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Literature summary for 1.2.1.13 extracted from

  • Cerff, R.
    Glyceraldehyde-3-phosphate dehydrogenase (NADP) from Sinapis alba L. (1978), Plant Physiol., 61, 369-372.
    View publication on PubMedView publication on EuropePMC

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
1 * 42000, SDS-PAGE Sinapis alba

Organism

Organism UniProt Comment Textmining
Sinapis alba
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
seedling
-
Sinapis alba
-

Subunits

Subunits Comment Organism
monomer 1 * 42000, SDS-PAGE Sinapis alba
More NAD(P)-controlled aggregation of glyceraldehyde-3-phosphate dehydrogenase (NADP) is due primarily to enzyme association with a separate binding fraction rather than to enzyme polymerization Sinapis alba

Cofactor

Cofactor Comment Organism Structure
NADP+ cofactor Sinapis alba