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Literature summary for 1.1.1.24 extracted from

  • Graziana, A.; Ranjeva, R.; Salimath, B.P.; Boudet, A.M.
    The reversible association of quinate:NAD+ oxidoreductase from carrot cells with a putative regulatory subunit depends on light conditions (1983), FEBS Lett., 163, 306-311.
No PubMed abstract available

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
transfer of carrot enzyme from dark to light conditions shifts MW from 42000 Da to 110000 Da, probably due to association of a regulatory subunit which may be a calciprotein Daucus carota
40000
-
1 * 40000 + 1 * 60000-63000, SDS-PAGE Daucus carota
110000
-
gel filtration Daucus carota

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-dehydroquinate + NADH Daucus carota
-
quinate + NAD+
-
r
quinate + NAD+ Daucus carota
-
5-dehydroquinate + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Daucus carota
-
carrot
-

Purification (Commentary)

Purification (Comment) Organism
-
Daucus carota

Source Tissue

Source Tissue Comment Organism Textmining
cell suspension culture
-
Daucus carota
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-dehydroquinate + NADH
-
Daucus carota quinate + NAD+
-
r
quinate + NAD+
-
Daucus carota 5-dehydroquinate + NADH + H+
-
?
quinate + NAD+
-
Daucus carota 5-dehydroquinate + NADH + H+
-
r

Subunits

Subunits Comment Organism
dimer 1 * 40000 + 1 * 60000-63000, SDS-PAGE Daucus carota