Literature summary for 1.14.19.34 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.

Search for more literature for 1.14.19.34

Cloned(Commentary)

Cloned (Comment)	Organism
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

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	-	Vernicia fordii	5783	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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

Organism	UniProt	Comment	Textmining
Vernicia fordii	Q8GZC3	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+	-	Vernicia fordii	a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O	-	?
additional information	a bifunctional enzyme also exhibiting the activity of EC 1.14.19.33	Vernicia fordii	?	-	?

Synonyms

Synonyms	Comment	Organism
DELTA12 oleate desaturase	-	Vernicia fordii
DELTA12 oleic acid desaturase	-	Vernicia fordii
FAD2	-	Vernicia fordii

Cofactor

Cofactor	Comment	Organism	Structure
cytochrome b5	-	Vernicia fordii

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to the FAD2 enzyme family	Vernicia fordii
physiological function	FAD2 converts oleic acid into linoleic acid in the plant seed oil	Vernicia fordii

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Release 2023.1 (January 2023)