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Literature summary extracted from

  • Lessire, R.; Chevalier, S.; Lucet-Levannier, K.; Lellouche, J.P.; Mioskowski, C.; Cassagne, C.
    Study of the 3-hydroxy-eicosanoyl-coenzyme A dehydratase and (E)-2,3 enoyl-coenzyme A reductase involved in acyl-coenzyme A elongation in etiolated leek seedlings (1999), Plant Physiol., 119, 1009-1015.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.1.8 microsome
-
 Allium ampeloprasum
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.8 trans-2-eicosenoyl-CoA + NADPH Allium ampeloprasum enzyme is part of acyl-CoA elongase complex responsible for fatty acid elongation eicosanoyl-CoA + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.8 Allium ampeloprasum
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.1.8 seedling
-
 Allium ampeloprasum
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.1.8 additional information
-
-
 Allium ampeloprasum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.8 trans-2-eicosenoyl-CoA + NADPH
-
 Allium ampeloprasum eicosanoyl-CoA + NADP+
-
 ?
1.3.1.8 trans-2-eicosenoyl-CoA + NADPH enzyme is part of acyl-CoA elongase complex responsible for fatty acid elongation Allium ampeloprasum eicosanoyl-CoA + NADP+
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.8 NADH 8 to 10fold less activity than with NADPH Allium ampeloprasum
1.3.1.8 NADPH preferred cofactor Allium ampeloprasum