IUBMB Enzyme Nomenclature

EC 1.14.13.194

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 1.14.13.30, leukotriene-B4 20-monooxygenase [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

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 1.14.13.194 created 2014]


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