The Enzyme Database

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Accepted name: phylloquinone ω-hydroxylase
Reaction: phylloquinone + NADPH + H+ + O2 = ω-hydroxyphylloquinone + NADP+ + H2O
Other name(s): vitamin K1 ω-hydroxylase; CYP4F2; CYP4F11
Systematic name: phylloquinone,NADPH:oxygen oxidoreductase (ω-hydroxyphylloquinone forming)
Comments: A heme-thiolate protein (cytochrome P-450). Isolated from human tissue. The enzyme will also act on menaquinone-4. Prolonged action of CYP4F2, but not CYP4F11, on the ω hydroxyl group oxidizes it to the corresponding carboxylic acid. CYP4F2 also oxidizes leukotriene B4; see EC, leukotriene-B4 20-monooxygenase [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Jin, R., Koop, D.R., Raucy, J.L. and Lasker, J.M. Role of human CYP4F2 in hepatic catabolism of the proinflammatory agent leukotriene B4. Arch. Biochem. Biophys. 359 (1998) 89–98. [PMID: 9799565]
2.  Tang, Z., Salamanca-Pinzon, S.G., Wu, Z.L., Xiao, Y. and Guengerich, F.P. Human cytochrome P450 4F11: heterologous expression in bacteria, purification, and characterization of catalytic function. Arch. Biochem. Biophys. 494 (2010) 86–93. [PMID: 19932081]
3.  Edson, K.Z., Prasad, B., Unadkat, J.D., Suhara, Y., Okano, T., Guengerich, F.P. and Rettie, A.E. Cytochrome P450-dependent catabolism of vitamin K: ω-hydroxylation catalyzed by human CYP4F2 and CYP4F11. Biochemistry 52 (2013) 8276–8285. [PMID: 24138531]
[EC created 2014]

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