Literature summary for 1.14.18.6 extracted from

Mitchell, A.; Martin, C.
Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids (1997), J. Biol. Chem., 272, 28281-28288.

Search for more literature for 1.14.18.6

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	protein is predicted to have two hydrophobic domains, each capable of spanning the membrane twice, and has the HX(2-3)(XH)H motifs that are characteristic of membrane-bound fatty acid desaturases	Saccharomyces cerevisiae	16020	-

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	Q03529	-	-

Synonyms

Synonyms	Comment	Organism
FAH1	-	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
cytochrome b5	expression of the FAH1 cytochrome b5 domain in Escherichia coli produces a soluble protein that exhibits the typical oxidized versus reduced differential absorbance spectra of cytochrome b5	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
physiological function	disruption of the FAH1 gene does not give any visible phenotype, and there is no observable difference in content or distribution of the most abundant long chain saturated and unsaturated 14-18-carbon fatty acid species. The gene-disrupted DELTAfah1 strain shows an approximately 40fold reduction of alpha-hydroxy-fatty acid 26:0 and a complementary increase in fatty acid 26:0. Expression of Arabidopsis thaliana FAH1 gene, which does not contain the cytochrome b5 domain, in the Saccharomyces cerevisiae DELTAfah1 strain produces an approximately 25fold increase in alpha-hydroxyfatty acid 26:0 and reduces the levels of its 26-carbon precursor	Saccharomyces cerevisiae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)