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
HSA4051(CYP4F3) 57834(CYP4F11) 8529(CYP4F2)
PTR100609185 100616514(CYP4F11) 748117(CYP4F3) 748531(CYP4F2)
PPS100967411(CYP4F2) 100969141(CYP4F3) 100995728(CYP4F11)
GGO101125692 101126416 101135418 101152881
PON100174280(CYP4F11) 100434096 100437847 100453229 100455064
NLE100579320 100588006 100592711 115836968
MCC718349 719317 719353
MCF102130440(CYP4F3) 102132489 102134301(CYP4F2) 102135027(CYP4F11)
CSAB103234079 103234089 103234090
CATY105601614 105601627 105601628
PANU101005940 101010705 101011071 116271679
TGE112612404 112613096 112613097
RRO104661011 104661012 104661014
RBB108543262 108543288 108543294 108543295
TFN117074427 117076174
PTEH111554202 111554233 111554287 111554290
CJC100411160 100411868(CYP4F11) 100412575(CYP4F2)
SBQ101050944 101051361
CSYR103250633
MMUR105867925 105867928 105867931
LCAT123634142 123636967 123639775
OGA100942215 100943471 100950748 100952962
CPOC100733735
OCU100348038 100350957
TUP102483333
VLG121495723
UAR123779961 123780007
LLV125083145
ZCA113917975
MLX118005050
MLF102425173 102436085
PKL118706555
DRO112305042
PDIC114503445
RFQ117038128
PGIG120606485
PVP105311420
RAY107517263
TOD119240020
LAV100657832
DNM101441145
 » 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
LinkDB

DBGET integrated database retrieval system