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Literature summary extracted from

  • Dyer, J.M.; Chapital, D.C.; Kuan, J.C.; Mullen, R.T.; Turner, C.; McKeon, T.A.; Pepperman, A.B.
    Molecular analysis of a bifunctional fatty acid conjugase/desaturase from tung. Implications for the evolution of plant fatty acid diversity (2002), Plant Physiol., 130, 2027-2038.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.19.14 expressed in Nicotiana tabacum BY-2 cells and in Saccharomyces cerevisiae Vernicia fordii
1.14.19.33 expression in Saccharomyces cerevisiae Vernicia fordii
1.14.19.33 gene FADX, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional expression of the enzyme in Saccharomyces cerevisiae strain MMYO11, transient expression of myc-tagged enzyme in Nicotiana tabacum cv. Bright-Yellow 2 suspension-cultured BY-2 cells Vernicia fordii
1.14.19.34 gene FAD2, DNA and amino acid sequence determination and analysis, functional expression of the enzyme in Saccharomyces cerevisiae strain MMYO11,transient expression of myc-tagged enzyme in Nicotiana tabacum cv. Bright-Yellow 2 suspension-cultured BY-2 cells Vernicia fordii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.19.14 endoplasmic reticulum
-
 Vernicia fordii 5783
-
1.14.19.33 endoplasmic reticulum
-
 Vernicia fordii 5783
-
1.14.19.34 endoplasmic reticulum
-
 Vernicia fordii 5783
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.19.33 a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ Vernicia fordii the enzyme is involved in the biosynthetic pathway of eleostearic acid an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate ?
1.14.19.33 a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ Vernicia fordii
-
 an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
-
 ?
1.14.19.33 a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ Vernicia fordii the enzyme is involved in the biosynthetic pathway of eleostearic acid an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate ?
1.14.19.34 an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ Vernicia fordii
-
 a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.19.14 Vernicia fordii Q8GZC2
-
-
1.14.19.33 Vernicia fordii Q8GZC2
-
-
1.14.19.34 Vernicia fordii Q8GZC3
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.19.14 additional information not detected in seed Vernicia fordii
-
1.14.19.14 seed
-
 Vernicia fordii
-
1.14.19.33 seed expressed exclusively within developing seeds Vernicia fordii
-
1.14.19.33 seed FADX is expressed exclusively in developing tung seeds Vernicia fordii
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.19.14 (6Z,9Z,12Z)-octadec-6,9,12-trienoyl-[glycerolipid] + reduced acceptor + O2
-
 Vernicia fordii (6Z,9Z,11E,13E)-octadec-6,9,11,13-tetraenoyl -[glycerolipid] + acceptor + H2O
-
 ?
1.14.19.14 (9Z)-hexadec-9-enoyl -[glycerolipid] + reduced acceptor + O2
-
 Vernicia fordii (9Z,12E)-hexadec-9,12-dienoyl-[glycerolipid] + acceptor + H2O
-
 ?
1.14.19.14 (9Z)-octadec-9-enoyl-[glycerolipid] + reduced acceptor + O2
-
 Vernicia fordii (9Z,12E)-octadec-9,12-dienoyl-[glycerolipid] + acceptor + H2O
-
 ?
1.14.19.14 (9Z,12Z)-octadec-9,12-dienoyl-[glycerolipid] + reduced acceptor + O2
-
 Vernicia fordii (9Z,11Z,13Z)-octadec-9,12,13-trienoyl-[glycerolipid] + acceptor + H2O
-
 ?
1.14.19.14 (9Z,12Z,15Z)-octadec-9,12,15-trienoyl-[glycerolipid] + reduced acceptor + O2
-
 Vernicia fordii (9Z,11E,13E,15Z)-octadec-9,11,13,15-tetraenoyl-[glycerolipid] + acceptor + H2O
-
 ?
1.14.19.14 additional information FADX is a bifunctional enzyme with robust desaturase/conjugase activity Vernicia fordii ?
-
 ?
1.14.19.33 (6Z,9Z,12Z)-octadeca-6,9,12-trienoate + 2 ferrocytochrome b5 + O2 + 2 H+
-
 Vernicia fordii (6Z,9Z,11E,13E)-octadeca-6,9,11,13-tetraenoate + 2 ferricytochrome b5 + 2 H2O
-
 ?
1.14.19.33 (9Z)-hexadecenoate + 2 ferrocytochrome b5 + O2 + 2 H+
-
 Vernicia fordii (9Z,12E)-hexadeca-9,12-dienoate + 2 ferricytochrome b5 + 2 H2O
-
 ?
1.14.19.33 (9Z)-octadecenoate + 2 ferrocytochrome b5 + O2 + 2 H+
-
 Vernicia fordii (9Z,12E)-octadeca-9,12-dienoate + 2 ferricytochrome b5 + 2 H2O
-
 ?
1.14.19.33 a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
-
 Vernicia fordii an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate ?
1.14.19.33 a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ the enzyme is involved in the biosynthetic pathway of eleostearic acid Vernicia fordii an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate ?
1.14.19.33 a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
-
 Vernicia fordii an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
-
 ?
1.14.19.33 a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
-
 Vernicia fordii an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate ?
1.14.19.33 a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ the enzyme is involved in the biosynthetic pathway of eleostearic acid Vernicia fordii an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate ?
1.14.19.33 a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ the double bond introduced by FADX during fatty acid desaturation is in the trans, rather than cis, configuration Vernicia fordii an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
-
 ?
1.14.19.33 additional information the enzyme is capable of generating a variety of alternative conjugated and 12-desaturated fatty acid products in yeast cells cultured in the presence of exogenously supplied fatty acid substrates Vernicia fordii ?
-
 ?
1.14.19.33 additional information a bifunctional enzyme also exhibiting the activity of EC 1.14.19.34 Vernicia fordii ?
-
 ?
1.14.19.34 an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
-
 Vernicia fordii a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
-
 ?
1.14.19.34 additional information a bifunctional enzyme also exhibiting the activity of EC 1.14.19.33 Vernicia fordii ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.19.14 FADX
-
 Vernicia fordii
1.14.19.33 DELTA12 desaturase
-
 Vernicia fordii
1.14.19.33 DELTA12 oleate desaturase
-
 Vernicia fordii
1.14.19.33 FADX
-
 Vernicia fordii
1.14.19.34 DELTA12 oleate desaturase
-
 Vernicia fordii
1.14.19.34 DELTA12 oleic acid desaturase
-
 Vernicia fordii
1.14.19.34 FAD2
-
 Vernicia fordii

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.19.33 cytochrome b5
-
 Vernicia fordii
1.14.19.34 cytochrome b5
-
 Vernicia fordii

General Information

EC Number General Information Comment Organism
1.14.19.14 physiological function enzyme expression is occasionally associated with dramatic changes in morphology of the endoplasmic reticulum Vernicia fordii
1.14.19.33 evolution tung FADX is grouped with DELTA12 fatty acid desaturases and hydroxylases rather than conjugases, which is consistent with its desaturase activity Vernicia fordii
1.14.19.33 additional information incubation of yeast cells expressing FADX with exogenously supplied palmitoleicacid leads to substantial incorporation of thisfatty acid into yeast cells, accounting for approximately79% of total fatty acids. Oleic acid is reduced to only 3% under these growth conditions Vernicia fordii
1.14.19.33 physiological function FADX converts linoleic acid into alpha-eleostearic acid. in the plant seed oil Vernicia fordii
1.14.19.34 evolution the enzyme belongs to the FAD2 enzyme family Vernicia fordii
1.14.19.34 physiological function FAD2 converts oleic acid into linoleic acid in the plant seed oil Vernicia fordii