KEGG   ENZYME: 1.14.14.1Help
Entry
EC 1.14.14.1                Enzyme                                 

Name
unspecific monooxygenase;
microsomal monooxygenase;
xenobiotic monooxygenase;
aryl-4-monooxygenase;
aryl hydrocarbon hydroxylase;
microsomal P-450;
flavoprotein-linked monooxygenase;
flavoprotein monooxygenase
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
substrate,reduced-flavoprotein:oxygen oxidoreductase (RH-hydroxylating or -epoxidizing)
Reaction(IUBMB)
RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Reaction(KEGG)
Substrate
RH [CPD:C01371];
reduced flavoprotein [CPD:C03024];
O2 [CPD:C00007]
Product
ROH [CPD:C01335];
oxidized flavoprotein [CPD:C03161];
H2O [CPD:C00001]
Comment
A group of heme-thiolate proteins (P-450), acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. Together with EC 1.6.2.4, NADPH---hemoprotein reductase, it forms a system in which two reducing equivalents are supplied by NADPH. Some of the reactions attributed to EC 1.14.15.3, alkane 1-monooxygenase, belong here.
History
EC 1.14.14.1 created 1961 as EC 1.99.1.1, transferred 1965 to EC 1.14.1.1, transferred 1972 to EC 1.14.14.1 (EC 1.14.14.2 created 1972, incorporated 1976; EC 1.14.99.8 created 1972, incorporated 1984)
Pathway
Fatty acid degradation
Steroid hormone biosynthesis
Caffeine metabolism
Tryptophan metabolism
Arachidonic acid metabolism
Linoleic acid metabolism
Aminobenzoate degradation
Retinol metabolism
Metabolism of xenobiotics by cytochrome P450
Drug metabolism - cytochrome P450
Metabolic pathways
Microbial metabolism in diverse environments
Orthology
K00490  
cytochrome P450, family 4, subfamily F
K00493  
unspecific monooxygenase
K07408  
cytochrome P450, family 1, subfamily A, polypeptide 1
K07409  
cytochrome P450, family 1, subfamily A, polypeptide 2
K07410  
cytochrome P450, family 1, subfamily B, polypeptide 1
K07411  
cytochrome P450, family 2, subfamily A
K07412  
cytochrome P450, family 2, subfamily B
K07413  
cytochrome P450, family 2, subfamily C
K07414  
cytochrome P450, family 2, subfamily D
K07416  
cytochrome P450, family 2, subfamily F
K07418  
cytochrome P450, family 2, subfamily J
K07420  
cytochrome P450, family 2, subfamily S, polypeptide 1
K07424  
cytochrome P450, family 3, subfamily A
K07426  
cytochrome P450, family 4, subfamily B, polypeptide 1
K07428  
cytochrome P450, family 4, subfamily X
K07429  
cytochrome P450, family 4, subfamily Z
K14338  
cytochrome P450 / NADPH-cytochrome P450 reductase
K17684  
cytochrome P450, family 2, subfamily A, polypeptide 7
K17685  
cytochrome P450, family 2, subfamily A, polypeptide 13
K17690  
cytochrome P450, family 3, subfamily A, polypeptide 5
K17691  
cytochrome P450, family 3, subfamily A, polypeptide 7
K17692  
cytochrome P450, family 3, subfamily A, polypeptide 43
K17712  
cytochrome P450, family 2, subfamily D, polypeptide 6
K17718  
cytochrome P450, family 2, subfamily C, polypeptide 8
K17720  
cytochrome P450, family 2, subfamily C, polypeptide 18
K17728  
cytochrome P450, family 4, subfamily F, polypeptide 8
K17729  
cytochrome P450, family 4, subfamily F, polypeptide 11
K17730  
cytochrome P450, family 4, subfamily F, polypeptide 12
Genes
HSA: 
11283(CYP4F8) 1543(CYP1A1) 1544(CYP1A2) 1545(CYP1B1) 1549(CYP2A7) 1551(CYP3A7) 1553(CYP2A13) 1558(CYP2C8) 1562(CYP2C18) 1565(CYP2D6) 1572(CYP2F1) 1573(CYP2J2) 1577(CYP3A5) 1580(CYP4B1) 199974(CYP4Z1) 260293(CYP4X1) 29785(CYP2S1) 57834(CYP4F11) 64816(CYP3A43) 66002(CYP4F12)
PTR: 
PPS: 
GGO: 
PON: 
MCC: 
100144394(CYP3A7) 100424240(CYP2C76) 678683(CYP2C8) 678686(CYP2C75) 678689(CYP2A24) 678690(CYP2A23) 678691(CYP2D6) 678692(CYP3A5) 678694(CYP1A1) 678696(CYP2F1) 693631 701855(CYP2C18) 702954(CYP2A26) 705753 709290 709535 709770(CYP3A43) 710385(CYP1B1) 718335(CYP4F8) 718379(CYP4F12) 722086
MCF: 
MMU: 
100041375(Cyp3a41b) 100066(Cyp2j11) 106648(Cyp4f15) 107141(Cyp2c50) 13076(Cyp1a1) 13077(Cyp1a2) 13078(Cyp1b1) 13085(Cyp2a12) 13086(Cyp2a4) 13087(Cyp2a5) 13088(Cyp2b10) 13089(Cyp2b13) 13090(Cyp2b19) 13094(Cyp2b9) 13095(Cyp2c29) 13096(Cyp2c37) 13097(Cyp2c38) 13098(Cyp2c39) 13099(Cyp2c40) 13101(Cyp2d10) 13105(Cyp2d9) 13107(Cyp2f2) 13109(Cyp2j5) 13110(Cyp2j6) 13112(Cyp3a11) 13113(Cyp3a13) 13114(Cyp3a16) 13120(Cyp4b1) 208285(Cyp4f17) 223706(Cyp2d34) 226105(Cyp2c70) 226143(Cyp2c44) 230459(Cyp2j13) 242546(Cyp2j12) 243881(Cyp2b23) 320997(Cyp4f39) 337924(Cyp3a44) 380997(Cyp2d12) 404195(Cyp2c54) 433247(Cyp2c68) 53973(Cyp3a41a) 545123(Cyp2d11) 56388(Cyp3a25) 56448(Cyp2d22) 631304(Cyp4f40) 665095(Cyp2j8) 69888(Cyp2c66) 70101(Cyp4f16) 71754(Cyp2d40) 72082(Cyp2c55) 72303(Cyp2c65) 74134(Cyp2s1) 74519(Cyp2j9) 76279(Cyp2d26) 81906(Cyp4x1)
RNO: 
100910877 171352(Cyp3a9) 171518(Cyp2c22) 171521(Cyp2c13) 171522(Cyp2d4) 24296(Cyp1a1) 24297(Cyp1a2) 24299(Cyp2a3) 24300(Cyp2b1) 24303(Cyp2d3) 24307(Cyp4b1) 246767(Cyp4x1) 24894(Cyp2a1) 24895(Cyp2a2) 25011(Cyp2c12) 25053(Cyp2d2) 252931(Cyp3a18) 25426(Cyp1b1) 25642(Cyp3a23/3a1) 266682(Cyp3a2) 266684(Cyp2d1) 286904(Cyp4f4) 286905(Cyp4f5) 286953(Cyp2b3) 286963(Cyp2d5) 292728(Cyp2b21) 29277(Cyp2c11) 29295(Cyp2b12) 29298(Cyp2c7) 293989(Cyp2c6v1) 299566(Cyp4f39) 308445(Cyp2s1) 313373(Cyp2j10) 313375(Cyp2j3) 361523(Cyp2b2) 499353(Cyp2c24) 500801(Cyp4f17) 502969(Cyp2j16) 503122(Cyp4f40) 54246(Cyp2f4) 65210(Cyp2j4) 83790(Cyp2c23)
CGE: 
HGL: 
TUP: 
CFA: 
100686778(CYP1A1) 100688697 415120(CYP2D15) 415122(CYP2C18) 415123(CYP2C41) 415129(CYP3A12) 474177(CYP2B6) 479740(CYP3A4) 482505(CYP4X1) 483038(CYP1B1) 484491(CYP2S1) 484494(CYP2A13) 494010(CYP1A2) 608452(CYP4B1) 610195(CYP2J2) 612477
AML: 
FCA: 
PTG: 
BTA: 
100847677 282211(CYP2D14) 282214(CYP3A5) 282870(CYP1A1) 504769(CYP2B6) 507988(CYP3A4) 510406(CYP2J2) 511470(CYP1B1) 511498 511936 514971(CYP2S1) 521656 526682(CYP3A5) 530571 530929 535243(CYP2C18) 540149(CYP4B1) 540707(CYP2A13) 616593(CYP2C87) 785540 785824(MGC127055)
BOM: 
PHD: 
CHX: 
OAS: 
SSC: 
100126281(CYP3A46) 100144468(CYP3A22) 100152910(CYP1A2) 100523190 100523909 100524750(CYP2J34) 100524940 100525112 100625479 100627093 397687(CYP2D25) 403103(CYP1A1) 403104(CYP2B22) 403106(CYP2C32) 403107(CYP2C33) 403111(CYP2C42) 403149(CYP2A19) 403215(CYP2C49) 403322(CYP3A39) 403324(CYP3A29)
CFR: 
BACU: 
LVE: 
ECB: 
MYB: 
MYD: 
PALE: 
MDO: 
SHR: 
OAA: 
GGA: 
100859277(CYP4F22) 396051(CYP1A1) 414832(CYP3A7) 414833(CYP2C45) 416477(CYP3A4) 417981(CYP2D6) 421466(CYP1B1) 424618(CYP4B1) 424676 424677 424678(CYP2J2) 424729 428832(CYP1B1) 771974
MGP: 
TGU: 
FAB: 
PHI: 
APLA: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
PBI: 
XLA: 
100036770(cyp2a6) 100036771(cyp4b1.2) 100036772(cyp4b1) 100036775(cyp1a1) 100036876 100037189(cyp3a4) 100337565(cyp4f42) 100337623 373549(cypxl301-a) 379297(cyp2c8.1) 379479(cyp2d6-b) 398964 432343(cyp2c18) 432347 444542(cyp2c8.2) 446878(cyp2d6) 495363(cyp3a5)
XTR: 
DRE: 
100034366(cyp2p8) 100034406(cyp2p7) 100150054(cyp1b1) 140634(cyp1a) 387527(cyp4t8) 393108(cyp2p6) 393592(cyp2p9) 399485(cyp2p10) 553969(cyp3a65) 792566 797309(cyp2j20)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
CIN: 
SPU: 
PHU: 
ISC: 
LOA: 
NVE: 
TAD: 
AQU: 
CIT: 
CIC: 
CAM: 
PPER: 
PMUM: 
MDM: 
CSV: 
CMO: 
RCU: 
POP: 
POPTR_0007s06240g(POPTRDRAFT_654851) POPTR_0007s06270g(POPTRDRAFT_562670) POPTR_0007s06310g(POPTRDRAFT_562677)
VVI: 
SBI: 
SORBI_03g028720(SORBIDRAFT_03g028720)
SMO: 
SELMODRAFT_144382(CYP703C2_v2) SELMODRAFT_74166(CYP703C2) SELMODRAFT_96541(CYP711A17) SELMODRAFT_97512(MAX1-2)
PPP: 
CRE: 
CSL: 
SCE: 
YDR402C(DIT2)
AGO: 
KLA: 
LTH: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0A12020(NCAS0A12020)
TPF: 
TPHA_0E02110(TPHA0E02110)
PIC: 
PICST_35590(ALK2) PICST_63000(CYP559)
LEL: 
CAL: 
CaO19.554(DIT2)
CDU: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_772164(AO090001000445)
ANG: 
ANI_1_2654014(An01g06820) ANI_1_396144(An16g02820)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
URE: 
ABE: 
TVE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
DSQ: 
SHS: 
PCO: 
PSQ: 
ADL: 
FME: 
GTR: 
MPR: 
MRR: 
SCM: 
UMA: 
TET: 
NGR: 
PCT: 
PEN: 
FTU: 
FTF: 
MME: 
RPI: 
RPF: 
REH: 
CNC: 
RME: 
BUR: 
VAP: 
VPE: 
VPD: 
HOH: 
MLO: 
SME: 
ATU: 
RET: 
RLE: 
BJA: 
BJU: 
BRA: 
BBT: 
BRS: 
RPB: 
RPD: 
RPE: 
AZC: 
SIT: 
RSP: 
RSQ: 
RDE: 
ELI: 
BSU: 
BSU07250(yetO) BSU27160(cypB)
BSR: 
BSL: 
BSH: 
BSY: 
BSS: 
BST: 
BSO: 
BSN: 
BSQ: 
BSUB: 
BSX: 
C663_0751(cypD) C663_2550(cypE)
BSP: 
BLI: 
BL02398(cypE)
BLD: 
BLi02848(yrhJ)
BLH: 
BAO: 
BAMF_0695(yetO) BAMF_2522(cypB)
BAY: 
BAQ: 
BYA: 
BAMP: 
BAML: 
BAMA: 
RBAU_0722(cypD) RBAU_2563(cypB)
BAMN: 
BASU_0699(cypD) BASU_2369(cypB)
BAMB: 
BAMT: 
BAZ: 
BQL: 
LL3_00745(yetO) LL3_02800(yrhJ)
BXH: 
BQY: 
MUS_0726(yetO) MUS_2901(yrhJ)
BAMI: 
BAMC: 
BAMF: 
BAE: 
BAN: 
BA_3221(cypD)
BAR: 
GBAA_3221(cypD)
BAT: 
BAH: 
BAI: 
BAA_3269(cypD)
BAX: 
BANT: 
BANR: 
BANS: 
BAL: 
BCE: 
BCA: 
BCE_3239(cypD)
BCZ: 
BCR: 
BCB: 
BCU: 
BCG: 
BCQ: 
BCQ_3034(cypD)
BCX: 
BCA_3251(cypD)
BNC: 
BCF: 
BCER: 
BTK: 
BTL: 
BTB: 
BTT: 
BTC: 
BTF: 
BTM: 
BTG: 
BTI: 
BTN: 
BTHT: 
BTHU: 
BWE: 
BTY: 
BMYC: 
DJ92_5480(cyp102A1)
BPU: 
BPUM_1680(yrhJ)
BPUM: 
BMQ: 
BMD: 
BMH: 
BJS: 
HHD: 
GYM: 
PPM: 
PPO: 
PPM_3514(M1_3883)
PPOL: 
PPQ: 
PMS: 
PMW: 
MGI: 
MSP: 
MABB: 
MRH: 
MNE: 
CUV: 
NFA: 
RHA: 
RER: 
REY: 
ROP: 
REQ: 
RPY: 
GBR: 
GPO: 
SRT: 
SCO: 
SCO0801(SCF43.12) SCO3636(SCH10.14c)
SMA: 
SAV_4539(cyp20) SAV_575(cyp2) SAV_7426(cyp27)
SCB: 
SCT: 
SCAT_4838(CYP102A)
SCY: 
SHY: 
SHO: 
SDV: 
SCI: 
SALU: 
NCA: 
SRO: 
NML: 
SEN: 
AOI: 
PDX: 
KAL: 
SACI: 
AVA: 
SGN: 
HAU: 
DGE: 
DDR: 
DGO: 
PTO: 
 » show all
Taxonomy
Reference
1  [PMID:13426111]
  Authors
BOOTH J, BOYLAND E.
  Title
The biochemistry of aromatic amines.  III.  Enzymic hydroxylation by rat-liver microsomes.
  Journal
Biochem. J. 66 (1957) 73-8.
Reference
2  [PMID:5132997]
  Authors
Fujita T, Mannering GJ.
  Title
Differences in soluble P-450 hemoproteins from livers of rats treated with phenobarbital and 3-methylcholanthrene.
  Journal
Chem. Biol. Interact. 3 (1971) 264-5.
Reference
3  [PMID:187601]
  Authors
Haugen DA, Coon MJ.
  Title
Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450.
  Journal
J. Biol. Chem. 251 (1976) 7929-39.
Reference
4  [PMID:3415241]
  Authors
Imaoka S, Inoue K, Funae Y.
  Title
Aminopyrine metabolism by multiple forms of cytochrome P-450 from rat liver microsomes: simultaneous quantitation of four aminopyrine metabolites by high-performance liquid chromatography.
  Journal
Arch. Biochem. Biophys. 265 (1988) 159-70.
Reference
5  [PMID:434823]
  Authors
Johnson EF, Zounes MC, Muller-Eberhard U.
  Title
Characterization of three forms of rabbit microsomal cytochrome P-450 by peptide mapping utilizing limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.
  Journal
Arch. Biochem. Biophys. 192 (1979) 282-9.
Reference
6  [PMID:489601]
  Authors
Kupfer D, Miranda GK, Navarro J, Piccolo DE, Theoharides AD.
  Title
Effect of inducers and inhibitors of monooxygenase on the hydroxylation of prostaglandins in the guinea pig. Evidence for several monooxygenases catalyzing omega- and omega-1-hydroxylation.
  Journal
J. Biol. Chem. 254 (1979) 10405-14.
Reference
7  [PMID:7298645]
  Authors
Lang MA, Gielen JE, Nebert DW.
  Title
Genetic evidence for many unique liver microsomal P-450-mediated monooxygenase activities in heterogeneic stock mice.
  Journal
J. Biol. Chem. 256 (1981) 12068-75.
Reference
8  [PMID:7298644]
  Authors
Lang MA, Nebert DW.
  Title
Structural gene products of the Ah locus. Evidence for many unique P-450-mediated monooxygenase activities reconstituted from 3-methylcholanthrene-treated C57BL/6N mouse liver microsomes.
  Journal
J. Biol. Chem. 256 (1981) 12058-67.
Reference
9  [PMID:2916844]
  Authors
Leo MA, Lasker JM, Raucy JL, Kim CI, Black M, Lieber CS.
  Title
Metabolism of retinol and retinoic acid by human liver cytochrome P450IIC8.
  Journal
Arch. Biochem. Biophys. 269 (1989) 305-12.
Reference
10 [PMID:4401153]
  Authors
Lu AY, Kuntzman R, West S, Jacobson M, Conney AH.
  Title
Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds, and endogenous substrates. II. Role of the cytochrome P-450 and P-448 fractions in drug and steroid hydroxylations.
  Journal
J. Biol. Chem. 247 (1972) 1727-34.
Reference
11 [PMID:13314626]
  Authors
MITOMA C, POSNER HS, REITZ HC, UDENFRIEND S.
  Title
Enzymatic hydroxylation of aromatic compounds.
  Journal
Arch. Biochem. Biophys. 61 (1956) 431-41.
Reference
12
  Authors
Mitoma, C. and Udenfriend, S.
  Title
Aryl-4-hydroxylase.
  Journal
Methods Enzymol. 5 (1962) 816-819.
Reference
13 [PMID:7295706]
  Authors
Napoli JL, Okita RT, Masters BS, Horst RL.
  Title
Identification of 25,26-dihydroxyvitamin D3 as a rat renal 25-hydroxyvitamin D3 metabolite.
  Journal
Biochemistry. 20 (1981) 5865-71.
Reference
14 [PMID:4387094]
  Authors
Nebert DW, Gelboin HV.
  Title
Substrate-inducible microsomal aryl hydroxylase in mammalian cell culture. I. Assay and properties of induced enzyme.
  Journal
J. Biol. Chem. 243 (1968) 6242-9.
Reference
15 [PMID:3264134]
  Authors
Suhara K, Ohashi K, Takahashi K, Katagiri M.
  Title
Aromatase and nonaromatizing 10-demethylase activity of adrenal cortex mitochondrial P-450(11)beta.
  Journal
Arch. Biochem. Biophys. 267 (1988) 31-7.
Reference
16 [PMID:7462235]
  Authors
Theoharides AD, Kupfer D.
  Title
Evidence for different hepatic microsomal monooxygenases catalyzing omega- and (omega-1)-hydroxylations of prostaglandins E1 and E2. Effects of inducers of monooxygenase on the kinetic constants of prostaglandin hydroxylation.
  Journal
J. Biol. Chem. 256 (1981) 2168-75.
Reference
17 [PMID:825720]
  Authors
Thomas PE, Lu AY, Ryan D, West SB, Kawalek J, Levin W.
  Title
Immunochemical evidence for six forms of rat liver cytochrome P450 obtained using antibodies against purified rat liver cytochromes P450 and P448.
  Journal
Mol. Pharmacol. 12 (1976) 746-58.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
9038-14-6

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