Information on EC 1.14.13.69 - alkene monooxygenase

Information on EC 1.14.13.69 - alkene monooxygenase:

Please wait a moment until all data are loaded. This message will disappear when all data are loaded.

EC NUMBER	COMMENTARY
1.14.13.69	-

RECOMMENDED NAME	GeneOntology No.
alkene monooxygenase	GO:0018645

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
propene + NADH + H+ + O2 = 1,2-epoxypropane + NAD+ + H2O		-	-	-	-

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
epoxidation	-	-	-	-
oxidation	-	-	-	-
redox reaction	-	-	-	-
reduction	-	-	-	-

PATHWAY	KEGG Link	MetaCyc Link
Chloroalkane and chloroalkene degradation	00625	-
Metabolic pathways	01100	-
Microbial metabolism in diverse environments	01120	-
propylene degradation	-	PWY-5534

SYSTEMATIC NAME

IUBMB Comments

alkene,NADH:oxygen oxidoreductase

The enzyme from Xanthobacter sp. strain Py2 is a multicomponent enzyme comprising (1) an NADH reductase, which provides the reductant for O2 activation; (2) a Rieske-type ferredoxin, which is an electron-transfer protein; (3) an oxygenase, which contains the catalytic centre for alkene epoxidation and (4) a small protein of unknown function that is essential for activity. Requires Fe(II). The enzyme oxygenates C2 to C6 aliphatic alkenes. With 1,2-epoxypropane as substrate, the stereospecifity of the epoxypropane formed is 95% (R) and 5% (S).

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
AkMO	Nocardioides sp., Nocardioides sp. C190, Nocardioides sp. CF8, Nocardioides sp. CT16, Nocardioides sp. J-326TK, Nocardioides sp. KP7, Nocardioides sp. strain JS614	-	-	677851
alkene epoxygenase	-	-	-	-
alkene monooxygenase	Trametes hirsuta, Trametes hirsuta 72, Trametes hirsuta lg-9, Trametes hirsuta MB 50, Trametes hirsuta MTCC 136	-	-	698495
alkene monooxygenase	Nocardioides sp. JS614	-	-	703485
AMO	-	-	-	-
AMO	Rhodococcus rhodochrous	-	-	674944
propene monooxygenase	-	-	-	-
XAMO	Xanthobacter autotrophicus	O87082	-	671530
EtnC	Nocardioides sp. JS614	-	-	703485
additional information	Xanthobacter autotrophicus	-	part of a multicomponent enzyme complex	658775
additional information	Xanthobacter autotrophicus	O87082	AMOs are members of the non-heme diiron monooxygenase family of enzymes	671530

CAS REGISTRY NUMBER	COMMENTARY
63439-50-9	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Gordonia rubripertincta	B-276	285337	-	-
Gordonia rubripertincta	B-276; enzyme is encoded by the linear plasmid pNC30; i.e. Nocardia corallina	285338	-	-
Gordonia rubripertincta	B-276; multi-component enzyme	285335	-	-
Gordonia rubripertincta B-276	B-276	285335, 285337, 285338	-	-
Mycobacterium aurum	L1; multi-component enzyme	285340	-	-
Mycobacterium aurum L1	L1	285340	-	-
Mycobacterium sp.	E20; E3	285334	-	-
Mycobacterium sp.	E3; multi-component enzyme	285340	-	-
Mycobacterium sp. E20	E20	285334	-	-
Mycobacterium sp. E3	E3	285334, 285340	-	-
Nocardioides sp.	gene etnC encoding the alpha-subunit	710973	-	-
Nocardioides sp.	strain JS614, ATCC BAA-499, gene etnC	677851	-	-
Nocardioides sp. JS614	-	703485	-	-
Rhodococcus rhodochrous	strain B-276	674944	-	-
Rhodococcus rhodochrous	strain B-276, formerly Nocardia corallina, high expression of enzyme when grown with propene as sole carbon and energy source	658683	-	-
Rhodococcus rhodochrous B-276	strain B-276	674944	-	-
Rhodococcus rhodochrous B-276	strain B-276, formerly Nocardia corallina, high expression of enzyme when grown with propene as sole carbon and energy source	658683	-	-
Rhodococcus ruber	P-IV-B-11 and P-V-B-171	285338	-	-
Trametes hirsuta	-	698495	-	-
Xanthobacter autotrophicus	gene xamoA, oxygenase alpha subunit; strain Py2, gene xamoA	671530	O87082	SwissProt
Xanthobacter autotrophicus	strain Py2	658775	-	-
Xanthobacter sp.	strain Py2	285336, 285338, 285339, 285341, 285342, 285343	-	-
Xanthobacter sp. Py2	strain Py2	285336, 285338, 285339, 285341, 285342, 285343	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
(R)-styrene oxide + NADH + H+ + O2	?		Xanthobacter autotrophicus	O87082	-	671530	-	-	?
(s)-styrene oxid + NADH + H+ + O2	?		Xanthobacter autotrophicus	O87082	-	671530	-	-	?
2-cresol + NADH + H+ + O2	?		Xanthobacter autotrophicus	O87082	-	671530	-	-	?
3-cresol + NADH + H+ + O2	?		Xanthobacter autotrophicus	O87082	-	671530	-	-	?
4-cresol + NADH + H+ + O2	?		Xanthobacter autotrophicus	O87082	-	671530	-	-	?
chloroethene + NADH + H+ + O2	2-chlorooxirane + NAD+ + H2O		Xanthobacter sp.	-	-	285336	-	-	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Rhodococcus rhodochrous	-	-	674944	-	-	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Mycobacterium sp.	-	-	285334	-	285334	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Mycobacterium sp.	-	-	285340	-	285340	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Gordonia rubripertincta	-	-	285335	-	285335	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Gordonia rubripertincta	-	-	285337	-	285337	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Gordonia rubripertincta, Rhodococcus ruber	-	-	285338	-	285338	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp.	-	-	285336	-	285336	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp.	-	-	285338	-	285338	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp.	-	-	285339	-	285339	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp.	-	-	285341	-	285341	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp.	-	-	285342	-	285342	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp.	-	-	285343	-	285343	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Mycobacterium aurum	-	-	285340	-	285340	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Gordonia rubripertincta	-	constitutive enzyme	285337	-	-	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp.	-	induction by propylene and propylene oxide and a variety of aliphatic and chlorinated alkenes and epoxides	285336	-	-	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp.	-	the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources	285342	-	-	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Rhodococcus ruber aerobic, Rhodococcus ruber TH, Rhodococcus ruber CGMCC3090	-	-	285338	-	285338	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp. TM1	-	-	285336	-	285336	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp. TM1	-	-	285338	-	285338	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp. TM1	-	-	285339	-	285339	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp. TM1	-	-	285341	-	285341	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Rhodococcus ruber DSM44541, Rhodococcus ruber CCTCC M 206040	-	-	285338	-	285338	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Mycobacterium aurum L1	-	-	285340	-	285340	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp. Py2	-	-	285336	-	285336	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp. Py2	-	-	285338	-	285338	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp. Py2	-	-	285339	-	285339	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp. Py2	-	-	285341	-	285341	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp. 124X	-	-	285336	-	285336	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp. 124X	-	-	285338	-	285338	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp. 124X	-	-	285339	-	285339	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp. 124X	-	-	285341	-	285341	?
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Rhodococcus ruber N75, Rhodococcus ruber DSM 44541, Rhodococcus ruber P25	-	-	285338	-	285338	?
propene + NADH + O2	1,2-epoxypropane + NAD+ + H2O		Rhodococcus rhodochrous	-	-	658683	-	-	?
propene + NADH + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter autotrophicus	-	-	658775	-	-	?
propene + NADH + O2	1,2-epoxypropane + NAD+ + H2O		Rhodococcus rhodochrous	-	enables the growth on propene as sole carbon and energy source	658683	-	-	?
toluene + NADH + H+ + O2	?		Xanthobacter autotrophicus	O87082	-	671530	-	-	?
trans-1,2-dichloroethylene + NADH + H+ + O2	2,3-dichlorooxirane + NAD+ + H2O		Xanthobacter sp.	-	-	285336	-	-	?
trichloroethylene + NADH + H+ + O2	2,2,3-trichlorooxirane + NAD+ + H2O		Gordonia rubripertincta	-	-	285338	-	-	?
trichloroethylene + NADH + H+ + O2	2,2,3-trichlorooxirane + NAD+ + H2O		Xanthobacter sp.	-	-	285336, 285338	-	-	?
vinyl chloride + NADH + H+ + O2	?		Nocardioides sp.	-	-	677851	-	-	?
ethene + NADH + H+ + O2	?		Nocardioides sp.	-	-	677851	-	-	?
additional information	?	-	Xanthobacter autotrophicus	O87082	the enzyme catalyses the asymmetric epoxidation of a broad range of alkenes, stereo- and regioselectivity, residues Asn34 and Arg57 are involved, AMO requires a small catalytic coupling/effector protein, AamD, substitution of AamD with IsoD, the coupling protein from the closely related isoprene monooxygenase, changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling, overview	671530	-	-	-
additional information	?	-	Rhodococcus rhodochrous	-	the enzyme is a three-component system encoded by the 4-gene operon amoABCD, which catalyzes the stereoselective epoxidation of aliphatic alkenes yielding primarily the R enantiomer	674944	-	-	-
additional information	?	-	Nocardioides sp.	-	alkene monooxygenase and epoxyalkane:coenzyme M transferase are the initial enzymes of vinyl chloride and ethene biodegradation in strain JS614	677851	-	-	-
additional information	?	-	Trametes hirsuta	-	alternative alkene cleavage mechanism by incorporating 2 oxygen atoms of different oxygen molecules	698495	-	-	-
additional information	?	-	Nocardioides sp.	-	ethene and propene are transformed by ethene-grown and propene-grown/EtO-induced JS614 to ethene oxide and propene oxide, respectively	710973	-	-	-
additional information	?	-	Trametes hirsuta MTCC 136, Trametes hirsuta lg-9, Trametes hirsuta MB 50, Trametes hirsuta 72	-	alternative alkene cleavage mechanism by incorporating 2 oxygen atoms of different oxygen molecules	698495	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Gordonia rubripertincta	-	constitutive enzyme	285337	-	-
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp.	-	induction by propylene and propylene oxide and a variety of aliphatic and chlorinated alkenes and epoxides	285336	-	-
propene + NADH + H+ + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter sp.	-	the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources	285342	-	-
propene + NADH + O2	1,2-epoxypropane + NAD+ + H2O		Xanthobacter autotrophicus	-	-	658775	-	-
propene + NADH + O2	1,2-epoxypropane + NAD+ + H2O		Rhodococcus rhodochrous	-	enables the growth on propene as sole carbon and energy source	658683	-	-
vinyl chloride + NADH + H+ + O2	?		Nocardioides sp.	-	-	677851	-	-
ethene + NADH + H+ + O2	?		Nocardioides sp.	-	-	677851	-	-
additional information	?	-	Nocardioides sp.	-	alkene monooxygenase and epoxyalkane:coenzyme M transferase are the initial enzymes of vinyl chloride and ethene biodegradation in strain JS614	677851	-	-
additional information	?	-	Trametes hirsuta	-	alternative alkene cleavage mechanism by incorporating 2 oxygen atoms of different oxygen molecules	698495	-	-
additional information	?	-	Nocardioides sp.	-	ethene and propene are transformed by ethene-grown and propene-grown/EtO-induced JS614 to ethene oxide and propene oxide, respectively	710973	-	-
additional information	?	-	Trametes hirsuta MTCC 136, Trametes hirsuta lg-9, Trametes hirsuta MB 50, Trametes hirsuta 72	-	alternative alkene cleavage mechanism by incorporating 2 oxygen atoms of different oxygen molecules	698495	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
FAD	Gordonia rubripertincta, Gordonia rubripertincta 11, Gordonia rubripertincta B 276, Gordonia rubripertincta B-276, Gordonia rubripertincta N657	-	the reductase component contains two prosthetic groups, an FAD centre and a [2Fe-2S] cluster. The FAD moiety is reduced by bound NADH in a two-electron reaction. The electrons are then transported to the [2Fe-2S] centre one at a time, which reduces the di-iron centre of the epoxydase. Reduction of the di-iron centre is required for oxygen binding and substrate oxidation	285335	2D-image
NADH	Xanthobacter autotrophicus 7C, Xanthobacter autotrophicus GJ10	-	-	658775	2D-image
NADH	Xanthobacter autotrophicus	-	-	658775, 671530	2D-image
NADH	Rhodococcus rhodochrous, Rhodococcus rhodochrous 172, Rhodococcus rhodochrous 89, Rhodococcus rhodochrous ATCC 33278, Rhodococcus rhodochrous ATCC 39484, Rhodococcus rhodochrous B-276, Rhodococcus rhodochrous B276, Rhodococcus rhodochrous CECT3042, Rhodococcus rhodochrous CTM, Rhodococcus rhodochrous IFO 15564, Rhodococcus rhodochrous J1, Rhodococcus rhodochrous K22, Rhodococcus rhodochrous KCTC 1061, Rhodococcus rhodochrous MTCC-291, Rhodococcus rhodochrous N5, Rhodococcus rhodochrous N75, Rhodococcus rhodochrous NCIMB 11216, Rhodococcus rhodochrous NCIMB 13064, Rhodococcus rhodochrous NCIMB13064, Rhodococcus rhodochrous NCIMB 13259, Rhodococcus rhodochrous PA-34, Rhodococcus rhodochrous PNKb1, Rhodococcus rhodochrous tg1-A6	-	-	658683, 674944	2D-image
NADH	Nocardioides sp., Nocardioides sp. C190, Nocardioides sp. CF8, Nocardioides sp. CT16, Nocardioides sp. J-326TK, Nocardioides sp. KP7, Nocardioides sp. strain JS614	-	-	677851	2D-image
FAD	Xanthobacter sp., Xanthobacter sp. 124X, Xanthobacter sp. Py2, Xanthobacter sp. TM1	-	the 35500 Da NADH reductase component contains 1 mol of FAD	285342	2D-image
additional information	Xanthobacter autotrophicus	O87082	the enzyme contains a Rieske-type ferredoxin. AMO requires a small catalytic coupling/effector protein, AamD, the coupling protein cannot or very poorly be substituted by coupling proteins of AMOs of other species, e.g. IsoD from Rhodococcus sp. strain AD45, or PmoB from Mycobacterium sp. strain M156, substitution with IsoD changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling, overview	671530	-

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Iron	Gordonia rubripertincta, Gordonia rubripertincta 11, Gordonia rubripertincta B 276, Gordonia rubripertincta B-276, Gordonia rubripertincta N657	-	the reductase component contains two prosthetic groups, an FAD centre and a [2Fe-2S] cluster. The FAD moiety is reduced by bound NADH in a two-electron reaction. The electrons are then transported to the [2Fe-2S] centre one at a time, which reduces the di-iron centre of the epoxydase. Reduction of the di-iron centre is required for oxygen binding and substrate oxidation	285335
Iron	Gordonia rubripertincta, Gordonia rubripertincta 11, Gordonia rubripertincta B 276, Gordonia rubripertincta B-276, Gordonia rubripertincta N657	-	enzyme contains a bridged dinuclear iron centre	285337
Iron	Xanthobacter sp., Xanthobacter sp. 124X, Xanthobacter sp. Py2, Xanthobacter sp. TM1	-	alpha-helical structure that surrounds the binuclear iron binding site	285339
Iron	Xanthobacter sp., Xanthobacter sp. 124X, Xanthobacter sp. Py2, Xanthobacter sp. TM1	-	enzyme contains 4 components: 1. a monomeric 35500 Da NADH reductase containing 1 mol of FAD and a probable 2Fe-2S center, 2. a 13300 Da ferredoxin containing a Rieske-type 2Fe-2S cluster, 3. a 11000 Da monomeric protein that contains no detectable cofactors, 4. a 212000 Da alpha2beta2gamma2 multimeric protein containing 4 atoms of nonheme iron. The physiological electron acceptor for the reductase is the Rieske-type ferredoxin, which is proposed to be an intermediate electron carrier between the reductase and terminal catalytic component of the system	285342
Iron	Rhodococcus rhodochrous, Rhodococcus rhodochrous 172, Rhodococcus rhodochrous 89, Rhodococcus rhodochrous ATCC 33278, Rhodococcus rhodochrous ATCC 39484, Rhodococcus rhodochrous B-276, Rhodococcus rhodochrous B276, Rhodococcus rhodochrous CECT3042, Rhodococcus rhodochrous CTM, Rhodococcus rhodochrous IFO 15564, Rhodococcus rhodochrous J1, Rhodococcus rhodochrous K22, Rhodococcus rhodochrous KCTC 1061, Rhodococcus rhodochrous MTCC-291, Rhodococcus rhodochrous N5, Rhodococcus rhodochrous N75, Rhodococcus rhodochrous NCIMB 11216, Rhodococcus rhodochrous NCIMB 13064, Rhodococcus rhodochrous NCIMB13064, Rhodococcus rhodochrous NCIMB 13259, Rhodococcus rhodochrous PA-34, Rhodococcus rhodochrous PNKb1, Rhodococcus rhodochrous tg1-A6	-	binuclear non-heme iron center	658683
Iron	Xanthobacter autotrophicus, Xanthobacter autotrophicus 7C, Xanthobacter autotrophicus GJ10	-	non-haem iron	658775
Iron	Xanthobacter autotrophicus	O87082	the enzyme is a non-heme diiron monooxygenase and contains a Rieske-type ferredoxin	671530
Iron	Rhodococcus rhodochrous, Rhodococcus rhodochrous 172, Rhodococcus rhodochrous 89, Rhodococcus rhodochrous ATCC 33278, Rhodococcus rhodochrous ATCC 39484, Rhodococcus rhodochrous B-276, Rhodococcus rhodochrous B276, Rhodococcus rhodochrous CECT3042, Rhodococcus rhodochrous CTM, Rhodococcus rhodochrous IFO 15564, Rhodococcus rhodochrous J1, Rhodococcus rhodochrous K22, Rhodococcus rhodochrous KCTC 1061, Rhodococcus rhodochrous MTCC-291, Rhodococcus rhodochrous N5, Rhodococcus rhodochrous N75, Rhodococcus rhodochrous NCIMB 11216, Rhodococcus rhodochrous NCIMB 13064, Rhodococcus rhodochrous NCIMB13064, Rhodococcus rhodochrous NCIMB 13259, Rhodococcus rhodochrous PA-34, Rhodococcus rhodochrous PNKb1, Rhodococcus rhodochrous tg1-A6	-	the enzyme possesses a dinuclear iron center within the large subunit of the epoxygenase component, AmoC, mutagenesis of AmoC alters the enantioselectivity of the enzyme	674944
[2Fe-2S]cluster	Gordonia rubripertincta, Gordonia rubripertincta 11, Gordonia rubripertincta B 276, Gordonia rubripertincta B-276, Gordonia rubripertincta N657	-	the reductase component contains two prosthetic groups, an FAD centre and a [2Fe-2S] cluster. The FAD moiety is reduced by bound NADH in a two-electron reaction. The electrons are then transported to the [2Fe-2S] centre one at a time, which reduces the di-iron centre of the epoxydase. Reduction of the di-iron centre is required for oxygen binding and substrate oxidation	285335

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
1,10-phenanthroline	Mycobacterium sp.	-	2 mM, 40% inhibition. Activity is completely restored by 2 mM Fe2+	285340	2D-image
1,2-Epoxypropane	Mycobacterium sp., Mycobacterium sp. 279, Mycobacterium sp. 607, Mycobacterium sp. AC777, Mycobacterium sp. E20, Mycobacterium sp. E3, Mycobacterium sp. HE5, Mycobacterium sp. HXN-1500, Mycobacterium sp. JC1, Mycobacterium sp. JC1 DSM 3803, Mycobacterium sp. JS60, Mycobacterium sp. NwIB-01, Mycobacterium sp. P101, Mycobacterium sp. s4, Mycobacterium sp. Takeo	-	-	285334	2D-image
8-hydroxyquinoline	Mycobacterium sp., Mycobacterium sp. 279, Mycobacterium sp. 607, Mycobacterium sp. AC777, Mycobacterium sp. E20, Mycobacterium sp. E3, Mycobacterium sp. HE5, Mycobacterium sp. HXN-1500, Mycobacterium sp. JC1, Mycobacterium sp. JC1 DSM 3803, Mycobacterium sp. JS60, Mycobacterium sp. NwIB-01, Mycobacterium sp. P101, Mycobacterium sp. s4, Mycobacterium sp. Takeo	-	-	285340	2D-image
Acetylene	Mycobacterium sp., Mycobacterium sp. 279, Mycobacterium sp. 607, Mycobacterium sp. AC777, Mycobacterium sp. E20, Mycobacterium sp. E3, Mycobacterium sp. HE5, Mycobacterium sp. HXN-1500, Mycobacterium sp. JC1, Mycobacterium sp. JC1 DSM 3803, Mycobacterium sp. JS60, Mycobacterium sp. NwIB-01, Mycobacterium sp. P101, Mycobacterium sp. s4, Mycobacterium sp. Takeo	-	-	285340	2D-image
Ethyne	Rhodococcus rhodochrous	-	irreversible inhibition in the presence of NADH, suicide substrate, growth inhibition when added to the culture medium	658683	2D-image
propyne	Gordonia rubripertincta, Gordonia rubripertincta 11, Gordonia rubripertincta B 276, Gordonia rubripertincta B-276, Gordonia rubripertincta N657	-	weak	285337	2D-image
propyne	Xanthobacter sp., Xanthobacter sp. 124X, Xanthobacter sp. Py2, Xanthobacter sp. TM1	-	mechanism-based inactivator of the 21200 Da protein	285342	2D-image
propyne	Rhodococcus rhodochrous	-	irreversible inhibition in the presence of NADH, suicide substrate, growth inhibition when added to the culture medium	658683	2D-image
KCN	Mycobacterium sp.	-	-	285340	2D-image
additional information	Gordonia rubripertincta, Gordonia rubripertincta 11, Gordonia rubripertincta B 276, Gordonia rubripertincta B-276, Gordonia rubripertincta N657	-	no inhibition by ethyne	285337	-
additional information	Nocardioides sp.	-	inactivation of AkMO during starvation of cells	677851	-

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
AamD	Xanthobacter autotrophicus	O87082	the enzyme requires interaction with the small catalytic coupling/effector protein, substitution of AamD with IsoD, the coupling protein from the closely related isoprene monooxygenase, changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling	671530	-
H2O2	Rhodococcus rhodochrous, Rhodococcus rhodochrous 172, Rhodococcus rhodochrous 89, Rhodococcus rhodochrous ATCC 33278, Rhodococcus rhodochrous ATCC 39484, Rhodococcus rhodochrous B-276, Rhodococcus rhodochrous B276, Rhodococcus rhodochrous CECT3042, Rhodococcus rhodochrous CTM, Rhodococcus rhodochrous IFO 15564, Rhodococcus rhodochrous J1, Rhodococcus rhodochrous K22, Rhodococcus rhodochrous KCTC 1061, Rhodococcus rhodochrous MTCC-291, Rhodococcus rhodochrous N5, Rhodococcus rhodochrous N75, Rhodococcus rhodochrous NCIMB 11216, Rhodococcus rhodochrous NCIMB 13064, Rhodococcus rhodochrous NCIMB13064, Rhodococcus rhodochrous NCIMB 13259, Rhodococcus rhodochrous PA-34, Rhodococcus rhodochrous PNKb1, Rhodococcus rhodochrous tg1-A6	-	-	658683	2D-image
additional information	Nocardioides sp., Nocardioides sp. C190, Nocardioides sp. CF8, Nocardioides sp. CT16, Nocardioides sp. J-326TK, Nocardioides sp. KP7, Nocardioides sp. strain JS614	-	epoxyethane, a metabolic intermediate of ethene biodegradation, induces enzyme expression, acetate reactivates extant AkMO in starved vinyl chloride- or ethene-grown cultures, overview	677851	-

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.016	-	Propene	Gordonia rubripertincta, Gordonia rubripertincta 11, Gordonia rubripertincta B 276, Gordonia rubripertincta B-276, Gordonia rubripertincta N657	-	-	285338	2D-image
0.235	-	Propene	Gordonia rubripertincta, Gordonia rubripertincta 11, Gordonia rubripertincta B 276, Gordonia rubripertincta B-276, Gordonia rubripertincta N657	-	-	285337	2D-image
0.187	-	trichlorethene	Gordonia rubripertincta, Gordonia rubripertincta 11, Gordonia rubripertincta B 276, Gordonia rubripertincta B-276, Gordonia rubripertincta N657	-	-	285338	2D-image

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
0.085	-	Gordonia rubripertincta, Gordonia rubripertincta 11, Gordonia rubripertincta B 276, Gordonia rubripertincta B-276, Gordonia rubripertincta N657	-	-	285337
0.145	-	Rhodococcus rhodochrous	-	purified enzyme, pH 7.5, 30�C	658683
additional information	-	Xanthobacter sp., Xanthobacter sp. 124X, Xanthobacter sp. Py2, Xanthobacter sp. TM1	-	-	285342
additional information	-	Xanthobacter autotrophicus	O87082	-	671530

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7.2	-	Xanthobacter autotrophicus	O87082	assay at	671530

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
30	-	Xanthobacter autotrophicus	O87082	assay at	671530
30	-	Rhodococcus rhodochrous	-	assay at	674944

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
culture condition:ethene-grown cell	Nocardioides sp., Nocardioides sp. C190, Nocardioides sp. CF8, Nocardioides sp. CT16, Nocardioides sp. J-326TK, Nocardioides sp. KP7, Nocardioides sp. strain JS614	-	-	677851
culture condition:vinyl chloride-grown cell	Nocardioides sp., Nocardioides sp. C190, Nocardioides sp. CF8, Nocardioides sp. CT16, Nocardioides sp. J-326TK, Nocardioides sp. KP7, Nocardioides sp. strain JS614	-	-	677851
additional information	Nocardioides sp., Nocardioides sp. C190, Nocardioides sp. CF8, Nocardioides sp. CT16, Nocardioides sp. J-326TK, Nocardioides sp. KP7, Nocardioides sp. strain JS614	-	strain JS614 grows on the C2 alkenes ethene, vinyl chloride, and vinyl fluoride as sole carbon sources. The presence of 400-800 microM ethene oxide extended the growth substrate range to propene and butene. Propene-dependent growth of JS614 is CO2-dependent and is prevented by the carboxylase/reductase inhibitor 2-bromoethanesulfonic acid, while growth on ethene is not CO2-dependent or 2-bromoethanesulfonic acid-sensitive. Propene oxide at 0.05-0.1 mM exerts inhibitory effects on growth of JS614 on both acetate and ethene, and on ethene oxide-induced growth on ethene	710973

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
No entries in this field

PDB	SCOP	CATH	ORGANISM
No entries in this field

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
58000	-	Nocardioides sp. JS614	-	SDS-PAGE	703485

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
hexamer	Xanthobacter autotrophicus 7C, Xanthobacter autotrophicus, Xanthobacter autotrophicus GJ10	-	alpha2beta2gamma2, 2 * 58100, 2 * 38000, 2 * 9650, calculated from deduced amino acid sequences, masses in SDS-PAGE appear to be smaller (alpha and gamma subunits) or larger (beta subunit)	658775
additional information	Gordonia rubripertincta 11, Gordonia rubripertincta B 276, Gordonia rubripertincta B-276, Gordonia rubripertincta, Gordonia rubripertincta N657	-	multi-component enzyme	285335
additional information	Mycobacterium aurum L1, Mycobacterium aurum, Mycobacterium sp. 279, Mycobacterium sp. 607, Mycobacterium sp. AC777, Mycobacterium sp. E20, Mycobacterium sp. E3, Mycobacterium sp. HE5, Mycobacterium sp. HXN-1500, Mycobacterium sp. JC1 DSM 3803, Mycobacterium sp. JC1, Mycobacterium sp. JS60, Mycobacterium sp., Mycobacterium sp. NwIB-01, Mycobacterium sp. P101, Mycobacterium sp. s4, Mycobacterium sp. Takeo	-	multi-component enzyme	285340
additional information	Xanthobacter sp. 124X	-	multi-component enzyme; x * 58037, oxygenase alpha-subunit, + x * 9740, gamma-subunit, + x * 13359, ferredoxin, + x * 11193, coupling or effector protein, + 38188, oxygenase beta-subunit, + x * 34171, reductase subunit, calculation from nucleotide sequence	285341
additional information	Xanthobacter sp.	-	multi-component enzyme	285341
additional information	Xanthobacter sp. Py2, Xanthobacter sp. TM1	-	multi-component enzyme; x * 58037, oxygenase alpha-subunit, + x * 9740, gamma-subunit, + x * 13359, ferredoxin, + x * 11193, coupling or effector protein, + 38188, oxygenase beta-subunit, + x * 34171, reductase subunit, calculation from nucleotide sequence	285341
additional information	Xanthobacter sp.	-	x * 58037, oxygenase alpha-subunit, + x * 9740, gamma-subunit, + x * 13359, ferredoxin, + x * 11193, coupling or effector protein, + 38188, oxygenase beta-subunit, + x * 34171, reductase subunit, calculation from nucleotide sequence	285341
additional information	Xanthobacter sp. 124X, Xanthobacter sp., Xanthobacter sp. Py2, Xanthobacter sp. TM1	-	enzyme contains 4 components: 1. a monomeric 35500 Da NADH reductase containing 1 mol of FAD and a probable 2Fe-2S center, mass spectrometry 2. a dimeric ferredoxin consisting of two 13300 Da subunits, each containing a Rieske-type 2Fe-2S cluster, SDS-PAGE 3. a 11000 Da monomeric protein that contains no detectable cofactors, mass spectrometry 4. a 212000 Da alpha2beta2gamma2 multimeric protein containing 4 atoms of nonheme iron	285342
additional information	Xanthobacter autotrophicus	O87082	the enzyme contains NADH-oxidoreductase and a Rieske-type ferredoxin components and the binuclear non-haem iron active site, it requires a small catalytic coupling/effector protein, AamD	671530

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Gordonia rubripertincta, Gordonia rubripertincta 11, Gordonia rubripertincta B 276, Gordonia rubripertincta B-276, Gordonia rubripertincta N657	-	285337
-	Rhodococcus rhodochrous	-	658683
recombinant proteins from Escherichia coli	Xanthobacter autotrophicus	-	658775
-	Xanthobacter sp., Xanthobacter sp. 124X, Xanthobacter sp. Py2, Xanthobacter sp. TM1	-	285342

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
gene etnC, expression analysis under different culture conditions, overview	Nocardioides sp., Nocardioides sp. C190, Nocardioides sp. CF8, Nocardioides sp. CT16, Nocardioides sp. J-326TK, Nocardioides sp. KP7, Nocardioides sp. strain JS614	-	677851
expression of wild-type and mutant enzymes	Rhodococcus rhodochrous	-	674944
native and His-tagged protein expressed in Escherichia coli Rosetta(DE3)(pLysS)	Xanthobacter autotrophicus	-	658775
expression in Xanthobacter autotrophicus	Xanthobacter sp., Xanthobacter sp. 124X, Xanthobacter sp. Py2, Xanthobacter sp. TM1	-	285343

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
both propene and propene oxide induce expression of the gene encoding the alpha subunit of alkene monooxygenase, etnC, to a similar level as ethene and ethene oxide	Nocardioides sp., Nocardioides sp. C190, Nocardioides sp. CF8, Nocardioides sp. CT16, Nocardioides sp. J-326TK, Nocardioides sp. KP7, Nocardioides sp. strain JS614	-	710973

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
additional information	Rhodococcus rhodochrous	-	quasi random mutation of the large subunit of the epoxygenase component, AmoC alters the enantioselectivity of the enzyme, screening for altered epoxidation abilities	674944

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM (UNIPROT ACCESSION NO.)	LINK TO PUBMED	SOURCE
285334	Habets-Cruetzen, A.Q.H.; De Bont, J.A.M.	Inactivation of alkene oxidation by epoxides in alkene- and alkane-grown bacteria	Appl. Microbiol. Biotechnol.	22	428-433	1985	Mycobacterium sp., Mycobacterium sp. E20, Mycobacterium sp. E3	-
285335	Gallagher, S.C.; Cammack, R.; Dalton, H.	Electron transfer reactions in the alkene mono-oxygenase complex from Nocardia corallina B-276	Biochem. J.	339	79-85	1999	Gordonia rubripertincta, Gordonia rubripertincta B-276	PubMed
285336	Ensign, S.A.	Aliphatic and chlorinated alkenes and epoxides as inducers of alkene monooxygenase and epoxidase activities in Xanthobacter strain Py2	Appl. Environ. Microbiol.	62	61-66	1996	Xanthobacter sp., Xanthobacter sp. Py2	PubMed
285337	Gallagher, S.C.; Cammack, R.; Dalton, H.	Alkene monooxygenase from Nocardia corallina B-276 is a member of the class of dinuclear iron proteins capable of stereospecific epoxygenation reactions	Eur. J. Biochem.	247	635-641	1997	Gordonia rubripertincta, Gordonia rubripertincta B-276	PubMed
285338	Saeki, H.; Akira, M.; Furuhashi, K.; Averhoff, B.; Gottschalk, G.	Degradation of trichloroethene by a linear-plasmid-encoded alkene monooxygenase in Rhodococcus corallinus (Nocardia corallina) B-276	Microbiology	145	1721-1730.	1999	Gordonia rubripertincta, Gordonia rubripertincta B-276, Rhodococcus ruber, Xanthobacter sp., Xanthobacter sp. Py2	PubMed
285339	Zhou, N.Y.; Jenkins, A.; Chan Kwo Chion, C.K.N.; Leak, D.J.	The alkene monooxygenase from Xanthobacter Py2 is a binuclear non-heme iron protein closely related to toluene 4-monooxygenase	FEBS Lett.	430	181-185	1998	Xanthobacter sp., Xanthobacter sp. Py2	PubMed
285340	Hartmans, S.; Weber, F.J.; Somhorst, D.P.M.; De Bont, J.A.M.	Alkene monooxygenase from Mycobacterium: a multicomponent enzyme	J. Gen. Microbiol.	137	2555-2560	1991	Mycobacterium aurum, Mycobacterium aurum L1, Mycobacterium sp., Mycobacterium sp. E3	PubMed
285341	Zhou, N.Y.; Jenkins, A.; Chan Kwo Chion, C.K.; Leak, D.J.	The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol	Appl. Environ. Microbiol.	65	1589-1595.	1999	Xanthobacter sp., Xanthobacter sp. Py2	PubMed
285342	Small, F.J.; Ensign, S.A.	Alkene monooxygenase from Xanthobacter strain Py2. Purification and characterization of a four-component system central to the bacterial metabolism of aliphatic alkenes	J. Biol. Chem.	272	24913-24920	1997	Xanthobacter sp., Xanthobacter sp. Py2	PubMed
285343	Zhou, N.Y.; Chan Kwo Chion, C.K.N.; Leak, D.J.	Cloning and expression of the genes encoding propene monooxygenase from Xanthobacter Py2	Appl. Microbiol. Biotechnol.	44	582-588	1996	Xanthobacter sp., Xanthobacter sp. Py2	-
658683	Fosdike, W.L.; Smith, T.J.; Dalton, H.	Adventitious reactions of alkene monooxygenase reveal common reaction pathways and component interactions among bacterial hydrocarbon oxygenases	FEBS J.	272	2661-2669	2005	Rhodococcus rhodochrous, Rhodococcus rhodochrous B-276	PubMed
658775	Champreda, V.; Zhou, N.Y.; Leak, D.J.	Heterologous expression of alkene monooxygenase components from Xanthobacter autotrophicus Py2 and reconstitution of the active complex	FEMS Microbiol. Lett.	239	309-318	2004	Xanthobacter autotrophicus	PubMed
671530	Champreda, V.; Choi, Y.J.; Zhou, N.Y.; Leak, D.J.	Alteration of the stereo- and regioselectivity of alkene monooxygenase based on coupling protein interactions	Appl. Microbiol. Biotechnol.	71	840-847	2006	Xanthobacter autotrophicus (O87082)	PubMed
674944	Perry, A.; Smith, T.J.	Protocol for mutagenesis of alkene monooxygenase and screening for modified enantiocomposition of the epoxypropane product	J. Biomol. Screen.	11	553-556	2006	Rhodococcus rhodochrous, Rhodococcus rhodochrous B-276	PubMed
677851	Mattes, T.E.; Coleman, N.V.; Chuang, A.S.; Rogers, A.J.; Spain, J.C.; Gossett, J.M.	Mechanism controlling the extended lag period associated with vinyl chloride starvation in Nocardioides sp. strain JS614	Arch. Microbiol.	187	217-226	2007	Nocardioides sp.	PubMed
698495	Lara, M.; Mutti, F.; Glueck, S.; Kroutil, W.	Oxidative enzymatic alkene cleavage: Indications for a nonclassical enzyme mechanism	J. Am. Chem. Soc.	131	5368-5369	2009	Trametes hirsuta	-
703485	Chuang, A.; Jin, Y.; Schmidt, L.; Li, Y.; Fogel, S.; Smoler, D.; Mattes, T.	Proteomic analysis of ethene-enriched groundwater microcosms from a vinyl chloride-contaminated site	Environ. Sci. Technol.	44	1594-1601	2010	Nocardioides sp. JS614, Nocardioides sp. JS614 (Q5U9J8)	PubMed
710973	Taylor, A.E.; Arp, D.J.; Bottomley, P.J.; Semprini, L.	Extending the alkene substrate range of vinyl chloride utilizing Nocardioides sp. strain JS614 with ethene oxide	Appl. Microbiol. Biotechnol.	87	2293-2302	2010	Nocardioides sp.	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.69)

NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM

IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

SYSTERS

Protein Mutant Database

InterPro (database of protein families, domains and functional sites)

Mark a special word or phrase in this record:
Select one or more organisms in this record: