KEGG   ENZYME: 1.14.14.78
Entry
EC 1.14.14.78               Enzyme                                 
Name
phylloquinone omega-hydroxylase;
vitamin K1 omega-hydroxylase;
CYP4F2;
CYP4F11
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
phylloquinone,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (omega-hydroxyphylloquinone-forming)
Reaction(IUBMB)
phylloquinone + [reduced NADPH---hemoprotein reductase] + O2 = omega-hydroxyphylloquinone + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R10728]
Reaction(KEGG)
R10728
Substrate
phylloquinone [CPD:C02059];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007]
Product
omega-hydroxyphylloquinone [CPD:C20806];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
H2O [CPD:C00001]
Comment
A cytochrome P-450 (heme-thiolate) protein. Isolated from human tissue. The enzyme will also act on menaquinone-4. Prolonged action of CYP4F2, but not CYP4F11, on the omega 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].
History
EC 1.14.14.78 created 2014 as EC 1.14.13.194, transferred 2018 to EC 1.14.14.78
Orthology
K17726  phylloquinone omega-hydroxylase / docosahexaenoic acid omega-hydroxylase / leukotriene-B4 20-monooxygenase
K17729  cytochrome P450 family 4 subfamily F11
Genes
HSA: 4051(CYP4F3) 57834(CYP4F11) 8529(CYP4F2)
PTR: 100609185 100616514(CYP4F11) 748117(CYP4F3) 748531(CYP4F2)
PPS: 100967411(CYP4F2) 100969141(CYP4F3) 100995728(CYP4F11)
GGO: 101125692 101126416 101135418 101152881
PON: 100174280(CYP4F11) 100434096 100437847 100453229 100455064
NLE: 100579320 100588006 100592711 115836968
HMH: 116478624 116478627 116478629
MCC: 718349 719317 719353
MCF: 102130440(CYP4F3) 102132489 102134301(CYP4F2) 102135027(CYP4F11)
MTHB: 126942243 126942252 126942253
MNI: 105494188 105494300 105494717
CSAB: 103234079 103234089 103234090
CATY: 105601614 105601627 105601628
PANU: 101005940 101010705 101011071 116271679
TGE: 112612404 112613096 112613097
MLEU: 105540101 105540126 105540131
RRO: 104661011 104661012 104661014
RBB: 108543262 108543288 108543294 108543295
TFN: 117074427 117076174
PTEH: 111554202 111554233 111554287 111554290
CANG: 105519773 105519778 105519779
CJC: 100411160 100411868(CYP4F11) 100412575
SBQ: 101050944 101051361
CIMI: 108298561(CYP4F2)
CSYR: 103250633
MMUR: 105867925 105867928 105867931
LCAT: 123634142 123636967 123639775
PCOQ: 105810118 105825072 105825741 105827104
OGA: 100942215 100943471 100950748 100952962
CPOC: 100733735
OCU: 100348038 100350957
TUP: 102483333
GVR: 103593427 103610570
VLG: 121495723
UAR: 123779961 123780007
LLV: 125083145
ZCA: 113917975
MLX: 118005050
MLF: 102425173 102436085
PKL: 118706555
DRO: 112305042
PDIC: 114503445
RFQ: 117038128
PGIG: 120606485
PVP: 105311420
RAY: 107517263
TOD: 119240020
LAV: 100657832
DNM: 101441145
 » show all
Reference
1  [PMID:9799565]
  Authors
Jin R, Koop DR, Raucy JL, Lasker JM
  Title
Role of human CYP4F2 in hepatic catabolism of the proinflammatory agent leukotriene B4.
  Journal
Arch Biochem Biophys 359:89-98 (1998)
DOI:10.1006/abbi.1998.0880
  Sequence
[hsa:8529]
Reference
2  [PMID:19932081]
  Authors
Tang Z, Salamanca-Pinzon SG, Wu ZL, Xiao Y, Guengerich FP
  Title
Human cytochrome P450 4F11: heterologous expression in bacteria, purification, and characterization of catalytic function.
  Journal
Arch Biochem Biophys 494:86-93 (2010)
DOI:10.1016/j.abb.2009.11.017
  Sequence
[hsa:57834]
Reference
3  [PMID:24138531]
  Authors
Edson KZ, Prasad B, Unadkat JD, Suhara Y, Okano T, Guengerich FP, Rettie AE
  Title
Cytochrome P450-dependent catabolism of vitamin K: omega-hydroxylation catalyzed by human CYP4F2 and CYP4F11.
  Journal
Biochemistry 52:8276-85 (2013)
DOI:10.1021/bi401208m
  Sequence
[hsa:8529 57834]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.78
IUBMB Enzyme Nomenclature: 1.14.14.78
ExPASy - ENZYME nomenclature database: 1.14.14.78
BRENDA, the Enzyme Database: 1.14.14.78

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Chemical substance (6)   
   KEGG COMPOUND (6)   
Chemical reaction (2)   
   KEGG REACTION (1)   
   KEGG RCLASS (1)   
Gene (336)   
   KEGG ORTHOLOGY (2)   
   KEGG GENES (116)   
   RefGene (218)   
Protein sequence (7)   
   UniProt (2)   
   SWISS-PROT (2)   
   RefSeq(pep) (3)   
DNA sequence (5)   
   RefSeq(nuc) (5)   
Protein domain (5)   
   InterPro (5)   
All databases (361)   

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