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1.14.14.1: unspecific monooxygenase

This is an abbreviated version!
For detailed information about unspecific monooxygenase, go to the full flat file.

Word Map on EC 1.14.14.1

Reaction

RH
+
[reduced NADPH-hemoprotein reductase]
+
O2
=
ROH
+
[oxidized NADPH-hemoprotein reductase]
+
H2O

Synonyms

3AH15, 6 beta-hydroxylase, 6-beta-testosterone hydroxylase, 7-alkoxycoumarin O-dealkylase, 7-ethoxycoumarin-O-deethylase, 7-ethoxyresorufin-O-deethylase, AA omega-hydroxylase, Aldehyde oxygenase, Arachidonic acid epoxygenase, aromatase, aryl hydrocarbon hydroxylase, aryl-4-monooxygenase, BG04_163, BM3, BPH, Brain aromatase, class IV cytochrome P450 monooxygenase, clavine oxidase, CLOA, Clone PF26, Clone PF3/46, Coumarin 7-hydroxylase, CP2D6, Cyp, CYP monooxygenase, CYP102, CYP102 monooxygenase, CYP1027H1, CYP102A1, CYP102A2, CYP102A3, CYP102A7, CYP102B1, CYP106, CYP107, CYP1074A2, CYP109, CYP116B3, CYP116B4, CYP116B46, CYP134, CYP150A20, CYP152, CYP154H1, CYP19, CYP197, CYP1A, CYP1A1, CYP1A2, CYP1A3, CYP1B1, CYP24A1, CYP27A1, CYP28A5, CYP2A3, CYP2A6, CYP2B, CYP2B4, CYP2B6, CYP2C11, CYP2C19, CYP2C8, CYP2C9, CYP2D6, CYP2E1, CYP305A1, CYP3A, CYP3A1, CYP3A4, CYP3A5, CYP3A7, CYP4, CYP4502F4, CYP4A, CYP4A4, CYP4A6, CYP4A7, CYP4AA1, CYP4E2, CYP4F, CYP4F2, CYP4F3A, CYP4F3B, CYP5035A2, CYP5035A3, CYP5035A5, CYP5035C1, CYP5036A1, CYP5036A3, CYP5037B2, CYP505D1, CYP505D2, CYP505D3, CYP505D4, CYP51, CYP512B5, CYP512H1, CYP5136A2, CYP5136A3, CYP5136A5, CYP5139A1, CYP5141A1, CYP5141D1, CYP5142A3, CYP5142C1, CYP5144A3, CYP5144A7, CYP5144A9, CYP5144C7, CYP5144D4, CYP5145A3, CYP5147A1, CYP5150B1, CYP53A15, CYP53C2, CYP53D2, CYP5A1, CYP63A2, CYP6B1, CYP6B1v1, CYP6B1V1/CYP6B1V2/ CYP6B1V3, CYP6B3V1/CYP6B3V2, CYP6B4V1/CYP6B4V2, CYP6B5V1, CYP714D1, CYP82E2, CYP82E3, CYP82E4v1, CYP82E4v2, CYP8A1, CYP9F2, CYPIA1, CYPIA2, CYPIA4, CYPIA5, CYPIB1, CYPIIA1, CYPIIA10, CYPIIA11, CYPIIA12, CYPIIA13, CYPIIA2, CYPIIA3, CYPIIA4, CYPIIA5, CYPIIA6, CYPIIA7, CYPIIA8, CYPIIA9, CYPIIB1, CYPIIB10, CYPIIB11, CYPIIB12, CYPIIB19, CYPIIB2, CYPIIB20, CYPIIB3, CYPIIB4, CYPIIB5, CYPIIB6, CYPIIB9, CYPIIC1, CYPIIC10, CYPIIC11, CYPIIC12, CYPIIC13, CYPIIC14, CYPIIC15, CYPIIC16, CYPIIC17, CYPIIC18, CYPIIC19, CYPIIC2, CYPIIC20, CYPIIC21, CYPIIC22, CYPIIC23, CYPIIC24, CYPIIC25, CYPIIC26, CYPIIC27, CYPIIC28, CYPIIC29, CYPIIC3, CYPIIC30, CYPIIC31, CYPIIC37, CYPIIC38, CYPIIC39, CYPIIC4, CYPIIC40, CYPIIC41, CYPIIC42, CYPIIC5, CYPIIC6, CYPIIC7, CYPIIC8, CYPIIC9, CYPIID1, CYPIID10, CYPIID11, CYPIID14, CYPIID15, CYPIID16, CYPIID17, CYPIID18, CYPIID19, CYPIID2, CYPIID3, CYPIID4, CYPIID5, CYPIID6, CYPIID9, CYPIIE1, CYPIIF1, CYPIIF3, CYPIIF4, CYPIIG1, CYPIIH1, CYPIIH2, CYPIIIA1, CYPIIIA10, CYPIIIA11, CYPIIIA12, CYPIIIA13, CYPIIIA14, CYPIIIA15, CYPIIIA16, CYPIIIA17, CYPIIIA18, CYPIIIA19, CYPIIIA2, CYPIIIA21, CYPIIIA24, CYPIIIA25, CYPIIIA27, CYPIIIA28, CYPIIIA29, CYPIIIA3, CYPIIIA30, CYPIIIA31, CYPIIIA5, CYPIIIA6, CYPIIIA7, CYPIIIA8, CYPIIIA9, CYPIIJ1, CYPIIJ2, CYPIIJ3, CYPIIJ5, CYPIIJ6, CYPIIK1, CYPIIK3, CYPIIK4, CYPIIL1, CYPIIM1, CYPIVA4, CYPIVA8, CYPIVB1, CYPIVC1, CYPIVF1, CYPIVF11, CYPIVF12, CYPIVF4, CYPIVF5, CYPIVF6, CYPIVF8, CYPVIA1, CYPVIB1, CYPVIB2, CYPVIB4, CYPVIB5, CYPVIB6, CYPVIB7, CYPXIX, CYPXIXA1, CYPXIXA2, CYPXIXA3, Cyt P450, cytochrome P-450 4 enzyme, cytochrome P-450 BM3, cytochrome P-450 monooxygenase, cytochrome P450 2B4, cytochrome P450 3A, cytochrome P450 3A4, cytochrome P450 aromatase, cytochrome P450 BM3, cytochrome P450 monooxygenase, cytochrome P450 monooxygenase 116B3, cytochrome P450 monooxygenase 2A6, cytochrome P450 monooxygenase 2C8, cytochrome P450 monooxygenase 2C9, cytochrome P450 monooxygenase 3A4, cytochrome P450 monooxygenase pc-2, cytochrome P450 monooxygenase pc-4, cytochrome P450 monooxygenase pc-5, cytochrome P450 monooxygenase pc-6, cytochrome P450 monooxygenase PC-foxy1, cytochrome P450 oxidoreductase, cytochrome P450 reductase, Cytochrome P450-D2, cytochrome P450-dependent monooxygenase, cytochrome P450-dependent monooxygenase 1A2, cytochrome P450-monooxygenase, cytochrome-P450 hydroxylase, DAH1, DAH2, Debrisoquine 4-hydroxylase, EC 1.14.1.1, EC 1.14.14.2, EC 1.14.99.8, EC 1.99.1.1, ECOD, Ema, EROD, Estrogen synthetase, EUI, fatty acid hydroxylase, flavocytochrome P450BM-3, flavoprotein monooxygenase, flavoprotein-linked monooxygenase, FMO3, FraEuI1c_1415, FraEuI1c_2494, FraEuI1c_5334, GA 16a,17-epoxidase, GA-deactivating enzyme, Hepatic cytochrome P-450MC1, HLp, HMPREF1624_01477, IIA3, Isozyme 3A, Laurate omega-1 hydroxylase, Lauric acid omega-6-hydroxylase, liver cytochrome P450-dependent monooxygenase, LMC1, Mephenytoin 4-hydroxylase, MFO, microsomal monooxygenase, microsomal P-450, mixed function oxygenase, monooxygenase 3, monooxygenase P450 BM-3, More, N-demethylase, nicotine oxidase, O-demethylase, OLF2, Olfactive, Os05g0482400 protein, Ovarian aromatase, oxygenase, flavoprotein-linked mono-, P(3)450, P-448, P-450 PHPAH1, P-450(M-1), P-450-MK2, P-450AROM, P-450IB, P-450IIIAM1, P-450MC, P-450MP, P-450UT, P1-88, P24, P450, P450 17-alpha, P450 19A1, P450 1A1, P450 1A2, P450 1B1, P450 2A6, P450 2B6, P450 2C19, P450 2C9, P450 2D-29/2D-35, P450 2D6, P450 2E1, P450 2J2, P450 3A4, P450 4A11, P450 4F2, P450 BM3, P450 CM3A-10, P450 DUT2, P450 FA, P450 FI, P450 form 3B, P450 form HP1, P450 HSM1, P450 HSM2, P450 HSM3, P450 HSM4, P450 IIB1, P450 IIC2, P450 LM4, P450 LM6, P450 LMC2, P450 MD, P450 monooxygenase, P450 MP-12/MP-20, P450 P49, P450 PB1, P450 PB4, P450 PBC1, P450 PBC2, P450 PBC3, P450 PBC4, P450 PCHP3, P450 PCHP7, P450 TCDDAA, P450 TCDDAHH, P450 type B2, P450 types B0 and B1, P450(I), P450-11A, P450-15-alpha, P450-15-COH, P450-16-alpha, P450-254C, P450-3C, P450-6B/29C, P450-A3, P450-AFB, P450-ALC, P450-BM3, P450-CMF1A, P450-CMF1B, P450-CMF2, P450-CMF3, P450-DB1, P450-DB2, P450-DB3, P450-DB4, P450-DB5, P450-HFLA, P450-HP, P450-IIA10, P450-IIA11, P450-IIA3.1, P450-IIA3.2, P450-IIA4, P450-KP1, P450-LM2, P450-MC1, P450-MC4, P450-MK1, P450-MKJ1, P450-MKMP13, P450-MKNF2, P450-NMB, P450-OLF1, P450-OLF3, P450-P1, P450-P2/P450-P3, P450-P3, P450-PB1 and P450-PB2, P450-PCN1, P450-PCN2, P450-PCN3, P450-PM4, P450-PP1, P450-PROS2, P4501A1, P450arom, P450cam, P450CB, P450CMEF, P450E, P450EF, P450F, P450H, P450I, P450IIC5, P450MT2, P450RAP, P450RLM6, P450s 3A, P450SMO, P52, PB15, PHP2, PHP3, PikC, PikC hydroxylase, Progesterone 21-hydroxylase, Prostaglandin omega-hydroxylase, PTF1, PTF2, S-mephenytoin 4-hydroxylase, Sam5, sertraline N-demethylase, SIAM614_30676, Steroid hormones 7-alpha-hydroxylase, Testosterone 15-alpha-hydroxylase, Testosterone 16-alpha hydroxylase, Testosterone 6-beta-hydroxylase, Testosterone 7-alpha-hydroxylase, xenobiotic monooxygenase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.14.1 unspecific monooxygenase

Engineering

Engineering on EC 1.14.14.1 - unspecific monooxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A74G/F88V
-
substrate specificity similar to wild-type
A74G/F88V/S189Q
-
substrate spectrum much broader than for wild-type
A74G/S189Q
-
substrate specificity similar to wild-type
H226Y
-
site-directed mutagenesis, altered coordination of the Fe2+ ion and binding of inhibitor bifonazole
F116A
no enzymatic activity
F116C
no enzymatic activity
F116H
no enzymatic activity
F116I
no enzymatic activity
F116L
no enzymatic activity
F116L/F484L
no enzymatic activity
F116L/F484Y
no enzymatic activity
F116S
no enzymatic activity
F116V
no enzymatic activity
F116W
some enzymatic activity against bergapten, xanthotoxin
F116Y
reduced enzymatic activity
F116Y/F484H
no enzymatic activity
F116Y/F484Y
no enzymatic activity
F206L
no enzymatic activity
F484C
no enzymatic activity
F484D
no enzymatic activity
F484H
no enzymatic activity
F484L
no enzymatic activity
F484S
no enzymatic activity
F484V
no enzymatic activity
F484W
no enzymatic activity
F484Y
no enzymatic activity
H117A
no enzymatic activity
H117F
no enzymatic activity
H117L/F484Y
no enzymatic activity
H117V
no enzymatic activity
H117Y
no enzymatic activity
H204L
activity similar to wild-type
V368A
V368F
no enzymatic activity
V368L
W129A/L324G
-
the mutant shows complete loss of activity toward pyrene and retains partial oxidation activity (32%) toward phenanthrene
W129F/L324F
-
the mutant shows complete loss of activity toward both phenanthrene and pyrene
W129F/L324G
-
the mutant shows complete loss of activity toward pyrene and retains partial oxidation activity (15%) toward phenanthrene
W129L/L324F
-
the mutant shows greater oxidation of phenanthrene and pyrene compared with the wild type enzyme
W129L/L324G
-
the mutant shows complete loss of activity toward both phenanthrene and pyrene
A328F
site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
A328K
site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
A328R
site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
A328Y
site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
A74E/F87V/P386S
-
site-directed mutagenesis, the mutant shows altered regioselectivity and activity, and cofactor specificity compared to the wild-type mutant
A74G/F87G/L188Q
site-directed mutagenesis. The introduction of a smaller amino acid at position 87 results in a more active monooxygenase and a different product profile for the oxidation of substrate (-)-alpha-pinene.
A74G/F87V/L188Q
A74G/F87V/L188Q/R966D
-
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
A74G/F87V/L188Q/R966M
-
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
A74G/F87V/L188Q/S965D
-
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
A74G/F87V/L188Q/W1046A
-
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
A74G/F87V/L188Q/W1046S
-
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
A74G/L188Q
site-directed mutagenesis. MD simulations of the double mutant A74G L188Q (GQ) show that the substrate is blocked from accessing the heme oxygen by the side chain of the F87, when it adopts the conformation found in the X-ray structure.
F87A
site-directed mutagenesis, the mutant exhibits an altered regioselectivity and substrate specificity compared with wild-type, it has lower tolerance toward DMSO
F87G
-
site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant
F87GA
-
site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant
R47E
-
the mutant enzyme retains significant hydroxylase activity towards saturated fatty acids and shows much increased activity towards C12-C16 alkyl trimethylammonium compounds
R47S/Y51W/ I401M
use for electrochemical conversion of p-xylene to 2,5-dimethylphenol
A328F
-
site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
-
A328K
-
site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
-
A328R
-
site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
-
A328Y
-
site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme
-
R47S/Y51W/ I401M
-
use for electrochemical conversion of p-xylene to 2,5-dimethylphenol
-
A86T/T91S/A109F/I179F/I267L
-
site-specific mutagenesis, mutant 70A08 shows 150fold increased dealkylation activity compared to the wild-type enzyme
T91S/A109L/I179F/I267L
-
site-specific mutagenesis, mutant 74H10 shows 240fold increased dealkylation activity compared to the wild-type enzyme
E723A
residue located between [2Fe-2S] cluster and heme, about 15% of wild-type activity
E729A
residue located between [2Fe-2S] cluster and heme, no activity detecable
F378A
residue located between [2Fe-2S] cluster and heme, no activity detecable
Q725A
residue located between [2Fe-2S] cluster and heme, about 100% of wild-type activity
R388A
residue located between [2Fe-2S] cluster and heme, no activity detecable
R392A
residue located between [2Fe-2S] cluster and heme, about 110% of wild-type activity
R718A
residue located between [2Fe-2S] cluster and heme, no activity detecable
S726A
residue located between [2Fe-2S] cluster and heme, about 30% of wild-type activity
additional information