| Entry |
|
|---|
| 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 O2 as oxidant and incorporation or
reduction of oxygen. The oxygen incorporated need not be derived
from O2;
With reduced flavin or flavoprotein as one donor, and incorporation
of one atom of oxygen into the other donor
 |
|---|
| Sysname |
substrate,reduced-flavoprotein:oxygen oxidoreductase
(RH-hydroxylating or -epoxidizing) |
|---|
| Reaction(IUBMB) |
RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
[RN:R04122] |
|---|
| Reaction(KEGG) |
R04122 > R01840 R01842 R02354 R02355 R02356 R02501 R02503 R03088
R03089 R03090 R03408 R03629 R04121;
(other) R02351 R03087 R03697 R04759 R04761 R05259 R07000 R07001
R07016 R07020 R07021 R07022 R07042 R07043 R07044 R07045 R07046
R07048 R07050 R07051 R07052 R07054 R07055 R07056 R07066 R07068
R07075 R07079 R07080 R07081 R07085 R07087 R07088 R07089 R07090
R07098 R07099 R07107 R07112 R07939 R07943 R07945 R08225 R08256
R08257 R08264 R08265 R08267 R08268 R08269 R08270 R08271 R08272
R08274 R08275 R08276 R08277 R08285 R08286 R08287 R08293 R08294
R08303 R08304 R08312 R08313 R08318 R08324 R08325 R08326 R08327
R08339 R08340 R08341 R08342 R08343 R08344 R08345 R08390 R08391
R08392
 |
|---|
| Substrate |
RH [CPD:C01371];
reduced flavoprotein [CPD:C03024];
O2 [CPD:C00007] |
|---|
| Product |
ROH [CPD:C01335];
oxidized flavoprotein [CPD:C03161];
H2O [CPD:C00001] |
|---|
| Cofactor |
Heme [CPD:C00032] |
|---|
| 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. |
|---|
| Pathway |
PATH: ec00071 Fatty acid metabolism
PATH: ec00140 Steroid hormone biosynthesis
PATH: ec00232 Caffeine metabolism
PATH: ec00361 gamma-Hexachlorocyclohexane degradation
PATH: ec00380 Tryptophan metabolism
PATH: ec00590 Arachidonic acid metabolism
PATH: ec00591 Linoleic acid metabolism
PATH: ec00830 Retinol metabolism
PATH: ec00980 Metabolism of xenobiotics by cytochrome P450
PATH: ec00982 Drug metabolism - cytochrome P450
PATH: ec00983 Drug metabolism - other enzymes
PATH: ec01063 Biosynthesis of alkaloids derived from shikimate
pathway
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K00493 unspecific monooxygenase
KO: K07408 cytochrome P450, family 1, subfamily A, polypeptide 1
KO: K07409 cytochrome P450, family 1, subfamily A, polypeptide 2
KO: K07410 cytochrome P450, family 1, subfamily B, polypeptide 1
KO: K07411 cytochrome P450, family 2, subfamily A
KO: K07412 cytochrome P450, family 2, subfamily B
KO: K07413 cytochrome P450, family 2, subfamily C
KO: K07414 cytochrome P450, family 2, subfamily D
KO: K07415 cytochrome P450, family 2, subfamily E
KO: K07416 cytochrome P450, family 2, subfamily F
KO: K07418 cytochrome P450, family 2, subfamily J
KO: K07420 cytochrome P450, family 2, subfamily S
KO: K07424 cytochrome P450, family 3, subfamily A
KO: K07426 cytochrome P450, family 4, subfamily B
KO: K07428 cytochrome P450, family 4, subfamily X
KO: K07429 cytochrome P450, family 4, subfamily Z
KO: K07434 cytochrome P450, family 19, subfamily A |
|---|
| Genes |
HSA: 1543(CYP1A1) 1544(CYP1A2) 1545(CYP1B1) 1548(CYP2A6)
1549(CYP2A7) 1551(CYP3A7) 1553(CYP2A13) 1555(CYP2B6)
1557(CYP2C19) 1558(CYP2C8) 1559(CYP2C9) 1562(CYP2C18)
1565(CYP2D6) 1571(CYP2E1) 1572(CYP2F1) 1573(CYP2J2)
1576(CYP3A4) 1577(CYP3A5) 1580(CYP4B1) 1588(CYP19A1)
199974(CYP4Z1) 260293(CYP4X1) 29785(CYP2S1) 64816(CYP3A43)
PTR: 450857 450909(CYP2C8) 453433(CYP19A1) 453744 456557 456833
456896 459163 463582(CYP3A4) 470228(CYP2D6) 472456(CYP3A43)
735881 737263(CYP3A67) 737374(CYP3A5) 738823 738883 740956
MCC: 678670(CYP3A64) 678683(CYP2C8) 678686(CYP2C75) 678687(CYP2B6)
678688(CYP2E1) 678690(CYP2A23) 678691(CYP2D6) 678692(CYP3A5)
678694(CYP1A1) 678696(CYP2F6) 678697 693631 705753 705884
709290 709535 709770(CYP3A43) 710385
MMU: 100066(Cyp2j11) 107141(Cyp2c50) 13075(Cyp19a1) 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)
13106(Cyp2e1) 13107(Cyp2f2) 13109(Cyp2j5) 13110(Cyp2j6)
13112(Cyp3a11) 13113(Cyp3a13) 13114(Cyp3a16) 13120(Cyp4b1)
226105(Cyp2c70) 226143(Cyp2c44) 230459(Cyp2j13) 337924(Cyp3a44)
404195(Cyp2c54) 433247(Cyp2c68) 53973(Cyp3a41a) 546837(Cyp2j7)
56388(Cyp3a25) 56448(Cyp2d22) 665095(Cyp2j8) 69888(Cyp2c66)
72082(Cyp2c55) 72303(Cyp2c65) 74134(Cyp2s1) 74519(Cyp2j9)
76279(Cyp2d26) 81906(Cyp4x1)
RNO: 171352(Cyp3a9) 171518(Cyp2c22) 171521(Cyp2c13) 171522(Cyp2d4v1)
24296(Cyp1a1) 24297(Cyp1a2) 24299(Cyp2a3a) 24300(Cyp2b1)
24303(Cyp2d3) 24307(Cyp4b1) 246070(Cyp2c6) 246767(Cyp4x1)
24894(Cyp2a1) 24895(Cyp2a2) 25011(Cyp2c12) 25053(Cyp2d2)
25086(Cyp2e1) 252931(Cyp3a18) 25426(Cyp1b1) 25642(Cyp3a23/3a1)
266682(Cyp3a2) 266684(Cyp2d1) 286953(Cyp2b3) 286963(Cyp2d5)
292728(Cyp2b21) 29277(Cyp2c) 29295(Cyp2b12) 29298(Cyp2c7)
308445(Cyp2s1) 313372(Cyp2j13) 313375(Cyp2j3) 361523(Cyp2b2)
502969(Cyp2j16) 54246(Cyp2f4) 65210(Cyp2j4) 687842
83790(Cyp2c23)
CFA: 415120(CYP2D15) 415123(CYP2C41) 415128(CYP2E1) 415129(CYP3A12)
474177(CYPIIB11) 479740 482505 483038(CYP1B1) 484491
484494(CYP2A13) 494003(CYP19A1) 494010(CYP1A2) 608452 610195
612477
BTA: 281740(CYP19A1) 282211(CYP2D6) 282213(CYP2E1) 282214(CYP3A4)
282870(CYP1A1) 503552(CYP1A2) 504769(CYP2B) 507988(CYP3A4)
511470(CYP1B1) 511498 514971(CYP2S1) 515036 526682(CYP3A5)
530929 535243(CYP2C18) 540149(CYP4B1) 540707 785824(MGC127055)
SSC: 100126281(CYP3A46) 100152910(CYP1A2) 100156640 397687(CYP2D25)
403103(CYP1A1) 403104(CYP2B22) 403107(CYP2C33) 403111(CYP2C42)
403149(CYP2A19) 403215(CYP2C49) 403216(CYP2E1) 403322(CYP3A39)
403324(CYP3A29) 403331(CYP19A1) 403333(CYP19A3)
ECB: 100009712(CYP19A1) 100051552 100061579 100061609 100062244
100062285(CYP1A1) 100064176 100066422(CYP2E1)
100067064(CYP3A89) 100067084 100067247 100068315 100068603
100070088 100070400 100070895 100146413 100147675
MDO: 100010745 100010783 100010820 100011610 100013114 100013238
100015828 100018790(CYPIIF2) 100018858 100018927 100018994
100023529 100023582 100026598 100026637 100029871 100029908
100031907 100031975 100031980
OAA: 100080942(CYP1A1) 100082218 100082250 100090373 100091970
GGA: 396051(CYP1A1) 414832(CYP3A37) 414833(CYP2C45) 414854(CYP19A1)
416477(CYP3A80) 417981 421466(CYP1B1) 424618(CYP4B1) 424676
428832
TGU: 100217987 100222415 100224220 100226034 100228872 100228937
100230258 100230890 100231862 751777(CYP19A1)
XLA: 100036775 100037189 373656(p450arom-A) 379297(MGC54008)
379479(cyp2d6-b) 398964 432343 432347 444542 446878(cyp2d6-a)
495363
XTR: 100036594(cyp19) 100037911 448236(cyp2c8) 496407(cyp2a13)
496408(cyp2f2) 548436(cyp2d6) 548503 550102(cyp4b1)
DRE: 100034366(cyp2j23) 140634(cyp1a) 30390(cyp19a1a)
393592(cyp2j22) 399485(cyp2j21) 553969(cyp3a65) 60640(cyp19a1b)
797309(cyp2j20)
BFO: BRAFLDRAFT_201702
CIN: 100169892 100182809 100187173
SPU: 576811 578655 581116
DME: Dmel_CG11466(Cyp9f2)
DPO: Dpse_GA15364 Dpse_GA26760
DAN: Dana_GF12366 Dana_GF17048
DER: Dere_GG17131 Dere_GG23366
DPE: Dper_GL10371 Dper_GL27180
DSE: Dsec_GM21045 Dsec_GM26014
DSI: Dsim_GD20572
DYA: Dyak_GE19209 Dyak_GE24523
DGR: Dgri_GH18868 Dgri_GH20129 Dgri_GH20130 Dgri_GH21099
DMO: Dmoj_GI20221 Dmoj_GI20851 Dmoj_GI24725
AGA: AgaP_AGAP012292 AgaP_AGAP012294 AgaP_AGAP012295(CYP9L1)
AgaP_AGAP012296
AAG: AaeL_AAEL002633 AaeL_AAEL002638 AaeL_AAEL006784 AaeL_AAEL006815
AaeL_AAEL014619
CQU: CpipJ_CPIJ005958 CpipJ_CPIJ010542 CpipJ_CPIJ010544
CpipJ_CPIJ012470
AME: 408383 409677(Cyp6as5) 410490 412209
NVI: 100113564 100114023 100118363 100120598 100122423
TCA: 100142582 659054 664280(Cyp9z1) 664290 664295 664302(Cyp9f2)
664469
API: 100164042 100165240
ISC: IscW_ISCW011997
CEL: C49C8.4(cyp-33E1) F42A9.5(cyp-33E2) R08F11.3(cyp-33C8)
Y49C4A.9(cyp-33C11)
CBR: CBG01027 CBG01302
NVE: NEMVE_v1g142057
TAD: TRIADDRAFT_13664 TRIADDRAFT_54215
SBI: SORBI_03g028720(SORBIDRAFT_03g028720)
CRE: CHLREDRAFT_196700(CYP743B3)
SCE: YDR402C(DIT2)
AGO: AGOS_AFR400C
KLA: KLLA0C06743g KLLA0D11638g
DHA: DEHA0C00902g
PIC: PICST_35590(ALK2) PICST_63000(CYP559)
CGR: CAGL0F02607g
NCR: NCU05185
PAN: PODANSg3804 PODANSg5780
MGR: MGG_01925 MGG_10879
FGR: FG01972.1
ANI: AN2706.2 AN6835.2
AFM: AFUA_1G04390 AFUA_3G09220 AFUA_5G02620
AOR: AO090001000445 AO090701000436
ANG: An16g02820
AFV: AFLA_085490 AFLA_127500
PCS: Pc20g04310
NFI: NFIA_067930
SSL: SS1G_11697
BFU: BC1G_05268 BC1G_15490
TET: TTHERM_00101170 TTHERM_00101290 TTHERM_00198200 TTHERM_00198220
TTHERM_00198230 TTHERM_00198340 TTHERM_00200550 TTHERM_00201630
TTHERM_00227020 TTHERM_00313500 TTHERM_00620930 TTHERM_00754700
TTHERM_00754730 TTHERM_00898320 TTHERM_01122780 TTHERM_01250020
TTHERM_01369770 TTHERM_01698320
PCT: PC1_0268
PEN: PSEEN2155
FTU: FTT_0632c
FTF: FTF0632c
RPI: Rpic_4258
RPF: Rpic12D_4368
REH: H16_B0939(cyp) H16_B1009
RME: Rmet_3467
BUR: Bcep18194_B0775 Bcep18194_B1689 Bcep18194_C6803
VAP: Vapar_4796
HOH: Hoch_2584
MLO: mll8468
SME: SMc01812
ATU: Atu1256
ATC: AGR_C_2319
RET: RHE_CH01585(ypch00550)
RLE: RL1686
BJA: blr2882
BRA: BRADO0283
BBT: BBta_0276
RPB: RPB_3645
RPD: RPD_1820
RPE: RPE_0057
AZC: AZC_3520
SIT: TM1040_1816
RSP: RSP_1946
RSQ: Rsph17025_0342
RDE: RD1_2962(cyp)
ELI: ELI_00100
BSU: BSU07250(yetO) BSU27160(cypB)
BAN: BA3221(cypD)
BAR: GBAA3221(cypD)
BAA: BA_3732
BAT: BAS2993
BAH: BAMEG_1392(cypD)
BAI: BAA_3269(cypD)
BCE: BC3211
BCA: BCE_3239(cypD)
BCZ: BCZK2921
BCR: BCAH187_A3250(cypD)
BCB: BCB4264_A3231(cypD)
BCU: BCAH820_3229(cypD)
BCG: BCG9842_B2016(cypD)
BCQ: BCQ_3034(cypD)
BCX: BCA_3251(cypD)
BTK: BT9727_2981
BTL: BALH_2868
BWE: BcerKBAB4_2936
BLI: BL02398(cypE)
BLD: BLi02848(yrhJ)
BAY: RBAM_007390(yetO) RBAM_024260(yrhJ)
BPU: BPUM_1680(yrhJ)
GYM: GYMC10_2763
SCO: SCO3636(SCH10.14c)
SMA: SAV_4539(cyp20) SAV_575(cyp2)
NCA: Noca_3536
SRO: Sros_6421
FAL: FRAAL1514 FRAAL5644
NML: Namu_2612 Namu_5109
SEN: SACE_0125(cyp20) SACE_2802 SACE_4144 SACE_4205(cypD)
SACE_5309(cyp20)
AVA: Ava_1981 Ava_2103 Ava_3921 Ava_4063
HAU: Haur_2522
DGE: Dgeo_0944
HMA: rrnAC0073(cyc) rrnAC3312(cyp1)
HWA: HQ3721A(cyc)
NPH: NP2540A(cyc)
PTO: PTO0085 PTO1399
 |
|---|
| Structures |
PDB: 1BU7 1BVY 1DT6 1FAG 1FAH 1JME 1JPZ 1N6B 1NR6 1OG2
1OG5 1P0V 1P0W 1P0X 1PO5 1PQ2 1R9O 1SMI 1SMJ 1SUO
1TQN 1W0E 1W0F 1W0G 1YQO 1YQP 1Z10 1Z11 1ZO4 1ZO9
1ZOA 2BDM 2BMH 2F9Q 2FDU 2FDV 2FDW 2FDY 2HI4 2HPD
2IJ2 2IJ3 2IJ4 2J0D 2J1M 2J4S 2NNB 2NNH 2NNI 2NNJ
2P85 2PG5 2PG6 2PG7 2Q6N 2RFB 2RFC 2UWH 2V0M 2VN0
2ZBX 2ZBY 2ZBZ 3B4X 3BEN 3CBD 3CV8 3CV9 3DGI 3E4E
3E6I 3EBS 3EKB 3EKD 3EKF 3EQM 3G5N 3G93 3HF2 3IBD |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:13426111]
BOOTH J, BOYLAND E.
The biochemistry of aromatic amines. III. Enzymic hydroxylation by
rat-liver microsomes.
Biochem. J. 66 (1957) 73-8.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:5132997]
Fujita T, Mannering GJ.
Differences in soluble P-450 hemoproteins from livers of rats
treated with phenobarbital and 3-methylcholanthrene.
Chem. Biol. Interact. 3 (1971) 264-5.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:187601]
Haugen DA, Coon MJ.
Properties of electrophoretically homogeneous
phenobarbital-inducible and beta-naphthoflavone-inducible forms of
liver microsomal cytochrome P-450.
J. Biol. Chem. 251 (1976) 7929-39.
Oryctolagus cuniculus |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:3415241]
Imaoka S, Inoue K, Funae Y.
Aminopyrine metabolism by multiple forms of cytochrome P-450 from
rat liver microsomes: simultaneous quantitation of four aminopyrine
metabolites by high-performance liquid chromatography.
Arch. Biochem. Biophys. 265 (1988) 159-70.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [PMID:434823]
Johnson EF, Zounes MC, Muller-Eberhard U.
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.
Arch. Biochem. Biophys. 192 (1979) 282-9.
Oryctolagus cuniculus |
|---|
Reference
Authors
Title
Journal
Organism
|
6 [PMID:489601]
Kupfer D, Miranda GK, Navarro J, Piccolo DE, Theoharides AD.
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.
J. Biol. Chem. 254 (1979) 10405-14.
Cavia porcellus |
|---|
Reference
Authors
Title
Journal
Organism
|
7 [PMID:7298645]
Lang MA, Gielen JE, Nebert DW.
Genetic evidence for many unique liver microsomal P-450-mediated
monooxygenase activities in heterogeneic stock mice.
J. Biol. Chem. 256 (1981) 12068-75.
Mus musculus [GN:mmu] |
|---|
Reference
Authors
Title
Journal
Organism
|
8 [PMID:7298644]
Lang MA, Nebert DW.
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.
J. Biol. Chem. 256 (1981) 12058-67.
Mus musculus [GN:mmu] |
|---|
Reference
Authors
Title
Journal
Organism
|
9 [PMID:2916844]
Leo MA, Lasker JM, Raucy JL, Kim CI, Black M, Lieber CS.
Metabolism of retinol and retinoic acid by human liver cytochrome
P450IIC8.
Arch. Biochem. Biophys. 269 (1989) 305-12.
Homo sapiens [GN:hsa] |
|---|
Reference
Authors
Title
Journal
Organism
|
10 [PMID:4401153]
Lu AY, Kuntzman R, West S, Jacobson M, Conney AH.
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.
J. Biol. Chem. 247 (1972) 1727-34.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
11 [PMID:13314626]
MITOMA C, POSNER HS, REITZ HC, UDENFRIEND S.
Enzymatic hydroxylation of aromatic compounds.
Arch. Biochem. Biophys. 61 (1956) 431-41.
Oryctolagus cuniculus |
|---|
Reference
Authors
Title
Journal
|
12
Mitoma, C. and Udenfriend, S.
Aryl-4-hydroxylase.
Methods Enzymol. 5 (1962) 816-819. |
|---|
Reference
Authors
Title
Journal
Organism
|
13 [PMID:7295706]
Napoli JL, Okita RT, Masters BS, Horst RL.
Identification of 25,26-dihydroxyvitamin D3 as a rat renal
25-hydroxyvitamin D3 metabolite.
Biochemistry. 20 (1981) 5865-71.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
14 [PMID:4387094]
Nebert DW, Gelboin HV.
Substrate-inducible microsomal aryl hydroxylase in mammalian cell
culture. I. Assay and properties of induced enzyme.
J. Biol. Chem. 243 (1968) 6242-9.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
15 [PMID:3264134]
Suhara K, Ohashi K, Takahashi K, Katagiri M.
Aromatase and nonaromatizing 10-demethylase activity of adrenal
cortex mitochondrial P-450(11)beta.
Arch. Biochem. Biophys. 267 (1988) 31-7.
Homo sapiens [GN:hsa], Bos taurus [GN:bta] |
|---|
Reference
Authors
Title
Journal
Organism
|
16 [PMID:7462235]
Theoharides AD, Kupfer D.
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.
J. Biol. Chem. 256 (1981) 2168-75.
Oryctolagus cuniculus |
|---|
Reference
Authors
Title
Journal
Organism
|
17 [PMID:825720]
Thomas PE, Lu AY, Ryan D, West SB, Kawalek J, Levin W.
Immunochemical evidence for six forms of rat liver cytochrome P450
obtained using antibodies against purified rat liver cytochromes
P450 and P448.
Mol. Pharmacol. 12 (1976) 746-58.
Rattus norvegicus [GN:rno] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.14.14.1
IUBMB Enzyme Nomenclature: 1.14.14.1
ExPASy - ENZYME nomenclature database: 1.14.14.1
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.14.1
BRENDA, the Enzyme Database: 1.14.14.1
CAS: 9038-14-6 |
|---|
