KEGG   ENZYME: 1.14.14.78Help
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
BRITE hierarchy
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)
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 F polypeptide 11
Genes
HSA: 4051(CYP4F3) 57834(CYP4F11) 8529(CYP4F2)
PTR: 100616514(CYP4F11) 748117(CYP4F3) 748531(CYP4F2)
PPS: 100967411 100969141 100969847 100982619 100995728
GGO: 101125692 101126416 101135418 101151919 101152881
PON: 100174280(CYP4F11) 100434096
NLE: 100579320 100588006 100592711 100592938
MCC: 718349 719317 719353
MCF: 102120579 102130440(CYP4F3v2) 102134301(CYP4F45) 102135027(CYP4F11)
CSAB: 103234077 103234079 103234089 103234090
RRO: 104661011 104661012 104661014 104661137
CJC: 100411160 100411868(CYP4F11) 100412575(CYP4F2)
MMU: 170716(Cyp4f13) 64385(Cyp4f14) 72054(Cyp4f18)
RNO: 266689(Cyp4f6) 290623(Cyp4f18) 56266(Cyp4f1)
CFA: 484867
FCA: 105259722
BTA: 100295883 507016(CYP4F2) 507615(CYP4F2) 509506 534967
SSC: 100113470(CYP4F2) 100620559(CYP4F55) 110259329
LVE: 103089103
MYB: 102257438
PHI: 102108727
DRE: 100037390(cyp4f3)
SRX: 107715173
SANH: 107688049
SGH: 107597750
CCAR: 109105400
IPU: 108274321(CYP4F66)
PHYP: 113527727
EEE: 113590686
TRU: 101071805
LCO: 104935050
NCC: 104952154
OLA: 101170499
XMA: 102221417
XCO: 114141248
PRET: 103474609
KMR: 108246779
ALIM: 106525713
AOCE: 111580294
POV: 109644290
LCF: 108892835
SDU: 111236695
SLAL: 111665305
HCQ: 109528684
BPEC: 110153255
MALB: 109960560
SASA: 106577419 106592262(CP4F3)
ELS: 105009756
SFM: 108930167
PKI: 111834641
LAK: 106155350
 » show all
Taxonomy
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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