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 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
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) 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
Show
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
Taxonomy
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
KEGG   ENZYME: 1.14.15.3Help
Entry
EC 1.14.15.3                Enzyme                                 
Name alkane 1-monooxygenase;
alkane 1-hydroxylase;
omega-hydroxylase;
fatty acid omega-hydroxylase;
alkane monooxygenase;
1-hydroxylase;
alkane hydroxylase
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 iron-sulfur protein as one donor, and incorporation of
one atom of oxygen into the other donor
BRITE hierarchy
Sysname alkane,reduced-rubredoxin:oxygen 1-oxidoreductase
Reaction(IUBMB) octane + reduced rubredoxin + O2 = 1-octanol + oxidized rubredoxin +
H2O [RN:R02879]
Reaction(KEGG) R02879;
(other) R01347 R01348 R02281 R07041
Show
Substrate octane [CPD:C01387];
reduced rubredoxin [CPD:C00340];
O2 [CPD:C00007]
Product 1-octanol [CPD:C00756];
oxidized rubredoxin [CPD:C00435];
H2O [CPD:C00001]
Cofactor Heme [CPD:C00032]
Comment Some enzymes in this group are heme-thiolate proteins (P-450). Also
hydroxylates fatty acids in the omega-position.
Pathway PATH: ec00071  Fatty acid metabolism
PATH: ec00590  Arachidonic acid metabolism
PATH: ec00830  Retinol metabolism
PATH: ec01100  Metabolic pathways
Orthology KO: K00496  alkane 1-monooxygenase
KO: K07425  cytochrome P450, family 4, subfamily A
Genes HSA: 1579(CYP4A11) 284541(CYP4A22)
PTR: 456835 739864
MCC: 709461
MMU: 100040843(Cyp4a32) 100044218 13117(Cyp4a10) 13118(Cyp4a12b)
     13119(Cyp4a14) 230639(Cyp4a29) 277753(Cyp4a12a)
     435802(Cyp4a30b) 546842(Gm12836) 640109 666168(Cyp4a31) 674298
RNO: 170544(Cyp4a1) 24306(Cyp4a2) 266674(Cyp4a8) 298423(Cyp4a3)
     50549(Cyp4a10)
CFA: 475366(CYP4A38) 482506(CYP4A37) 610362 610385(CYP4A11)
BTA: 511890(CYP4A11) 516085(CYP4A22)
SSC: 403326(CYP4A24) 403327(CYP4A21)
ECB: 100064020
MDO: 100023663
OAA: 100092213
PAE: PA1525(alkB2) PA2574(alkB1)
PAU: PA14_30810(alkB1) PA14_44700(alkB2)
PAP: PSPA7_2642 PSPA7_3808
PAG: PLES_27201(alkB1) PLES_38031(alkB2)
PFL: PFL_2935(alkB)
PFS: PFLU3535
PMY: Pmen_0443 Pmen_2750
PRW: PsycPRwf_2053
ACI: ACIAD1411(alkM)
ACB: A1S_1641
ABM: ABSDF1860(alkM)
ABY: ABAYE2014(alkM)
ABC: ACICU_01666
ABN: AB57_1863
ABB: ABBFA_001858
MAQ: Maqu_0440 Maqu_0610 Maqu_2843
LPN: lpg2997
LPF: lpl2925
LPP: lpp3068
LPC: LPC_3312
HCH: HCH_04734(alkB)
ABO: ABO_0122(alkB2) ABO_2707(alkB1)
RPI: Rpic_4109
RPF: Rpic12D_4221
BMA: BMA0635(alkB)
BMV: BMASAVP1_A2377(alkB)
BML: BMA10229_A2910(alkB)
BMN: BMA10247_1692(alkB)
BPS: BPSL2350
BPM: BURPS1710b_2801
BPL: BURPS1106A_2735(alkB)
BPD: BURPS668_2678(alkB)
BPR: GBP346_A2857
BTE: BTH_I1814
BVI: Bcep1808_0897
BUR: Bcep18194_A4085 Bcep18194_B1222
BCN: Bcen_0501
BCH: Bcen2424_0980
BCM: Bcenmc03_0941
BCJ: BCAL3029
BAM: Bamb_0841
BAC: BamMC406_0853
BMU: Bmul_2418
BMJ: BMULJ_00816(alkB)
BXE: Bxe_B1208
BPY: Bphyt_5401
BGL: bglu_1g25240
MPT: Mpe_B0606(alkB)
BBA: Bd2197
CAK: Caul_5439
SIT: TM1040_2646
RSP: RSP_1467
RSH: Rsph17029_0118
RSQ: Rsph17025_0065
RSK: RSKD131_2858
JAN: Jann_0394
PDE: Pden_2098
DSH: Dshi_0027(alkB1)
ACR: Acry_1262
RCE: RC1_0393(alkB)
MTU: Rv3252c(alkB)
MTC: MT3350(alkB)
MRA: MRA_3293(alkB)
MTF: TBFG_13281
MTB: TBMG_03300(TBMG_03300.1)
MBO: Mb3280c(alkB)
MBB: BCG_3281c(alkB)
MBT: JTY_3277(alkB)
MPA: MAP3364c
MAV: MAV_4215
MSM: MSMEG_1839
MUL: MUL_2749(alkB_1)
MVA: Mvan_1742 Mvan_3100
MGI: Mflv_3369 Mflv_4721
MAB: MAB_3598c
MMC: Mmcs_1333
MKM: Mkms_1350
MJL: Mjls_1369
MMI: MMAR_1291(alkB) MMAR_3516(alkB_1)
CJK: jk1916(alkM)
NFA: nfa46140 nfa46180
RHA: RHA1_ro02534(alkB) RHA1_ro02535(rubA)
RER: RER_21620(alkB)
ROP: ROP_22570(alkB)
GBR: Gbro_4212
NCA: Noca_0122
TCU: Tcur_0560
FRA: Francci3_1251
FRE: Franean1_2192
FAL: FRAAL1986
CAI: Caci_1373
Taxonomy
Reference
  Authors
  Title

  Journal
  Organism
 1  [PMID:4317878]
Cardini G, Jurtshuk P.
The enzymatic hydroxylation of n-octane by Corynebacterium sp.
strain 7E1C.
J. Biol. Chem. 245 (1970) 2789-96.
Corynebacterium sp.
Reference
  Authors
  Title

  Journal
  Organism
 2  [PMID:4395379]
McKenna EJ, Coon MJ.
Enzymatic omega-oxidation. IV. Purification and properties of the
omega-hydroxylase of Pseudomonas oleovorans.
J. Biol. Chem. 245 (1970) 3882-9.
Pseudomonas oleovorans
Reference
  Authors
  Title

  Journal
  Organism
 3  [PMID:4294330]
Peterson JA, Kusunose M, Kusunose E, Coon MJ.
Enzymatic omega-oxidation. II. Function of rubredoxin as the
electron carrier in omega-hydroxylation.
J. Biol. Chem. 242 (1967) 4334-40.
Pseudomonas oleovorans
Other DBs ExplorEnz - The Enzyme Database: 1.14.15.3
IUBMB Enzyme Nomenclature: 1.14.15.3
ExPASy - ENZYME nomenclature database: 1.14.15.3
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.15.3
BRENDA, the Enzyme Database: 1.14.15.3
CAS: 9059-16-9
DBGET integrated database retrieval system