| Entry |
|
|---|
| 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
 |
|---|
| 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
 |
|---|
| 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
 |
|---|
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 |
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