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Enzyme Nomenclature
Information on EC 1.14.13.25 - methane monooxygenase (soluble)
Word Map on EC 1.14.13.25
- 1.14.13.25
- methanotrophs
- methanol
- capsulatus
- methylosinus
- methylococcus
- trichosporium
-
methane-oxidizing
- methylocystis
- trichloroethylene
- methylomonas
- dioxygen
- ch4
- methylobacter
- alkane
-
carboxylate-bridged
- methylomicrobium
-
groundwater
-
copper-containing
-
ammonia-oxidizing
-
antiferromagnetically
-
peat
-
diironii
-
wetland
-
upland
-
landfill
-
non-motile
-
trinuclear
-
high-valent
- degradation
- propene
-
dicopper
- sphagnum
- biotechnology
-
t-rflp
-
cometabolic
-
seep
- nitrosomonas
-
aquifer
-
diferrous
- synthesis
-
mixed-valence
-
peroxo
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.25
-
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RECOMMENDED NAME
GeneOntology No.
methane monooxygenase (soluble)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
kinetic model of protein component interaction
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
mechanism
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
mechanism
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
modeling of interaction between the different protein components of sMMO
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
structural model for component protein B of sMMO
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methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
reaction mechanism, substrate radical intermediates in the reaction of soluble methane monooxygenase, the reaction involves the conversion of the enzyme hydroxylase component, MMOH, diiron cluster to a strongly oxidizing bis-l-oxo-Fe(IV)2 species termed compound Q, that is capable of the fissure of stable C–H bonds in methane and many other hydrocarbons
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
via diiron(IV) reaction intermediate Q, reaction mechanism of the soluble enzyme with different substrates, overview
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
reaction cycle, via formation of the hydroperoxo intermediate compound P and the key reaction cycle intermediate compound Q, overview
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
reaction mechanism via carboxylate-bridged diiron center and dioxygen, a di(my-oxo)diiron(IV) intermediate termed Q is responsible for the catalytic activity with hydrocarbons, the peroxodiiron(III) intermediate precedes Q formation in the catalytic cycle, which consists of four principal steps, overview
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
distribution of electrons in intermolecular electron-transfer intermediates, isomerization of the initial ternary complex is required for maximal electron-transfer rates
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
the soluble enzyme utilizes a carboxylate-bridged diiron center and dioxygen, a di(my-oxo)diiron(IV) intermediate termed Q is responsible for the catalytic activity with hydrocarbons, the peroxodiiron(III) intermediate precedes Q formation in the catalytic cycle
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
reaction mechanism, spin states analysis of polynuclear metal clusters, a dinuclear oxygen-bridged iron(IV) model for the intermediate Q of the hydroxylase component of methane monooxygenase by means of spin-unrestricted Kohn–Sham density functional theory, overview
methylotrophic bacterium
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
reaction mechanism and regulation, catalytic cycle of sMMO, the enzyme complex causes quantum tunneling to dominate in C–H bond cleavage reaction for methane, selectively increasing the rate for this substrate, mechanism of C-H bond cleavage, overview
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
catalyzes the oxidation of methane through the activation of O2 at a nonheme biferrous center in the hydroxylase component MMOH
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
distribution of electrons in intermolecular electron-transfer intermediates, isomerization of the initial ternary complex is required for maximal electron-transfer rates; mechanism; mechanism; mechanism; modeling of interaction between the different protein components of sMMO; reaction mechanism via carboxylate-bridged diiron center and dioxygen, a di(my-oxo)diiron(IV) intermediate termed Q is responsible for the catalytic activity with hydrocarbons, the peroxodiiron(III) intermediate precedes Q formation in the catalytic cycle, which consists of four principal steps, overview; structural model for component protein B of sMMO; the soluble enzyme utilizes a carboxylate-bridged diiron center and dioxygen, a di(my-oxo)diiron(IV) intermediate termed Q is responsible for the catalytic activity with hydrocarbons, the peroxodiiron(III) intermediate precedes Q formation in the catalytic cycle; via diiron(IV) reaction intermediate Q, reaction mechanism of the soluble enzyme with different substrates, overview
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-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
methane,NAD(P)H:oxygen oxidoreductase (hydroxylating)
The enzyme is soluble, in contrast to the particulate enzyme, EC 1.14.18.3. Broad specificity; many alkanes can be hydroxylated, and alkenes are converted into the corresponding epoxides; CO is oxidized to CO2, ammonia is oxidized to hydroxylamine, and some aromatic compounds and cyclic alkanes can also be hydroxylated, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
51961-97-8
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
protein A fragment, gene pmoA; a gammaproteobacterium closely related to methanotrophs
SwissProt
alpha-subunit, strain LAY; isolated from acidic forest soil near Marburg, Germany, gene mmoX
UniProt
alpha-subunit, strain SOP9; isolated from an acidic peat soil sampled at a depth of 10 to 20 cm of the Sphagnum peat bog Bakchar, West Siberia, Russia, gene mmoX
UniProt
alpha subunit and beta subunit and gamma subunit
P22869 and P18798 and P11987
UniProt
Bath
438920, 438922, 438923, 438928, 438929, 438930, 438931, 438932, 438936, 438937, 438938, 438939, 438943, 658051
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-
Bath
438920, 438922, 438923, 438928, 438929, 438930, 438931, 438932, 438936, 438937, 438938, 438939, 438943, 438949, 658051
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-
alpha-subunit, strain AR4T; isolated from an acidic peat soil sampled at a depth of 10 cm of the oligo-mesotrophic fen Torfjanoye, Archangelsk region, European North Russia, gene mmoX
UniProt
alpha-subunit, strain LAY; isolated from acidic forest soil near Marburg, Germany, gene mmoX
UniProt
alpha-subunit, strain SOP9; isolated from an acidic peat soil sampled at a depth of 10 to 20 cm of the Sphagnum peat bog Bakchar, West Siberia, Russia, gene mmoX
UniProt
alpha-subunit, strain AR4T; isolated from an acidic peat soil sampled at a depth of 10 cm of the oligo-mesotrophic fen Torfjanoye, Archangelsk region, European North Russia, gene mmoX
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
pMMO consists of two protein components (NADH-OR and pMH) and is coupled to the electron transport chain
physiological function
-
soluble methane monooxygenase is a bacterial enzyme that converts methane to methanol at a carboxylate-bridged diiron center with exquisite control. The enzyme is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane
physiological function
-
pMMO consists of two protein components (NADH-OR and pMH) and is coupled to the electron transport chain
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-dimethylpentane + NAD(P)H + O2
3,4-dimethylpentan-2-ol + NAD(P)+ + H2O
-
-
-
?
2-methylpropane + NAD(P)H + O2
2-methylpropan-2-ol + 2-methylpropan-1-ol + NAD(P)+ + H2O
-
-
-
?
adamantane + NAD(P)H + O2
1-adamantanol + 2-adamantanol + NAD(P)+ + H2O
-
-
-
?
beta-pinene + NAD(P)H + O2
6,6-dimethylbicyclo[3.1.1]hept-2-ene-2-methanol + beta-pinene oxide + NAD(P)+ + H2O
-
-
-
?
biphenyl + NAD(P)H + H+ + O2
2-hydroxybiphenyl + 4-hydroxybiphenyl + NAD(P)+ + H2O
-
-
-
-
?
chlorobenzene + NAD(P)H + O2
chlorophenol + NAD(P)+ + H2O
-
sMMO
-
?
chloromethane + NAD(P)H + O2
formaldehyde + NAD(P)+ + H2O + ?
-
-
-
?
chloronaphthalene + NAD(P)H + O2
chloronaphthol + NAD(P)+ + H2O
-
sMMO
-
?
chloropentane + NAD(P)H + O2
chloropentanol + NAD(P)+ + H2O
-
sMMO
-
?
cis-1,3-dimethylcyclohexane + NAD(P)H + O2
3,5-dimethylcyclohexanol + 1-cis-3-dimethylcyclohexanol + NAD(P)+ + H2O + 1-trans-3-dimethylcyclohexanol
-
-
1-trans-3-dimethylcyclohexanol is produced in a low concentration
?
cis-1,4-dimethylcyclohexane + NAD(P)H + O2
1-cis-4-dimethylcyclohexanol + NAD(P)+ + H2O + trans-2,5-dimethylcyclohexanol
-
-
trans-2,5-dimethylcyclohexanol is produced in a low concentration
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
cyclohexene + NAD(P)H + O2
epoxycyclohexane + 2-cyclohexen-1-ol + NAD(P)+ + H2O
-
-
-
?
cytochrome c + NAD(P)H + O2
reduced cytochrome c + NAD(P)+ + H2O
-
sMMO
-
-
?
dichloromethane + NAD(P)H + O2
CO + Cl- + NAD(P)+ + H2O
-
-
-
?
ethylbenzene + NAD(P)H + H+ + O2
1-phenylethanol + 3-ethylphenol + 4-ethylphenol + NAD(P)+ + H2O
-
-
-
-
?
fluorobenzene + NAD(P)H + O2
fluorophenol + NAD(P)+ + H2O
-
sMMO
-
?
isobutane + NAD(P)H + O2
2-methyl-1-propanol + 2-methyl-2-propanol + NADP+ + H2O
-
-
-
?
isopentane + NAD(P)H + O2
2-methylbutan-1-ol + 3-methylbutan-1-ol + 2-methylbutan-2-ol + 3-methylbutan-2-ol + NADP+ + H2O
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
-
-
-
-
?
methane + trans-dichloroethylene + vinyl chloride + trichloroethylene + ?
formaldehyde + ?
-
each of these compounds is completely degraded by sMMO-expressing cells when initial concentrations are either 0.01 or 0.03 mM
-
-
?
methanol + NADH + H+ + O2
? + H2O + NAD+
-
substrate of intermediate species, Hperoxo and Q, kinetics, overview
-
-
?
methylamine + NADH + H+ + O2
hydroxymethylamine + H2O + NAD+
-
substrate of intermediate species, Hperoxo and Q, kinetics, overview
-
-
?
methylcyanide + NADH + H+ + O2
hydroxymethylcyanide + H2O + NAD+
-
substrate of intermediate species, Hperoxo and Q, kinetics, and proposed mechanism of CH3CN hydroxylation by Hperoxo, overview
-
-
?
methylene cyclohexane + NAD(P)H + O2
1-cyclohexane-1-methanol + methylene cyclohexane oxide + 4-hydroxymethylene cyclohexane + NAD(P)+ + H2O
-
-
-
?
naphthalene + NAD(P)H + H+ + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
-
-
-
?
octane + NAD(P)H + O2
1-octanol + 2-octanol + NAD(P)+ + H2O
-
-
-
?
phenylalanine + NAD(P)H + O2
tyrosine + NAD(P)+ + H2O
-
-
-
?
propylaldehyde + NADH + H+ + O2
? + H2O + NAD+
-
substrate of intermediate species, Hperoxo and Q, kinetics, overview
-
-
?
propylene + duroquinol + O2
propylene oxide + reduced duroquinol + H2O
-
-
-
-
?
propylene + NADH + H+ + O2
propylene epoxide + NAD+ + H2O
-
-
-
-
?
pyridine + NAD(P)H + O2
pyridine N-oxide + NAD(P)+ + H2O
-
-
-
?
toluene + NAD(P)H + H+ + O2
benzyl alcohol + cresol + NAD(P)+ + H2O
-
-
-
-
?
toluene + NAD(P)H + O2
benzyl alcohol + cresol + NAD(P)+ + H2O
-
-
-
?
toluene + NAD(P)H + O2
benzyl alcohol + NAD(P)+ + H2O
-
-
-
?
trichloromethane + NAD(P)H + O2
CO2 + Cl- + NAD(P)+ + H2O
-
-
-
?
1-butene + NAD(P)H + O2
1,2-epoxybutane + NAD(P)+ + H2O
-
-
-
?
1-butene + NAD(P)H + O2
1,2-epoxybutane + NAD(P)+ + H2O
-
-
-
?
benzene + NAD(P)H + O2
cyclohexanol + phenol + hydroquinone + NAD(P)+ + H2O
-
-
-
?
benzene + NAD(P)H + O2
cyclohexanol + phenol + hydroquinone + NAD(P)+ + H2O
-
-
-
?
butane + NAD(P)H + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
-
-
-
?
butane + NAD(P)H + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
-
-
only 2-butanol, sMMO
?
butane + NAD(P)H + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
-
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
-
-
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
-
-
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
-
-
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
-
sMMO
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
-
sMMO
-
?
difluoromethane + NADH + O2
difluoromethanol + NAD+ + H2O
-
soluble enzyme
-
-
?
difluoromethane + NADH + O2
difluoromethanol + NAD+ + H2O
-
soluble enzyme
-
-
?
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
-
-
-
-
?
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
-
-
-
?
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
-
-
-
?
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
-
no activity
-
-
-
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
-
-
-
?
fluoromethane + NADH + O2
fluoromethanol + NAD+ + H2O
-
soluble enzyme
-
-
?
fluoromethane + NADH + O2
fluoromethanol + NAD+ + H2O
-
soluble enzyme
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + NAD(P)+ + H2O
-
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + NAD(P)+ + H2O
-
-
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + NAD(P)+ + H2O
-
sMMO
position of hydroxylation cannot be determined exactly
?
hexane + NAD(P)H + O2
1-hexanol + 2-hexanol + NAD(P)+ + H2O
-
-
-
?
hexane + NAD(P)H + O2
1-hexanol + 2-hexanol + NAD(P)+ + H2O
-
-
-
-
?
hexane + NAD(P)H + O2
1-hexanol + 2-hexanol + NAD(P)+ + H2O
-
sMMO
position of hydroxylation cannot be determined exactly
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
consists of three subunits, the hydroxylase (MMOH), at which the oxidation of methane takes place, the reductase (MMOR) and a small regulating unit MMOB
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
initial step in the assimilation of methane in bacteria that grow with methane as sole carbon and energy source
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
initial step in the assimilation of methane in bacteria that grow with methane as sole carbon and energy source
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
via diiron(IV) reaction intermediate Q, the decay rate of intermediate Q is substantially accelerated in the presence of fluuoromethane and difluoromethane
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
modeling intermolecular electron transfer in the sMMO system, interconversion of rapid and slow electron-transfer pathways, overview
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
via diiron(IV) reaction intermediate Q, the decay rate of intermediate Q is substantially accelerated in the presence of fluuoromethane and difluoromethane
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
modeling intermolecular electron transfer in the sMMO system, interconversion of rapid and slow electron-transfer pathways, overview
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
methane is oxidized to methanol with 100% efficiency with no over-oxidation, methanol is then further oxidized by other enzymes in two electron steps to CO2
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
for the MMOH alone the rate of turnover is increased 150fold and rate constant for O2 binding is increased 1000fold in the binary complex compared to the complete enzyme
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
oxidized by sMMO
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
oxidized by sMMO
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
sMMO
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
oxidized by sMMO
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
oxidized by sMMO
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
-
-
-
?
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
-
-
-
-
?
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
-
-
-
-
?
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
-
-
-
-
?
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
-
-
-
-
?
nitrobenzene + NADH + O2
nitrophenol + NAD+ + H2O
-
an electron is removed from nitrobenzene by Q in the first step of the reaction and then the bound hydroxyl radical formed in this process rebounds to form nitrophenol
-
-
?
pentane + NAD(P)H + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
-
-
-
?
pentane + NAD(P)H + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
-
-
-
?
pentane + NAD(P)H + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
-
sMMO
position of hydroxylation cannot be determined exactly
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
-
-
-
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
-
-
only 2-propanol, sMMO
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
-
-
only 2-propanol, sMMO
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
-
-
-
-
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
?
propylene + NAD(P)H + O2
propylene oxide + NADP+ + H2O
-
enzyme form sMMO
-
?
propylene + NAD(P)H + O2
propylene oxide + NADP+ + H2O
-
enzyme form sMMO
-
?
propylene + NAD(P)H + O2
propylene oxide + NADP+ + H2O
-
enzyme form sMMO
-
?
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
-
-
-
-
?
propylene + NADH + O2
propylene oxide + NAD+ + H2O
-
the peroxodiiron(III) intermediate that precedes Q formation in the catalytic cycle has been demonstrated to react with propylene
-
-
?
propylene + NADH + O2
propylene oxide + NAD+ + H2O
-
the peroxodiiron(III) intermediate that precedes Q formation in the catalytic cycle has been demonstrated to react with propylene
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
-
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
-
-
-
?
additional information
?
-
-
cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode
-
-
-
additional information
?
-
-
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview
-
-
-
additional information
?
-
-
a number of substituted methanes, e.g. CH3X (X) H, CH3, OH, CN, NO2, or F, react with MMOH, quantitative modeling of substrate hydroxylation via mixed quantum mechanics/molecular mechanics techniques, overview
-
-
-
additional information
?
-
-
the enzyme catalyzes the selective oxidation of methane to methanol, but the enzyme is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane
-
-
-
additional information
?
-
-
the enzyme catalyzes the selective oxidation of methane to methanol, but is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane. Reactions of the two intermediate species, of Hperoxo and Q, two oxidants that are generated sequentially during the reaction of reduced protein with O, with a panel of substrates of varying C-H bond strength, double-mixing stoppedflow spectroscopy, overview. Three classes of substrates exist according to the rate-determining step in the reaction
-
-
-
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
-
pMMO has broader substrate specificity but lower activity with smaller hydrocarbons like methane, ethane, and propene compared to pMMO
-
-
-
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
-
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview
-
-
-
additional information
?
-
-
a number of substituted methanes, e.g. CH3X (X) H, CH3, OH, CN, NO2, or F, react with MMOH, quantitative modeling of substrate hydroxylation via mixed quantum mechanics/molecular mechanics techniques, overview
-
-
-
additional information
?
-
-
pMMO has broader substrate specificity but lower activity with smaller hydrocarbons like methane, ethane, and propene compared to pMMO
-
-
-
additional information
?
-
-
sMMO expressed at low copper concentration shows low substrate specificity, while pMMO expressed at high copper concentration shows high substrate specificity
-
-
-
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
-
sMMO expressed at low copper concentration shows low substrate specificity, while pMMO expressed at high copper concentration shows high substrate specificity
-
-
-
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
-
pMMO has broader substrate specificity but lower activity with smaller hydrocarbons like methane, ethane, and propene compared to pMMO
-
-
-
additional information
?
-
-
access and regulation in the methane monooxygenase system via interaction of reductase protein MMOB and hydroxylase protein MMOH, regulatory effects of MMOB, overview
-
-
-
additional information
?
-
-
oxidation of deuterated compounds
-
-
-
additional information
?
-
-
effects of spin-traps on MMO activity, overview
-
-
-
additional information
?
-
-
inactive toward anthracene and phenanthrene
-
-
-
additional information
?
-
-
pMMO has broader substrate specificity but lower activity with smaller hydrocarbons like methane, ethane, and propene compared to pMMO
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
initial step in the assimilation of methane in bacteria that grow with methane as sole carbon and energy source
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
initial step in the assimilation of methane in bacteria that grow with methane as sole carbon and energy source
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
via diiron(IV) reaction intermediate Q, the decay rate of intermediate Q is substantially accelerated in the presence of fluuoromethane and difluoromethane
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
via diiron(IV) reaction intermediate Q, the decay rate of intermediate Q is substantially accelerated in the presence of fluuoromethane and difluoromethane
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
methane is oxidized to methanol with 100% efficiency with no over-oxidation, methanol is then further oxidized by other enzymes in two electron steps to CO2
-
-
?
additional information
?
-
-
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview
-
-
-
additional information
?
-
-
the enzyme catalyzes the selective oxidation of methane to methanol, but the enzyme is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane
-
-
-
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
-
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview
-
-
-
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
-
access and regulation in the methane monooxygenase system via interaction of reductase protein MMOB and hydroxylase protein MMOH, regulatory effects of MMOB, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome c
-
one of three protein components is a soluble CO-binding cytochrome c
Ferredoxin
-
several MMOR ferredoxin analogues, intermolecular electron transfer from ferredoxin analogues to hydroxylase protein MMOH, redox potential determinations, overview
-
FAD
-
protein C, reductase component: contains 1 mol FAD per mol protein
FAD
-
protein C, reductase component: contains 1 mol FAD per mol protein
FAD
-
protein C, reductase component: contains 1 mol FAD per mol protein
NADH
-
-
438921, 438922, 438924, 438932, 438933, 438934, 438935, 438941, 438946, 438948, 657998, 671721, 672102, 672130, 684566, 685262, 685272, 701759
NADH
-
two-electron reduction of MMOHox by NADH mediated by MMOR enables further oxidation cycles
NADH
-
-
438920, 438922, 438928, 438929, 438930, 438931, 438932, 438936, 438937, 438938, 438939, 438943, 438945, 438949, 658051, 671722, 672049, 673999, 674145, 674158, 674170, 701759, 711260, 728376
additional information
-
component D contains no metal ions or organic cofactors
-
additional information
-
cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
-
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview
Cu2+
Fe2+
Iron
Zn2+
additional information
Cu2+
-
copper genetically regulates the enzyme activity of the soluble and membrane-bound form
Cu2+
-
cells adapted to the respective medium, either lacking Cu (sMMO production) or containing 0.01 mM Cu (pMMO production)
Cu2+
-
cells adapted to the respective medium, either lacking Cu (sMMO production) or containing 0.01 mM Cu (pMMO production)
Cu2+
-
copper-containing protein component contains one copper atom per molecule; cytochrome component contains 0.3-0.8 atoms copper per molecule
Cu2+
-
the membrane-bound pMMO contains 4.8 Cu2+ ions per 100 kDa protomer the purified pMMO contains 1.4 Cu2+ ions per 100 kDa protomer, the enzyme contains a dinuclear copper center
Cu2+
-
cells adapted to the respective medium, either lacking Cu (sMMO production) or containing 0.01 mM Cu (pMMO production)
Cu2+
-
expression of the genes encoding sMMO and pMMO is regulated by copper ions, with sMMO expressed solely when copper is limiting
Cu2+
-
when allylthiourea is removed, sMMO activity is maintained for an additional 24 generations, albeit at a slightly lower level due to the presence of 0.0007 mM of Cu2+ in the feed medium
Fe2+
-
MOOH contains 3.7-4.1 Fe atoms per dimer, binding structure and geometric configuration, EXAFS and Fourier transformation analysis, detailed overview
Fe2+
-
the [2Fe-2S] cofactor of MMOR is a one-electron carrier, the ferredoxin center must transfer two electrons sequentially to MMOH to reduce fully each diiron(III) hydroxylase active site, overview
Fe2+
-
the enzyme contains a Fe2S2 cluster, a bis-my-hydroxo-bridged dinuclear iron cluster, that binds to the enzyme reductase domain MMOR
Fe2+
-
the purified pMMO contains 7.6 Fe2+ ions per 100 kDa protomer, the membrane-bound pMMO contains 2.1 Fe2+ ions per 100 kDa protomer
Fe2+
methylotrophic bacterium
-
spin states in the polynuclear [Fe2O2] core cluster, a dinuclear oxygen-bridged iron(IV) model for the intermediate Q of the hydroxylase component of methane monooxygenase by means of spin-unrestricted Kohn–Sham density functional theory, calculated coupling constants in calculation of Heisenberg coupling constants with Noodleman’s Broken-Symmetry approach, computational method, optimized cluster structures, overview
Iron
-
protein A, hydroxylase component: contains a binuclear iron center; protein C, reductase component: contains 1 [Fe2-S2]
Iron
-
1 mol of [2Fe-2S(S-Cys)4]centre per mol protein; 2 g-atom iron; characterization of [Fe2-S2] redox centre of component C
Iron
-
a [2Fe-2S]cluster; contains hydroxo-bridged binuclear iron clusters; contains oxo-bridged binuclear iron clusters
Iron
-
non-heme iron, 3.02 mol iron per mol of enzyme, addition of exogenous FeCl2 or FeCl3 does not affect the enzyme activity
Iron
-
contains an Fe4+(micro-O)2Fe4+ center. A terminal hydroxo and a protonated His147 which is dissociated from a nearby Fe, is more asymmetric in its Fe(micro-O)2Fe diamond core, and is another very good candidate for intermediate Q
Iron
-
in MmoH Fe-water distances vary from about 1.9 to 2.7 A, showing Fe1 to be 5 or 6 coordinate. The effect of binding toluene-4-monooxygenase D/MmoB to toluene-4-monooxygenase H/MmoH is not to remove a water ligand from either iron but to induce a change in orientation of the terminal glutamate on Fe2. This allows O2 to bridge the diiron site and aligns the redox active orbital on each Fe for efficient 2-electron transfer, facilitating the formation of a stabilized peroxo intermediate
Zn2+
-
component A, hydroxylase component: contains 0.5 mol zinc per mol protein
Zn2+
-
the purified pMMO contains 1.3 Zn2+ ions per 100 kDa protomer, the membrane-bound pMMO contains 2.7 Zn2+ ions per 100 kDa protomer
additional information
-
sMMO activity and expression does not require Cu2+
additional information
-
the enzyme contains very low or no amounts of copper and zinc
additional information
-
sMMO activity and expression does not require Cu2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
protein MMOB
-
inhibition of sMMO auxiliary proteins MMOB or MMOD severely diminishes electron-transfer throughput from MMOR, primarily by shifting the bulk of electron transfer to the slowest pathway, the biphasic reactions for electron transfer to MMOH from several MMOR ferredoxin analogues are also inhibited, overview
-
protein MMOD
-
inhibition of sMMO auxiliary proteins MMOB or MMOD severely diminishes electron-transfer throughput from MMOR, primarily by shifting the bulk of electron transfer to the slowest pathway, the biphasic reactions for electron transfer to MMOH from several MMOR ferredoxin analogues are also inhibited, overview
-
2,4-Dichloro-(6-phenylphenoxy)ethylamine hydrochloride
-
no inhibition
Allylthiourea
-
pMMO inhibitor and copper chelator. Without allylthiourea strain OB3b quickly loses sMMO activity whenever it is grown on NMS medium with methane as the sole carbon and energy source. No loss of sMMO activity when the growth substrate is switched from methane to methanol when allylthiourea is added to growth medium containing copper
Cu2+
-
copper ions irreversibly inhibit the activity of sMMO in vivo and in vitro by inactivating the reductase component
Cu2+
-
copper ions irreversibly inhibit the activity of sMMO in vivo and in vitro by inactivating the reductase component
Cu2+
-
copper ions irreversibly inhibit the activity of sMMO in vivo and in vitro by inactivating the reductase component
Cu2+
-
loss of sMMO activity with copper addition to a culture growing on methanol. Recovery of sMMO activity by addition of allylthiourea
Fe2+
-
activation of dioxygen occurs at a diiron centre within the hydroxylase subunit. The monooxygenation of a substrate by sMMO requires only two oxidation equivalents, and, consequently, after the oxygenation the two iron centres remain in the oxidation state +III
poly-beta-hydroxybutyrate
-
MMO activity dramatically decreases when cellular poly-beta-hydroxybutyrate accumulates in the second stage. The more poly-beta-hydroxybutyrate are accumulated, the slower MMO activity decreases. Cellular poly-beta-hydroxybutyrate content has some influence on the maintenance of the MMO activity
poly-beta-hydroxybutyrate
-
MMO activity dramatically decreases when cellular poly-beta-hydroxybutyrate accumulates in the second stage. The more poly-beta-hydroxybutyrate are accumulated, the slower MMO activity decreases. Cellular poly-beta-hydroxybutyrate content has some influence on the maintenance of the MMO activity
poly-beta-hydroxybutyrate
-
MMO activity dramatically decreases when cellular poly-beta-hydroxybutyrate accumulates in the second stage. The more poly-beta-hydroxybutyrate are accumulated, the slower MMO activity decreases. Cellular poly-beta-hydroxybutyrate content has some influence on the maintenance of the MMO activity
additional information
-
sMMO is completely inhibited by monomeric component D, but not by dimeric, monomeric MMOD is interfering with the catalytically active complex between component A hydroxylase and component protein B
-
additional information
-
when cultivated in nutrients deficiency culture, activity of sMMO does not decrease
-
additional information
-
when cultivated in nutrients deficiency culture, activity of sMMO decreases
-
additional information
-
different chlorinated hydrocarbons cause different inhibition patterns
-
additional information
-
when cultivated in nutrients deficiency culture, activity of sMMO in strain OB3b decreases, whereas activity of sMMO in strain IMV3011 does not decrease
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
catalase
-
reduction current is enhanced by the presence of catalase ot if the reaction is performed in a flow-cell, probably because O2 is reduced to H2O2, by the hydroxylase component of the enzyme MMOH at the electrode surface and the H2O2 then inactivates the enzyme unless removed by catalase or a continous flow solution
-
regulatory protein MMOB
-
the native regulatory protein MMOB is required for maximum enzyme activity
-
additional information
-
when the growth-limiting substrate is switched from methane to methanol, in the presence of the particulate MMO inhibitor allylthiourea, growth continues unabated and sMMO activity is completely retained. During the brief period when both methane and methanol are present, higher sMMO activity is observed
-
additional information
-
contains one axial water which also H-bonds to both side chains of Glu243 and Glu114, and one bidentate carboxylate group from the side chain of Glu144, which is likely to represent the active site of MMOH-Q
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
soluble enzyme, stopped-flow transient kinetics, double-mixing stopped-flow optical spectroscopic measurements, difluoromethane exhibits a smaller second-order rate constant for reaction with intermediate Q compared to methane
-
additional information
additional information
-
effects of the C-terminal region of the B component MMOB and the active site diiron cluster of sMMO on the steady-state turnover, stopped-flow transient kinetics of the reaction cycle of wild-type and mutant enzymes, overview, deuterium kinetic isotope effect for the reaction of Q with methane, overview
-
additional information
additional information
-
steady-state kinetics
-
additional information
additional information
-
kinetics, deuterium kinetic isotope effects, overview
-
additional information
additional information
-
thermodynamics, stopped-flow kinetics, time-course profiles for MMOH reduction by MMOR ferredoxin and by MMOR3e-
-
additional information
additional information
-
analysis of kinetics of single turnover reactions of the two intermediates with ethyl vinyl ether and diethyl ether, single- and double-mixing stopped-flow optical spectroscopy, overview, stopped-flow kinetics, analytical model of transient kinetics
-
additional information
additional information
methylotrophic bacterium
-
energetic parameters
-
additional information
additional information
-
kinetics for class III substrates of Hperoxo, and kinetics and thermodynamic parameters for class III substrates of Q at 4°C and 20°C, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Methylosinus trichosporium
-
turnover numbers of component A
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00011
-
purified enzyme, using propylene and duroquinol as substrates
0.0029
-
membrane-bound enzyme, using propylene and NADH as substrates
0.003
-
membrane-bound enzyme, using propylene and duroquinol as substrates
additional information
additional information
-
recombinant shows higher activity than the wild-type
additional information
-
quantitative modeling of substrate hydroxylation via mixed quantum mechanics/molecular mechanics techniques, overview
additional information
-
component protein B is involved in enzyme regulation and enhances the activity 10fold
additional information
-
effects of spin-traps on MMO activity, spin trapping by 5,5-dimethyl-1-pyrroline N-oxide and alpha-4-pyridyl-1-oxide N-tert-butylnitrone, mechanism, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.4 - 7.4
-
pH 6.4: about 20% of activity maximum, pH 7.4: about 25% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
45
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C
additional information
colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C
additional information
colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C
additional information
-
colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C
additional information
-
colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C; colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C
-
additional information
-
colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C
-
additional information
-
colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C
-
additional information
-
colorimetric naphthalene oxidation test used for sMMO activity in cells, cells are able to grow on methane and independently of Cu2+. Cells grow at pH range 3.5-7.2 with the 11 optimum at pH 4.8-5.2. The temperature range for growth is 4-33°C with the optimum at 20-23°C
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme from cells grown under conditions of low copper availability
-
-
-
cytoplasmatic, soluble enzyme form termed sMMO
-
cytoplasmatic, soluble enzyme form termed sMMO; enzyme from cells grown under conditions of low copper availability
-
-
cytoplasmatic, soluble enzyme form termed sMMO; enzyme from cells grown under conditions of low copper availability
-
cytoplasmatic, soluble enzyme form termed sMMO; enzyme from cells grown under conditions of low copper availability
-
-
cytoplasmatic, soluble enzyme form termed sMMO; enzyme from cells grown under conditions of low copper availability
-
membrane-bound particulate enzyme form termed pMMO
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15100
15800
-
component B containing FAD and [Fe2-S2]-cluster, gel filtration
17000
20000
22700
-
component A: 2 * 54400 alpha, 2 * 43000 beta + 2 * 22700 gamma, sedimentation velocity, SDS-PAGE, amino acid analysis
23000
24000
36000
-
2 * 58000, alpha-subunit, + 2 * 36000, beta-subunit, + 2 * 23000, gamma-subunit, (alphabetagamma)2, SDS-PAGE
40000
42000
43000
54000
-
component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation
54400
-
component A: 2 * 54400 alpha, 2 * 43000 beta + 2 * 22700 gamma, sedimentation velocity, SDS-PAGE, amino acid analysis
55000
-
component A: 2 * 55000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
56000
-
component A: 2 * 56000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
57000
-
component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE
58000
-
2 * 58000, alpha-subunit, + 2 * 36000, beta-subunit, + 2 * 23000, gamma-subunit, (alphabetagamma)2, SDS-PAGE
220000
additional information
17000
-
component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation
20000
-
component A: 2 * 56000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
20000
-
component A: 2 * 55000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
23000
-
component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE
23000
-
2 * 58000, alpha-subunit, + 2 * 36000, beta-subunit, + 2 * 23000, gamma-subunit, (alphabetagamma)2, SDS-PAGE
40000
-
component A: 2 * 55000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
42000
-
component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation
43000
-
component A: 2 * 54400 alpha, 2 * 43000 beta + 2 * 22700 gamma, sedimentation velocity, SDS-PAGE, amino acid analysis
43000
-
component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE
additional information
-
3 components: 1 soluble CO-binding cytochrome c, 1 copper-containing protein, and 1 small protein, SDS-PAGE; enzyme system consists of 3 protein components A, B, C; see under subunits: molecular weights of the subunits of components
additional information
-
enzyme system consists of 3 protein components A, B, C; see under subunits: molecular weights of the subunits of components
additional information
-
enzyme system consists of 3 protein components A, B, C; see under subunits: molecular weights of the subunits of components
additional information
-
enzyme system consists of 3 protein components A, B, C; see under subunits: molecular weights of the subunits of components
additional information
-
enzyme system consists of 3 protein components A, B, C; see under subunits: molecular weights of the subunits of components
additional information
-
enzyme system consists of 3 protein components A, B, C; see under subunits: molecular weights of the subunits of components
additional information
-
enzyme system consists of 3 protein components A, B, C; see under subunits: molecular weights of the subunits of components
additional information
-
see under subunits: molecular weights of the subunits of components
additional information
-
enzyme system consists of 3 protein components A, B, C
additional information
-
enzyme system consists of 3 protein components A, B, C; structure, review
additional information
-
enzyme system consists of 3 protein components A, B, C
additional information
-
complex formation of protein components; enzyme system consists of 3 protein components A, B, C
additional information
-
enzyme system consists of 3 protein components A, B, C
additional information
-
enzyme system consists of 3 protein components A, B, C
additional information
-
enzyme system consists of 3 protein components A, B, C
additional information
-
enzyme system consists of 3 protein components A, B, C
additional information
-
sMMO is a multicomponent enzyme consisting of a hydroxylase, a protein B and a reductase
additional information
-
protein B shows unusual behaviour in gel filtration
additional information
-
sMMO is a multicomponent enzyme consisting of a hydroxylase, a protein B and a reductase
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotrimer
hexamer
additional information
?
-
component A: 2 * 55000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
?
-
protein A: 2 * 54000-60630, alpha+ 2 * 42000-44720, beta + 2 * 17000-19840, gamma
?
-
component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation
?
-
component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation; protein A: 2 * 54000-60630, alpha+ 2 * 42000-44720, beta + 2 * 17000-19840, gamma
-
?
-
component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE
?
-
component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE
-
?
-
component A: 2 * 56000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
?
-
component A: 2 * 56000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
-
?
-
component A: 2 * 54400 alpha, 2 * 43000 beta + 2 * 22700 gamma, sedimentation velocity, SDS-PAGE, amino acid analysis
hexamer
-
2 * 58000, alpha-subunit, + 2 * 36000, beta-subunit, + 2 * 23000, gamma-subunit, (alphabetagamma)2, SDS-PAGE
hexamer
-
2 * 58000, alpha-subunit, + 2 * 36000, beta-subunit, + 2 * 23000, gamma-subunit, (alphabetagamma)2, SDS-PAGE
-
additional information
-
enzyme system consists of 3 protein components A, B, C; see under molecular weight for the size of the protein components
additional information
-
enzyme system consists of 3 protein components A, B, C
additional information
-
component A is a hydroxylase; enzyme system consists of 3 protein components A, B, C; see under molecular weight for the size of the protein components
additional information
-
component A is a hydroxylase; enzyme system consists of 3 protein components A, B, C; structure, review
additional information
-
component A is a hydroxylase; enzyme system consists of 3 protein components A, B, C
additional information
-
sMMO consists of 4 components: a hydroxylase, a reductase, a protein B and a protein D
additional information
-
enzyme structure, the enzyme consists of a hydroxylase protein MMOH and a regulatory reductase protein MMOR, comparison of MMOH-MMOR-ferrdoxin and MMOH-MMOR, binding interactions, overview
additional information
-
component A is a hydroxylase; component A is a hydroxylase; component A is a hydroxylase; component A is a hydroxylase; component A is a hydroxylase; enzyme structure, the enzyme consists of a hydroxylase protein MMOH and a regulatory reductase protein MMOR, comparison of MMOH-MMOR-ferrdoxin and MMOH-MMOR, binding interactions, overview; enzyme system consists of 3 protein components A, B, C; enzyme system consists of 3 protein components A, B, C; enzyme system consists of 3 protein components A, B, C; enzyme system consists of 3 protein components A, B, C; enzyme system consists of 3 protein components A, B, C; see under molecular weight for the size of the protein components; see under molecular weight for the size of the protein components; sMMO consists of 4 components: a hydroxylase, a reductase, a protein B and a protein D; structure, review
-
additional information
-
sMMO is a multicomponent enzyme consisting of a hydroxylase, a protein B and a reductase
additional information
-
three-dimensional structure, the enzyme consists as three protein component system, the regulatory protein MMOB, containing Fe2S2 cluster and a FAD cofactor, binds to the active site-containing hydroxylase protein creating a pore sized for methane into the active site, the third component is termed B, the complex appears to cause quantum tunneling to dominate in C–H bond cleavage reaction for methane, selectively increasing the rate for this substrate, overview
additional information
-
enzyme system consists of 3 protein components A, B, C; see under molecular weight for the size of the protein components
additional information
-
enzyme system consists of 3 protein components A, B, C; see under molecular weight for the size of the protein components
-
additional information
-
3 components: 1 soluble CO-binding cytochrome c, 1 copper-containing protein, and 1 small protein, SDS-PAGE; component A is a hydroxylase; enzyme system consists of 3 protein components A, B, C; see under molecular weight for the size of the protein components
additional information
-
component A is a hydroxylase; enzyme system consists of 3 protein components A, B, C; see under molecular weight for the size of the protein components
additional information
-
complex formation of protein components; component A is a hydroxylase; enzyme system consists of 3 protein components A, B, C
additional information
-
component A is a hydroxylase; enzyme system consists of 3 protein components A, B, C
additional information
-
interaction of the soluble methane monooxygenase regulatory component, MMOB, and the active site-bearing hydroxylase component, MMOH, spin labeling with 4-maleimido-2,2,6,6-tetramethyl-1-piperidinyloxy, high affinity of labeled MMOB for the oxidized MMOH decreases substantially with increasing pH and increasing ionic strength but is nearly unaffected by addition of nonionic detergents, the MMOB-MMOH complex is stabilized by electrostatic interactions, overview
additional information
-
the enzyme mainly exists of alpha-helical regions, circular dichroism measurement
additional information
-
the enzyme mainly exists of alpha-helical regions, circular dichroism measurement
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M MES (pH 6.5) and 15% PEG 20000 (w/v)
-
X-ray crystal structure of the apo, Mn(II)-soaked, and Co(II)-grown hydroxylase component of methane monooxygenase, determined at 2.3 A or greater resolution, reveal that the presence of metal ions is essential for the proper folding of helices E, F, and H of the alpha-subunit
-
sitting drop vapour diffusion method with 100 mM cacodylate, pH 6.5, 20% (v/v) PEG 3000, 250 mM magnesium formate or MnCl2
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
N-terminal truncated sMMO component B increases the heat stability of the sMMO hydroxylase
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
5 mM thioglycollate, 5 mM dithiothreitol, 5 mM NADH stabilize component C at 0°C
-
instability of enzyme in crude extract
instability of the enzyme during purification is probably due to loss of iron
-
protein B, in crude form requires addition of protease inhibitor phenylmethylsulfonyl fluoride
-
protein C requires presence of thiol protective agent, e.g. sodium thioglycolate throughout purification
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, sMMO component C reductase, 90% loss of activity after 120 h, can be restored by Fe2+
-
sMMO component A hydroxylase is very unstable, splits into inactive subunits when stored frozen even for short periods
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 components: a soluble CO-binding cytochrome c, a copper-containing protein, another small protein
-
component D of sMMO recombinant from Escherichia coli as His-tagged thioredoxin-fusion protein, the thioredoxin is cleaved off during purification by factor Xa
-
DEAE-Sepharose column chromatography, Q sepharose column chromatography, S-200 gel filtration, and S-300 gel filtration
-
native enzyme 8.08fold by anion exchange chromatography, ultrafiltration, gel filtration, and again anion exchange chromatography, to 95% purity
-
native MMOH, in the purification procedure includes anion exchange chromatography and gel filtration
-
recombinant component protein B of sMMO as glutathione-S-transferase fusion protein from Escherichia coli
-
recombinant enzyme component MMOB from Escherichia coli by solubilization from the 12000 x g pellet with 8 M urea, followed by dilution for enzyme refolding, and gel filtration
-
sMMO protein B wild-type and mutants recombinant from Escherichia coli by affinity chromatography, high salt concentration increases the binding stability between protein B and hydroxylase of sMMO
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative expression analysis
DNA and amino acid sequence determination and analysis. The sMMO gene cluster consists of the structural genes mmoXYBZDC, the regulatory genes mmoG and mmoR and another ORF orf1. These sMMO genes are transcribed as a single unit from a s54-dependent promoter located upstream of mmoX
DNA sequence analysis; overexpression of an additional protein component D of sMMO encoded by orfY as thioredoxin-fusion protein with His-Tag in Escherichia coli, protein component D is termed MMOD
-
expressed in Escherichia coli
expression in Escherichia coli, determination of complete sMMO DNA gene sequence, phylogenetic analysis
-
expression of component protein B of sMMO as glutathione-S-transferase fusion protein in Escherichia coli
-
expression of His-tagged triple mutant G10A/G13Q/G16A and G13Q mutant in Escherichia coli
-
gene mmoX, DNA and amino acid sequence determination and analysis; gene mmoX, DNA and amino acid sequence determination and analysis; gene mmoX, DNA and amino acid sequence determination and analysis
mutants are expressed in sMMO-negative cells of Methylosinus trichosporium
-
transcription of sMMO is repressed at Cu2+ concentration above 0.00086 mM per g dry cell weight
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activity of pMMO in whole cells is approximately 10fold greater than that of the purified sample
-
activity of pMMO in whole cells is approximately 10fold greater than that of the purified sample; the sMMO enzyme is expressed when cells are essentially starved for copper and the copper-to-biomass ratio is low (less than 0.0002 mM Cu2+)
-
-
necessary for the expression are a sigma(54)-dependent transcriptional activator, MmoR, and a putative GroEL-like chaperone, MmoG
-
sMMO is expressed at low copper/biomass ratios
the sMMO enzyme is expressed when cells are essentially starved for copper and the copper-to-biomass ratio is low (less than 0.0002 mM Cu2+)
transcription of sMMO is arrested in cells exposed to high levels of copper ions and sMMO mRNA transcripts are not detected 15 min after the addition of CuSO4
the sMMO enzyme is expressed when cells are essentially starved for copper and the copper-to-biomass ratio is low (less than 0.0002 mM Cu2+)
-
the sMMO enzyme is expressed when cells are essentially starved for copper and the copper-to-biomass ratio is low (less than 0.0002 mM Cu2+)
-
the sMMO enzyme is expressed when cells are essentially starved for copper and the copper-to-biomass ratio is low (less than 0.0002 mM Cu2+)
-
the sMMO enzyme is expressed when cells are essentially starved for copper and the copper-to-biomass ratio is low (less than 0.0002 mM Cu2+)
-
-
the sMMO enzyme is expressed when cells are essentially starved for copper and the copper-to-biomass ratio is low (less than 0.0002 mM Cu2+)
-
-
transcription of sMMO is arrested in cells exposed to high levels of copper ions and sMMO mRNA transcripts are not detected 15 min after the addition of CuSO4
-
transcription of sMMO is arrested in cells exposed to high levels of copper ions and sMMO mRNA transcripts are not detected 15 min after the addition of CuSO4
-
transcription of sMMO is arrested in cells exposed to high levels of copper ions and sMMO mRNA transcripts are not detected 15 min after the addition of CuSO4
-
transcription of sMMO is arrested in cells exposed to high levels of copper ions and sMMO mRNA transcripts are not detected 15 min after the addition of CuSO4
-
-
transcription of sMMO is arrested in cells exposed to high levels of copper ions and sMMO mRNA transcripts are not detected 15 min after the addition of CuSO4
-
-
transcription of sMMO is arrested in cells exposed to high levels of copper ions and sMMO mRNA transcripts are not detected 15 min after the addition of CuSO4
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G10A/G13Q/G16A
-
His-tagged protein B of sMMO, triple mutant is resistant to degradation in contrast to the wild-type, N-terminus is responsible for unusual mobility in size exclusion chromatography and proteolytic sensitivity of protein B; reduced activity
G13Q
G10A/G13Q/G16A
-
His-tagged protein B of sMMO, triple mutant is resistant to degradation in contrast to the wild-type, N-terminus is responsible for unusual mobility in size exclusion chromatography and proteolytic sensitivity of protein B; reduced activity
-
G13Q
-
reduced activity; sMMO, alteration of a cleavage site in component protein B
-
A115C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
A62C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview, the mutant MMOH-MMOB complex is perturbed by salts but not nonionic detergents
D71C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
D87C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
G119C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
K15C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
K44C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
L110C
-
mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl, and ethylbenzene as a substrate compared to the wild type enzyme
L110G
-
mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl, and ethylbenzene as a substrate compared to the wild type enzyme
L110R
-
mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl, and ethylbenzene as a substrate compared to the wild type enzyme
L110Y
-
mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl and ethylbenzene as a substrate compared to the wild type enzyme
R133C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
S109C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
T111C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
T111Y
V39C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
V68C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
Y102C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
additional information
G13Q
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enhanced temperature stability compared to wild-type, site-directed mutagenesis; sMMO, alteration of a cleavage site in component protein B
G13Q
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reduced activity; sMMO, alteration of a cleavage site in component protein B
T111Y
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mutant enzyme with increased rate constant for the reaction of large substrates such as ethane, furan, and nitrobenzene with the reactive MMOH (regulatory componant of the enzyme) intermediate Q while decreasing the rate constant for the reaction with methane. The regiospecificity for nitrobenzene oxidation is altered and 10fold more T111Y than wild-type MMOB is required to maximize the rate of turnover
T111Y
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the T111Y variant of MMOB causes only a small increase in reactivity
additional information
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native parallel occurence of full length and 2 N-terminal truncated forms of regulatory component protein B of sMMO, truncated forms are inactive
additional information
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mutagenesis of MMOB potentially broadening the substrate range of the enzyme
additional information
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construction of deletion mutants of subunit MMOB missing 5, 8, and 13 C-terminal residues, the mutations cause progressive decreases in the maximum steady-state turnover number, as well as lower apparent rate constants for formation of the key reaction cycle intermediate compound Q, the deletions result in substantial uncoupling at or before the P intermediate due to competition between slow H2O2 release from one of the intermediates and the reaction that carries this intermediate on to the next step in the cycle, which is slowed by the mutation
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme component MMOB from Escherichia coli is solubilized from the 12000 x g pellet with 8 M urea, followed by dilution to 1 mg/ml protein for enzyme refolding
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
degradation
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sMMO can be used for biodegradation of mixtures of chlorinated solvents, i.e., trichloroethylene, trans-dichloroethylene, and vinyl chloride. If the concentrations are increased to 0.1 mM, sMMO-expressing cells grow slower and degrade less of these pollutants in a shorter amount of time than pMMO
synthesis
biotechnology
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high particulate methane monooxygenase activity may contribute to the synthesis of poly-beta-hydroxybutyrate in the cell, which may be used to improve the yield of poly-beta-hydroxybutyrate in methanotrophs
biotechnology
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high particulate methane monooxygenase activity may contribute to the synthesis of poly-beta-hydroxybutyrate in the cell, which may be used to improve the yield of poly-beta-hydroxybutyrate in methanotrophs
biotechnology
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high particulate methane monooxygenase activity may contribute to the synthesis of poly-beta-hydroxybutyrate in the cell, which may be used to improve the yield of poly-beta-hydroxybutyrate in methanotrophs. Poly-beta-hydroxybutyrate content of strain OB3b can reach the highest level in the shortest time as compared to other methanotrophs. Nutrients deficiency condition is beneficial for strain IMV3011 to synthesize PHB whereas it is not beneficial for other strains
biotechnology
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method by which sMMO can be produced by strain OB3b while growing on methanol in copper-containing medium
biotechnology
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methanol can be employed to produce large amounts of Methylosinus trichosporium biomass containing sMMO. Enzyme expression can be maintained during growth on methanol which may aid in the development of sMMO-based industrial and environmental processes
biotechnology
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high particulate methane monooxygenase activity may contribute to the synthesis of poly-beta-hydroxybutyrate in the cell, which may be used to improve the yield of poly-beta-hydroxybutyrate in methanotrophs
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synthesis
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cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode. The electrochemically driven enzyme shows the same catalytic activity and regulation by the protein component B (MMOB) as the natural NAD(P)H-driven reaction and may have the potential for development into economic NAD(P)H-independent oxygenation catalyst
synthesis
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the enzyme is a base or scaffold for design of small molecule catalysts for use in large scale methanol synthesis
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.25)
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