ExplorEnz: EC 1.14.14.80

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1.14.14.80

Accepted name:

long-chain fatty acid ω-monooxygenase

Reaction:

a long-chain fatty acid + [reduced NADPH—hemoprotein reductase] + O₂ = an ω-hydroxy-long-chain fatty acid + [oxidized NADPH—hemoprotein reductase] + H₂O

Other name(s):

CYP704B1 (gene name); CYP52M1 (gene name); CYP4A (gene name); CYP86A (gene name)

Systematic name:

long-chain fatty acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ω-hydroxylating)

Comments:

A cytochrome P-450 (heme thiolate) enzyme. The plant enzyme CYP704B1, which is involved in the synthesis of sporopollenin, a complex polymer found at the outer layer of spores and pollen, acts on palmitate (18:0), stearate (18:0) and oleate (18:1). The plant enzyme CYP86A1 also acts on laurate (12:0). The enzyme from the yeast Starmerella bombicola (CYP52M1) acts on C₁₆ to C₂₀ saturated and unsaturated fatty acids and can also hydroxylate the (ω-1) position. The mammalian enzyme CYP4A acts on laurate (12:0), myristate (14:0), palmitate (16:0), oleate (18:1), and arachidonate (20:4).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Benveniste, I., Tijet, N., Adas, F., Philipps, G., Salaun, J.P. and Durst, F. CYP86A1 from Arabidopsis thaliana encodes a cytochrome P450-dependent fatty acid ω-hydroxylase. Biochem. Biophys. Res. Commun. 243 (1998) 688–693. [DOI] [PMID: 9500987]
2.	Hoch, U., Zhang, Z., Kroetz, D.L. and Ortiz de Montellano, P.R. Structural determination of the substrate specificities and regioselectivities of the rat and human fatty acid ω-hydroxylases. Arch. Biochem. Biophys. 373 (2000) 63–71. [DOI] [PMID: 10620324]
3.	Dobritsa, A.A., Shrestha, J., Morant, M., Pinot, F., Matsuno, M., Swanson, R., Møller, B.L. and Preuss, D. CYP704B1 is a long-chain fatty acid ω-hydroxylase essential for sporopollenin synthesis in pollen of Arabidopsis. Plant Physiol. 151 (2009) 574–589. [DOI] [PMID: 19700560]
4.	Huang, F.C., Peter, A. and Schwab, W. Expression and characterization of CYP52 genes involved in the biosynthesis of sophorolipid and alkane metabolism from Starmerella bombicola. Appl. Environ. Microbiol. 80 (2014) 766–776. [DOI] [PMID: 24242247]

[EC 1.14.14.80 created 2015 as EC 1.14.13.205, transferred 2018 to EC 1.14.14.80]