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Literature summary 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.24 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
1.1.1.24 40000
-
1 * 40000 + 1 * 60000-63000, SDS-PAGE Daucus carota
1.1.1.24 110000
-
gel filtration Daucus carota

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.24 3-dehydroquinate + NADH Daucus carota
-
quinate + NAD+
-
r
1.1.1.24 quinate + NAD+ Daucus carota
-
5-dehydroquinate + NADH + H+
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.24 Daucus carota
-
carrot
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.24
-
Daucus carota

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.24 cell suspension culture
-
Daucus carota
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.24 3-dehydroquinate + NADH
-
Daucus carota quinate + NAD+
-
r
1.1.1.24 quinate + NAD+
-
Daucus carota 5-dehydroquinate + NADH + H+
-
?
1.1.1.24 quinate + NAD+
-
Daucus carota 5-dehydroquinate + NADH + H+
-
r

Subunits

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