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Literature summary extracted from

  • Dauk, M.; Lam, P.; Kunst, L.; Smith, M.A.
    A FAD2 homologue from Lesquerella lindheimeri has predominantly fatty acid hydroxylase activity (2007), Plant Sci., 173, 43-49.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.18.4 gene FAH12, subcloning in Escherichia coli strain DH5alpha, expression in Saccharomyces cerevisiae results in the synthesis of ricinoleic acid and very low levels of di-unsaturated fatty acids. Expression of LlinFAH12 in Arabidopsis thaliana seeds results in hydroxy fatty acid accumulation, fatty acid composition in transformed compared to wild-type plants, overview Physaria lindheimeri

Protein Variants

EC Number Protein Variants Comment Organism
1.14.18.4 M295L site-directed mutagenesis, expression of the mutant FAH12gene in yeast does not result in any obvious changes in the ratio of hydroxy and diunsaturated fatty acids accumulating Physaria lindheimeri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.18.4 additional information Physaria lindheimeri in Lesquerella fendleri ricinoleic acid is efficiently elongated to lesquerolic acid in a reaction catalyzed by a condensing enzyme specific to hydroxy fatty acids ?
-
 ?
1.14.18.4 oleate + ferrocytochrome P-450 + H+ + O2 Physaria lindheimeri the enzyme is primarily a fatty acid hydroxylase, rather than a bifunctional oleate 12-hydroxylase-desaturase, involved in ricinoleic acid biosynthesis, overview 12-hydroxy-oleate + ferricytochrome P-450 + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.18.4 Physaria lindheimeri A5HB93 gene FAH12
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.18.4 seed
-
 Physaria lindheimeri
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.18.4 additional information in Lesquerella fendleri ricinoleic acid is efficiently elongated to lesquerolic acid in a reaction catalyzed by a condensing enzyme specific to hydroxy fatty acids Physaria lindheimeri ?
-
 ?
1.14.18.4 oleate + ferrocytochrome P-450 + H+ + O2 the enzyme is primarily a fatty acid hydroxylase, rather than a bifunctional oleate 12-hydroxylase-desaturase, involved in ricinoleic acid biosynthesis, overview Physaria lindheimeri 12-hydroxy-oleate + ferricytochrome P-450 + H2O
-
 ?
1.14.18.4 oleate + ferrocytochrome P-450 + H+ + O2 the enzyme is primarily a fatty acid hydroxylase rather than a bifunctional oleate 12-hydroxylase-desaturase, overview Physaria lindheimeri 12-hydroxy-oleate + ferricytochrome P-450 + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.18.4 oleate 12-hydroxylase
-
 Physaria lindheimeri

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.18.4 NADH
-
 Physaria lindheimeri