe, O.J.
    Purification and properties of a nicotinamide adenine dinucleotide phosphate-requiring glyceraldehyde 3-phosphate dehydrogenase from spinach leaves (1970), J. Biol. Chem., 245, 4193-4198.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
600000
-
equilibrium sedimentation 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
-
?

Cofactor

Cofactor Comment Organism Structure
NAD+ cofactor Spinacia oleracea
NAD+ NADP+ and NAD+ react with the enzyme at the same catalytic site Spinacia oleracea
NADP+ cofactor Spinacia oleracea
NADP+ NADP+ and NAD+ react with the enzyme at the same catalytic site Spinacia oleracea