1.14.13.25: methane monooxygenase (soluble)
This is an abbreviated version!
For detailed information about methane monooxygenase (soluble), go to the full flat file.
Word Map on EC 1.14.13.25
-
1.14.13.25
-
methanotrophs
-
methanol
-
methylosinus
-
capsulatus
-
methylococcus
-
trichosporium
-
methane-oxidizing
-
methylocystis
-
ch4
-
methylomonas
-
dioxygen
-
dinuclear
-
methylobacter
-
trichloroethylene
-
methylomicrobium
-
alkane
-
diironii
-
ammonia-oxidizing
-
landfill
-
upland
-
antiferromagnetically
-
wetland
-
high-valent
-
non-motile
-
copper-containing
-
carboxylate-bridged
-
peat
-
copper-dependent
-
dicopper
-
ch3oh
-
nitrosomonas
-
cometabolic
-
diferrous
-
methanobactins
-
energy production
-
mixed-valent
-
gammaproteobacterial
-
sphagnum
-
t-rflp
-
seep
-
propene
-
synthesis
-
biotechnology
-
degradation
-
exafs
-
nitrify
-
peroxo
- 1.14.13.25
- methanotrophs
- methanol
- methylosinus
- capsulatus
- methylococcus
- trichosporium
-
methane-oxidizing
- methylocystis
- ch4
- methylomonas
- dioxygen
-
dinuclear
- methylobacter
- trichloroethylene
- methylomicrobium
- alkane
-
diironii
-
ammonia-oxidizing
-
landfill
-
upland
-
antiferromagnetically
-
wetland
-
high-valent
-
non-motile
-
copper-containing
-
carboxylate-bridged
-
peat
-
copper-dependent
-
dicopper
- ch3oh
- nitrosomonas
-
cometabolic
-
diferrous
-
methanobactins
- energy production
-
mixed-valent
-
gammaproteobacterial
- sphagnum
-
t-rflp
-
seep
- propene
- synthesis
- biotechnology
- degradation
-
exafs
-
nitrify
-
peroxo
Reaction
Synonyms
chcA, cytoplasmic methane monooxygenase, methane hydroxylase, methane mono-oxygenase, methane monooxygenase, methane monooxygenase hydroxylase, MmMmoC, MMO, MMO Bath, MMOB, MmoC, MMOH, MMOR, oxygenase, methane mono-, particulate methane monooxygenase, pMMO, sMMO, soluble methane monooxygenase, soluble methane monooxygenase hydroxylase
ECTree
1.14.13.25 methane monooxygenase (soluble)Advanced search results
results (
results (Substrates Products
Substrates Products on EC 1.14.13.25 - methane monooxygenase (soluble)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
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
cycloheptanecarboxylate + NADH + H+ + O2
trans-4-hydroxycycloheptane-1-carboxylate + NAD+ + H2O
cyclohexanecarboxylate + NADH + H+ + O2
trans-4-hydroxycyclohexane-1-carboxylate + NAD+ + H2O
cyclohexene + NAD(P)H + O2
epoxycyclohexane + 2-cyclohexen-1-ol + NAD(P)+ + H2O
-
-
-
?
cyclopentanecarboxylate + NADH + H+ + O2
trans-3-hydroxycyclopentane-1-carboxylate + NAD+ + 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
-
-
-
-
?
ethylbenzene + NAD(P)H + H+ + O2
?
molecular dynamics simulation to rationalize regioselective hydroxylation of aromatic substrates
-
-
?
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 + 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
-
-
-
-
?
propylene + NADH + H+ + O2
propylene oxide + NAD+ + H2O
-
-
-
?
pyridine + NAD(P)H + O2
pyridine N-oxide + NAD(P)+ + H2O
-
-
-
?
toluene + NAD(P)H + H+ + O2
?
molecular dynamics simulation to rationalize regioselective hydroxylation of aromatic substrates
-
-
?
toluene + NAD(P)H + H+ + O2
benzyl alcohol + cresol + NAD(P)+ + H2O
-
-
-
-
?
toluene + NAD(P)H + H+ + O2
benzyl alcohol + NAD(P)+ + H2O
-
-
-
?
toluene + NAD(P)H + H+ + O2
benzyl alcohol + p-cresol + 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 + H+ + O2
phenol + hydroquinone + NAD(P)+ + H2O
-
-
-
?
benzene + NAD(P)H + H+ + O2
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
-
-
-
?
cycloheptanecarboxylate + NADH + H+ + O2
trans-4-hydroxycycloheptane-1-carboxylate + NAD+ + H2O
-
-
-
-
?
cycloheptanecarboxylate + NADH + H+ + O2
trans-4-hydroxycycloheptane-1-carboxylate + NAD+ + H2O
Paraburkholderia terrae KU-64
-
-
-
-
?
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
-
-
-
?
cyclohexanecarboxylate + NADH + H+ + O2
trans-4-hydroxycyclohexane-1-carboxylate + NAD+ + H2O
-
-
-
-
?
cyclohexanecarboxylate + NADH + H+ + O2
trans-4-hydroxycyclohexane-1-carboxylate + NAD+ + H2O
Paraburkholderia terrae KU-64
-
-
-
-
?
cyclopentanecarboxylate + NADH + H+ + O2
trans-3-hydroxycyclopentane-1-carboxylate + NAD+ + H2O
-
-
-
-
?
cyclopentanecarboxylate + NADH + H+ + O2
trans-3-hydroxycyclopentane-1-carboxylate + NAD+ + H2O
Paraburkholderia terrae KU-64
-
-
-
-
?
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 + H+ + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
Methylococcus capsulatus Bath.
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
-
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
presentation of experimental and computational data consistent with an open-core structure for the key intermediate in methane oxidation
-
-
?
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 + H+ + O2
methanol + NAD+ + H2O
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + 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
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
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
?
-
multicomponent monooxygenase. The ferredoxin domain of the reductase binds to the canyon region of the hydroxylase, previously determined to be the regulatory protein binding site as well. The latter thus inhibits reductase binding to the hydroxylase and, consequently, intermolecular electron transfer from the reductase to the hydroxylase diiron active site. The binding competition between the regulatory protein and the reductase may serve as a control mechanism for regulating electron transfer, and other BMM enzymes are likely to adopt the same mechanism
-
-
?
additional information
?
-
-
multicomponent monooxygenase. The ferredoxin domain of the reductase binds to the canyon region of the hydroxylase, previously determined to be the regulatory protein binding site as well. The latter thus inhibits reductase binding to the hydroxylase and, consequently, intermolecular electron transfer from the reductase to the hydroxylase diiron active site. The binding competition between the regulatory protein and the reductase may serve as a control mechanism for regulating electron transfer, and other BMM enzymes are likely to adopt the same mechanism
-
-
?
additional information
?
-
the regulatory component (MMOB) of soluble methane monooxygenase (sMMO) has a unique N-terminal tail not found in regulatory proteins of other bacterial multicomponent monooxygenases. This N-terminal tail is indispensable for proper function, yet its solution structure and role in catalysis remain elusive. The oxidation state of the hydroxylase component, MMOH, modulates the conformation of the N-terminal tail in the MMOH-2MMOB complex, which in turn facilitates catalysis. The N-terminal tail switches from a relaxed, flexible conformational state to an ordered state upon MMOH reduction from the diiron(III) to the diiron(II) state
-
-
?
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
?
-
Methylococcus capsulatus Bath.
the regulatory component (MMOB) of soluble methane monooxygenase (sMMO) has a unique N-terminal tail not found in regulatory proteins of other bacterial multicomponent monooxygenases. This N-terminal tail is indispensable for proper function, yet its solution structure and role in catalysis remain elusive. The oxidation state of the hydroxylase component, MMOH, modulates the conformation of the N-terminal tail in the MMOH-2MMOB complex, which in turn facilitates catalysis. The N-terminal tail switches from a relaxed, flexible conformational state to an ordered state upon MMOH reduction from the diiron(III) to the diiron(II) state
-
-
?
additional information
?
-
Methylococcus capsulatus Bath.
multicomponent monooxygenase. The ferredoxin domain of the reductase binds to the canyon region of the hydroxylase, previously determined to be the regulatory protein binding site as well. The latter thus inhibits reductase binding to the hydroxylase and, consequently, intermolecular electron transfer from the reductase to the hydroxylase diiron active site. The binding competition between the regulatory protein and the reductase may serve as a control mechanism for regulating electron transfer, and other BMM enzymes are likely to adopt the same mechanism
-
-
?
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
?
-
-
sMMO expressed at low copper concentration shows low substrate specificity, while pMMO expressed at high copper concentration shows high substrate specificity
-
-
?
additional information
?
-
-
Methyloferula stellata AR4 is an aerobic acidophilic methanotroph, which, in contrast to most known methanotrophs but similar to Methylocella spp., possesses only a soluble methane monooxygenase
-
-
?
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 soluble methane monooxygenase receives electrons from NADH via its reductase MmoC for oxidation of methane. The NADH-dependent reductase MmoC produces only trace amounts of superoxide, but mainly hydrogen peroxide during uncoupled turnover reactions
-
-
-
additional information
?
-
-
the soluble methane monooxygenase receives electrons from NADH via its reductase MmoC for oxidation of methane. The NADH-dependent reductase MmoC produces only trace amounts of superoxide, but mainly hydrogen peroxide during uncoupled turnover reactions
-
-
-
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
?
-
-
enzyme sMMO shows oxidation ability of various substrates, including alkanes, alkenes, aromatics, heterocyclics, and chlorinated compounds
-
-
-
additional information
?
-
-
sMMO is known to oxidize a variety of hydrocarbons, including alkanes ranging from methane to octane. The presence of 1,6-hexanediol near the di-iron center can be explained by the opening of the cavity, mediated by the side-chain rearrangement of Leu110 and Phe188, both of which function together as a gate for substrate and product passage to the active site. While MMOB is known to connect cavities for substrate access, the MMOD-mediated cavity opening appears to be a consequence of MMOHbeta-NT dissociation and subsequent structural relaxation of MMOHalpha. Both substrate ingress and product egress may take place through the substrate access cavity and not through the pore located near the active site, at least for hydrocarbon chain substrates such as hexane
-
-
-
additional information
?
-
-
enzyme sMMO shows oxidation ability of various substrates, including alkanes, alkenes, aromatics, heterocyclics, and chlorinated compounds
-
-
-
additional information
?
-
-
sMMO is known to oxidize a variety of hydrocarbons, including alkanes ranging from methane to octane. The presence of 1,6-hexanediol near the di-iron center can be explained by the opening of the cavity, mediated by the side-chain rearrangement of Leu110 and Phe188, both of which function together as a gate for substrate and product passage to the active site. While MMOB is known to connect cavities for substrate access, the MMOD-mediated cavity opening appears to be a consequence of MMOHbeta-NT dissociation and subsequent structural relaxation of MMOHalpha. Both substrate ingress and product egress may take place through the substrate access cavity and not through the pore located near the active site, at least for hydrocarbon chain substrates such as hexane
-
-
-
additional information
?
-
Methylosinus sporium ATCC 35069
-
enzyme sMMO shows oxidation ability of various substrates, including alkanes, alkenes, aromatics, heterocyclics, and chlorinated compounds
-
-
-
additional information
?
-
Methylosinus sporium ATCC 35069
-
sMMO is known to oxidize a variety of hydrocarbons, including alkanes ranging from methane to octane. The presence of 1,6-hexanediol near the di-iron center can be explained by the opening of the cavity, mediated by the side-chain rearrangement of Leu110 and Phe188, both of which function together as a gate for substrate and product passage to the active site. While MMOB is known to connect cavities for substrate access, the MMOD-mediated cavity opening appears to be a consequence of MMOHbeta-NT dissociation and subsequent structural relaxation of MMOHalpha. Both substrate ingress and product egress may take place through the substrate access cavity and not through the pore located near the active site, at least for hydrocarbon chain substrates such as hexane
-
-
-
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
-
-
?
additional information
?
-
-
naphthalene assay for sMMO activity
-
-
?
additional information
?
-
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
a colorimetric assay is adopted for the sMMO activity detection of biofilm
-
-
-
