Information on EC 1.14.13.25 - methane monooxygenase (soluble)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
1.14.13.25
-
RECOMMENDED NAME
GeneOntology No.
methane monooxygenase (soluble)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
mechanism
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
mechanism
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
mechanism
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
structural model for component protein B of sMMO
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
kinetic model of protein component interaction
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
modeling of interaction between the different protein components of sMMO
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
reaction mechanism and regulation, catalytic cycle of sMMO, the enzyme complex causes quantum tunneling to dominate in CH 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
show the reaction diagram
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
show the reaction diagram
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 KohnSham density functional theory, overview
methylotrophic bacterium
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
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 CH bonds in methane and many other hydrocarbons
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
mechanism, modeling of interaction between the different protein components of sMMO, structural model for component protein B of sMMO, via diiron(IV) reaction intermediate Q, reaction mechanism of the soluble enzyme with different substrates, overview, 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, distribution of electrons in intermolecular electron-transfer intermediates, isomerization of the initial ternary complex is required for maximal electron-transfer rates, 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
Methylococcus capsulatus Bath
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
Methane metabolism
-
-
methane oxidation to methanol I
-
-
Microbial metabolism in diverse environments
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methane hydroxylase
-
-
-
-
methane mono-oxygenase
-
-
-
-
methane monooxygenase hydroxylase
-
-
methane monooxygenase hydroxylase
Methylosinus trichosporium IMV 3011
-
-
-
MMO
Methylococcus capsulatus Bath, Methylococcus capsulatus HD6T
-
-
-
MMO
Methylosinus sporium 5
-
-
-
MMO
synthetic construct
-
-
MMO Bath
Methylococcus capsulatus Bath
-
-
-
MMOB
-
cofactor-free, monomeric component of sMMO, has regulatory role in catalysis
MMOB
synthetic construct
-
-
MMOH
P22869 and P18798 and P11987
-
MMOH
P22869 and P18798 and P11987
diiron(II) center of the hydroxylase component of soluble methane monooxygenase
MMOH
Methylococcus capsulatus Bath
-
;
-
MMOH
-
hydroxylase component of sMMO, contains a binuclear nonheme iron active site that is essential for O2 activation and subsequent methane oxidation
MMOH
synthetic construct
-
-
MMOR
-
reductase component of sMMO, contains a FAD cofactor and a [2Fe-2S] cluster, is responsible for transferring the reducing equivalents from NAD(P)H to MMOH
oxygenase, methane mono-
-
-
-
-
particulate methane monooxygenase
Q2LI72
-
particulate methane monooxygenase
-
-
particulate methane monooxygenase
Methylococcus capsulatus Bath, Methylococcus capsulatus HD6T
-
-
-
particulate methane monooxygenase
-
-
particulate methane monooxygenase
-
-
particulate methane monooxygenase
-
-
particulate methane monooxygenase
methylotrophic bacterium
-
-
pMMO
-
particulate, membrane-bound enzyme form
pMMO
Methylococcus capsulatus Bath
-
; particulate, membrane-bound enzyme form; particulate, membrane-bound enzyme form
-
pMMO
Methylococcus capsulatus HD6T
-
-
-
pMMO
Methylocystis sp.
-
particulate, membrane-bound enzyme form
pMMO
Methylocystis sp. WI 14
-
particulate, membrane-bound enzyme form
-
pMMO
-
particulate, membrane-bound enzyme form
pMMO
methylotrophic bacterium
-
-
sMMO
-
-
sMMO
-
soluble, cytoplasmic enzyme form
sMMO
P22869 and P18798 and P11987
-
sMMO
P22869 and P18798 and P11987
the enzyme contains three protein components, a 251 kDa hydroxylase (MMOH), a 38.6 kDa reductase (MMOR), and a 15.9 kDa regulatory protein (MMOB) required to couple electron consumption with substrate hydroxylation at the catalytic diiron center of MMOH
sMMO
Methylococcus capsulatus Bath
-
soluble, cytoplasmic enzyme form; soluble, cytoplasmic enzyme form
-
sMMO
Methylococcus capsulatus HD6T
-
-
-
sMMO
Methylocystis sp.
-
-
sMMO
Methylocystis sp.
-
multicomponent enzyme; soluble, cytoplasmic enzyme form
sMMO
Methylocystis sp.
-
soluble, cytoplasmic enzyme form
sMMO
-
-
-
sMMO
Methylocystis sp. WI 14
-
soluble, cytoplasmic enzyme form
-
sMMO
E0WMN6, E0WMN7, E0WMN8
-
sMMO
Methyloferula stellata AR4T
E0WMN6
-
-
sMMO
Methyloferula stellata gen. nov., sp. nov.
-
-
-
sMMO
Methyloferula stellata LAY
E0WMN8
-
-
sMMO
Methyloferula stellata SOP9
E0WMN7
-
-
sMMO
-
soluble, cytoplasmic enzyme form
sMMO
Methylosinus trichosporium IMV 3011
-
-
-
sMMO
synthetic construct
-
-
soluble methane monooxygenase
-
-
soluble methane monooxygenase
Methylococcus capsulatus Bath, Methylococcus capsulatus HD6T
-
-
-
soluble methane monooxygenase
Methylocystis sp.
-
-
soluble methane monooxygenase
-
-
-
soluble methane monooxygenase
E0WMN6, E0WMN7, E0WMN8
-
soluble methane monooxygenase
Methyloferula stellata AR4T
E0WMN6
-
-
soluble methane monooxygenase
Methyloferula stellata gen. nov., sp. nov.
-
-
-
soluble methane monooxygenase
Methyloferula stellata LAY
E0WMN8
-
-
soluble methane monooxygenase
Methyloferula stellata SOP9
E0WMN7
-
-
soluble methane monooxygenase
-
-
soluble methane monooxygenase
-
-
-
soluble methane monooxygenase
-
-
soluble methane monooxygenase
-
-
soluble methane monooxygenase
-
-
soluble methane monooxygenase
-
-
soluble methane monooxygenase
E1CBX4
-
soluble methane monooxygenase
E1CBX4
-
-
soluble methane monooxygenase
synthetic construct
-
-
soluble methane monooxygenase hydroxylase
-
-
soluble methane monooxygenase hydroxylase
Methylococcus capsulatus Bath
-
-
-
soluble methane monooxygenase hydroxylase
-
-
soluble methane monooxygenase hydroxylase
Methylosinus trichosporium IMV 3011
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
51961-97-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
protein A fragment, gene pmoA; a gammaproteobacterium closely related to methanotrophs
SwissProt
Manually annotated by BRENDA team
alpha subunit and beta subunit and gamma subunit
P22869 and P18798 and P11987
UniProt
Manually annotated by BRENDA team
Bath; enzyme form sMMO
-
-
Manually annotated by BRENDA team
enzyme form sMMO
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus Bath
-
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus Bath
strain Bath
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus HD6T
; HD6T
-
-
Manually annotated by BRENDA team
Methylocystis sp.
-
-
-
Manually annotated by BRENDA team
Methylocystis sp.
enzyme form sMMO; methanotroph type II; strain WI 14
-
-
Manually annotated by BRENDA team
Methylocystis sp. WI 14
strain WI 14
-
-
Manually annotated by BRENDA team
; gene mmoX
-
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
alpha-subunit, strain LAY; isolated from acidic forest soil near Marburg, Germany, gene mmoX
UniProt
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Methyloferula stellata AR4T
-
-
-
Manually annotated by BRENDA team
Methyloferula stellata AR4T
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
Manually annotated by BRENDA team
Methyloferula stellata gen. nov., sp. nov.
gene mmoX
-
-
Manually annotated by BRENDA team
Methyloferula stellata LAY
alpha-subunit, strain LAY; isolated from acidic forest soil near Marburg, Germany, gene mmoX
UniProt
Manually annotated by BRENDA team
Methyloferula stellata SOP9
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
Manually annotated by BRENDA team
Methylosinus sporium 5
strain 5
-
-
Manually annotated by BRENDA team
; strains OB3b and IMV3011
-
-
Manually annotated by BRENDA team
enzyme form sMMO; strain OB3b
-
-
Manually annotated by BRENDA team
strain IMV 3011
-
-
Manually annotated by BRENDA team
strain OB3b, a type II methanotroph
-
-
Manually annotated by BRENDA team
Methylosinus trichosporium IMV 3011
strain IMV 3011
-
-
Manually annotated by BRENDA team
methylotrophic bacterium
-
-
-
Manually annotated by BRENDA team
alpha-subunit; a type I methanotroph
UniProt
Manually annotated by BRENDA team
alpha-subunit; a type I methanotroph
UniProt
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Methylococcus capsulatus M
-
pMMO consists of two protein components (NADH-OR and pMH) and is coupled to the electron transport chain
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,1,2,2-tetramethylcyclopropane + NADH + O2
?
show the reaction diagram
-
-
-
-
?
1-butene + NAD(P)H + O2
1,2-epoxybutane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
1-butene + NAD(P)H + O2
1,2-epoxybutane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
2,3-dimethylpentane + NAD(P)H + O2
3,4-dimethylpentan-2-ol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
2-methylpropane + NAD(P)H + O2
2-methylpropan-2-ol + 2-methylpropan-1-ol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
adamantane + NAD(P)H + O2
1-adamantanol + 2-adamantanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
ammonia + NAD(P)H + O2
hydroxylamine + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
ammonia + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
benzene + NAD(P)H + O2
cyclohexanol + phenol + hydroquinone + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
benzene + NAD(P)H + O2
cyclohexanol + phenol + hydroquinone + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
benzene + NAD(P)H + O2
phenol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
benzene + NAD(P)H + O2
phenol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
-
-
?
benzene + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
beta-pinene + NAD(P)H + O2
6,6-dimethylbicyclo[3.1.1]hept-2-ene-2-methanol + beta-pinene oxide + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
biphenyl + NAD(P)H + H+ + O2
2-hydroxybiphenyl + 4-hydroxybiphenyl + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
bromobenzene + NAD(P)H + O2
bromophenol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
?
bromomethane + NAD(P)H + O2
?
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
-
-
-
?
bromomethane + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
butane + NAD(P)H + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
butane + NAD(P)H + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
butane + NAD(P)H + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
-
only 2-butanol, sMMO
?
butylene + NAD(P)H + O2
butylene oxide + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
?
carbon monoxide + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
chlorobenzene + NAD(P)H + O2
chlorophenol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
?
chloromethane + NAD(P)H + O2
formaldehyde + NAD(P)+ + H2O + ?
show the reaction diagram
-
-
-
?
chloromethane + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
chloronaphthalene + NAD(P)H + O2
chloronaphthol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
?
chloropentane + NAD(P)H + O2
chloropentanol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
?
cis-1,3-dimethylcyclohexane + NAD(P)H + O2
3,5-dimethylcyclohexanol + 1-cis-3-dimethylcyclohexanol + NAD(P)+ + H2O + 1-trans-3-dimethylcyclohexanol
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
CO + NAD(P)H + O2
CO2 + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
CO + NAD(P)H + O2
CO2 + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
CO + NAD(P)H + O2
CO2 + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
?
cyclohexene + NAD(P)H + O2
epoxycyclohexane + 2-cyclohexen-1-ol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
cytochrome c + NAD(P)H + O2
reduced cytochrome c + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
-
?
dichloromethane + NAD(P)H + O2
CO + Cl- + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp. WI 14
-
sMMO
-
?
difluoromethane + NADH + O2
difluoromethanol + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
soluble enzyme
-
-
?
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
show the reaction diagram
-
no activity
-
-
-
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
dimethyl ether + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
ethane + NAD(P)H + O2
ethanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
ethane + NAD(P)H + O2
ethanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
ethane + NAD(P)H + O2
ethanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
ethane + NADH + O2
ethanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
ethane + NADH + O2
?
show the reaction diagram
-
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp. WI 14
-
sMMO
-
?
ethylbenzene + NAD(P)H + H+ + O2
1-phenylethanol + 3-ethylphenol + 4-ethylphenol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
fluorobenzene + NAD(P)H + O2
fluorophenol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
?
fluoromethane + NADH + O2
fluoromethanol + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
soluble enzyme
-
-
?
formate + NAD(P)H + O2
?
show the reaction diagram
-
assay with whole cells
-
-
?
furan + NAD(P)H + O2
?
show the reaction diagram
-
-
-
-
?
furan + NADH + O2
? + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
position of hydroxylation cannot be determined exactly
?
hexane + NAD(P)H + O2
1-hexanol + 2-hexanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
hexane + NAD(P)H + O2
1-hexanol + 2-hexanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
hexane + NAD(P)H + O2
1-hexanol + 2-hexanol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
position of hydroxylation cannot be determined exactly
?
isobutane + NAD(P)H + O2
2-methyl-1-propanol + 2-methyl-2-propanol + NADP+ + H2O
show the reaction diagram
-
-
-
?
isopentane + NAD(P)H + O2
2-methylbutan-1-ol + 3-methylbutan-1-ol + 2-methylbutan-2-ol + 3-methylbutan-2-ol + NADP+ + H2O
show the reaction diagram
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Methylosinus sporium 5
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
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
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp. WI 14
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylosinus trichosporium IMV 3011
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
Methylocystis sp.
-
-
-
-
-
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
Methylocystis sp., Methylococcus capsulatus Bath
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus HD6T
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + H+ + O2
methanol + H2O + NAD+
show the reaction diagram
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
methylotrophic bacterium
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
Q2LI72
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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 + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
modeling intermolecular electron transfer in the sMMO system, interconversion of rapid and slow electron-transfer pathways, overview
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
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
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
modeling intermolecular electron transfer in the sMMO system, interconversion of rapid and slow electron-transfer pathways, overview
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
methane + trans-dichloroethylene + vinyl chloride + trichloroethylene + ?
formaldehyde + ?
show the reaction diagram
-
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+
show the reaction diagram
-
substrate of intermediate species, Hperoxo and Q, kinetics, overview
-
-
?
methylamine + NADH + H+ + O2
hydroxymethylamine + H2O + NAD+
show the reaction diagram
-
substrate of intermediate species, Hperoxo and Q, kinetics, overview
-
-
?
methylcyanide + NADH + H+ + O2
hydroxymethylcyanide + H2O + NAD+
show the reaction diagram
-
substrate of intermediate species, Hperoxo and Q, kinetics, and proposed mechanism of CH3CN hydroxylation by Hperoxo, overview
-
-
?
naphthalene + NAD(P)H + H+ + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
show the reaction diagram
-
oxidized by sMMO
-
-
?
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
show the reaction diagram
Methylomonas sp., Methylococcus capsulatus HD6T
-
-
-
-
?
nitrobenzene + NADH + O2
nitrophenol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
nitrobenzene + NADH + O2
nitrophenol + NAD+ + H2O
show the reaction diagram
-
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
-
-
?
nitromethane + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
octane + NAD(P)H + O2
1-octanol + 2-octanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
pentane + NAD(P)H + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
pentane + NAD(P)H + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
pentane + NAD(P)H + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
position of hydroxylation cannot be determined exactly
?
phenylalanine + NAD(P)H + O2
tyrosine + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp., Methylocystis sp. WI 14
-
-
only 2-propanol, sMMO
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus HD6T
-
-
-
-
?
propene + NADH + H+ + O2
epoxypropane + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
propylaldehyde + NADH + H+ + O2
? + H2O + NAD+
show the reaction diagram
-
substrate of intermediate species, Hperoxo and Q, kinetics, overview
-
-
?
propylene + duroquinol + O2
propylene oxide + reduced duroquinol + H2O
show the reaction diagram
-
-
-
-
?
propylene + NAD(P)H + O2
propylene oxide + NADP+ + H2O
show the reaction diagram
-
enzyme form sMMO
-
?
propylene + NAD(P)H + O2
propylene oxide + NADP+ + H2O
show the reaction diagram
Methylocystis sp.
-
enzyme form sMMO
-
?
propylene + NAD(P)H + O2
propylene oxide + NADP+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
enzyme form sMMO
-
?
propylene + NADH + H+ + O2
propylene epoxide + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
propylene + NADH + O2
propylene oxide + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
propylene + NADH + O2
propylene oxide + NAD+ + H2O
show the reaction diagram
-
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
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
propylene + NADH + O2
propylene oxide + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
the peroxodiiron(III) intermediate that precedes Q formation in the catalytic cycle has been demonstrated to react with propylene
-
-
?
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
show the reaction diagram
Methylosinus trichosporium IMV 3011
-
-
-
-
?
propylene + NADH + O2
propylene + NADH + O2
show the reaction diagram
-
-
-
-
?
pyridine + NAD(P)H + O2
pyridine N-oxide + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
pyridine + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
styrene + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
toluene + NAD(P)H + H+ + O2
benzyl alcohol + cresol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
toluene + NAD(P)H + O2
cresol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
?
toluene + NAD(P)H + O2
benzyl alcohol + cresol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
toluene + NAD(P)H + O2
benzyl alcohol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
trichloromethane + NAD(P)H + O2
CO2 + Cl- + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
trichloromethane + NADH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
xylene + NAD(P)H + O2
xylenol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
sMMO
-
?
methylene cyclohexane + NAD(P)H + O2
1-cyclohexane-1-methanol + methylene cyclohexane oxide + 4-hydroxymethylene cyclohexane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
additional information
?
-
-
broad specificity
-
-
-
additional information
?
-
-
very non-specific oxygenase
-
-
-
additional information
?
-
-
oxidation of norborneols, oxidation of deuterated compounds
-
-
-
additional information
?
-
Methylocystis sp.
-
sMMO expressed at low copper concentration shows low substrate specificity, while pMMO expressed at high copper concentration shows high substrate specificity
-
-
-
additional information
?
-
-
cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode
-
-
-
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
?
-
-
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
?
-
-
effects of spin-traps on MMO activity, overview
-
-
-
additional information
?
-
-
fluoroform is no substrate
-
-
-
additional information
?
-
-
inactive toward anthracene and phenanthrene
-
-
-
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, 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
?
-
Methylococcus capsulatus Bath
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
Methylococcus capsulatus Bath
-
very non-specific oxygenase
-
-
-
additional information
?
-
Methylococcus capsulatus Bath
-
broad specificity
-
-
-
additional information
?
-
Methylococcus capsulatus Bath
-
fluoroform is no substrate
-
-
-
additional information
?
-
Methylococcus capsulatus Bath
-
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
?
-
Methylococcus capsulatus Bath
-
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 HD6T
-
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
?
-
Methylocystis sp. WI 14
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
formate + NAD(P)H + O2
?
show the reaction diagram
-
assay with whole cells
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
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
show the reaction diagram
Methylosinus trichosporium IMV 3011
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + H+ + O2
methanol + H2O + NAD+
show the reaction diagram
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath, Methylomicrobium album BG8, Methylocystis sp. M
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
methylotrophic bacterium
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
Q2LI72
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
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
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
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
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
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
?
-
-
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
?
-
Methylococcus capsulatus, Methylomicrobium album, Methylocystis sp., Methylococcus capsulatus Bath
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
-
additional information
?
-
Methylococcus capsulatus Bath
-
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
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome c
-
one of three protein components is a soluble CO-binding cytochrome c
FAD
-
protein C, reductase component: contains 1 mol FAD per mol protein
FAD
-
characterization of FAD redox centre of component C
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
-
bound to the MMOR enzyme component
FAD
-
binds to the enzyme reductase protein MMOR
NADH
-
preferred
NADH
Methylocystis sp.
-
in vivo only NADH can be the electron donor
NADH
methylotrophic bacterium
-
-
NADH
-
binds to the enzyme hydroxylase protein MMOH
NADH
-
two-electron reduction of MMOHox by NADH mediated by MMOR enables further oxidation cycles
NADPH
Methylocystis sp.
-
only in vitro
NADPH
-
-
Ferredoxin
-
several MMOR ferredoxin analogues, intermolecular electron transfer from ferredoxin analogues to hydroxylase protein MMOH, redox potential determinations, overview
-
additional information
-
component B has no prosthetic group
-
additional information
-
-
-
additional information
-
component D contains no metal ions or organic cofactors
-
additional information
Methylocystis sp.
-
component B has no prosthetic group
-
additional information
-
cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode
-
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+
-
copper-containing protein component contains one copper atom per molecule; cytochrome component contains 0.3-0.8 atoms copper per molecule
Cu2+
-
copper genetically regulates the enzyme activity of the soluble and membrane-bound form
Cu2+
-
component C contains no copper
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+
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 KohnSham density functional theory, calculated coupling constants in calculation of Heisenberg coupling constants with Noodlemans Broken-Symmetry approach, computational method, optimized cluster structures, 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+
-
contains Fe2+
Fe2+
-
contains a diiron center
Iron
-
cytochrome component contains 1 atom iron per molecule
Iron
-
protein A, hydroxylase component: contains a binuclear iron center; protein C, reductase component: contains 1 [Fe2-S2]
Iron
-
2 mol Fe per mol enzyme; 4.3 mol Fe per mol enzyme
Iron
-
1 mol Fe per mol enzyme; 2.1 mol Fe per mol enzyme
Iron
-
2.8 mol Fe per mol protein
Iron
-
characterization of [Fe2-S2] redox centre of component C
Iron
-
2.3 mol Fe per mol protein
Iron
-
protein C, reductase component: contains 1 [Fe2-S2]
Iron
-
contains oxo-bridged binuclear iron clusters
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
-
1.3-1.5 atoms iron per molecule
Iron
-
a [2Fe-2S]cluster; contains hydroxo-bridged binuclear iron clusters; contains oxo-bridged binuclear iron clusters
Iron
Methylocystis sp.
-
3.6 mol of iron per mol of hydroxylase component A
Iron
Methylocystis sp.
-
component B of sMMO
Iron
-
active site diiron cluster
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
synthetic construct
-
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
Ni2+
-
protein B contains 0.04 mol Ni2+ per mol protein
Zn2+
-
component A, hydroxylase component: contains 0.5 mol zinc per mol protein
Zn2+
-
0.2-0.5 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
[2Fe-2S] cluster
-
bound to the MMOR enzyme component
Iron
synthetic construct
-
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
additional information
Methylocystis sp.
-
sMMO contains no metal ions
additional information
-
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+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-Dimercaptopropan-1-ol
-
-
2,4-Dichloro-(6-phenylphenoxy)ethylamine hydrochloride
-
-
2,4-Dichloro-(6-phenylphenoxy)ethylamine hydrochloride
-
no inhibition
2,4-Dichloro-(6-phenylphenoxy)ethyldiethylamine
-
-
2-mercaptoethanol
-
-
3-Amino-1,2,4-triazole
-
-
8-hydroxyquinoline
-
-
8-hydroxyquinoline
-
compound C not inhibited
Acetylene
-
component C not inhibited
Acetylene
-
complete inhibition at 0.1 mM
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
ammonium chloride
-
slightly
Cd2+
-
soluble enzyme form more than the membrane-bound form
Chloramphenicol
-
sMMO
Co2+
Methylocystis sp.
-
slightly, sMMO
Cu+
-
soluble enzyme form sMMO
Cu+
-
soluble enzyme form sMMO
Cu2+
-
soluble enzyme form, sMMO
Cu2+
-
copper ions irreversibly inhibit the activity of sMMO in vivo and in vitro by inactivating the reductase component
Cu2+
Methylocystis sp.
-
causes protein aggregation
Cu2+
-
soluble enzyme form, sMMO
Cu2+
-
loss of sMMO activity with copper addition to a culture growing on methanol. Recovery of sMMO activity by addition of allylthiourea
Dichloromethane
-
competitively in presence of formate
Dimercaptopropanol
-
-
Dithionite
-
34% inhibition at 5 mM
dithiothreitol
-
-
DTT
-
24% inhibition at 20 mM
ethyl carbamate
-
-
Fe2+
-
slightly, membrane-bound enzyme form
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
Fe3+
-
slightly, soluble enzyme form sMMO
Fe3+
-
slightly, soluble enzyme form sMMO
glycerol
-
40% inhibition at 15%
Hg2+
Methylocystis sp.
-
complete inhibition at 0.01 mM
N2
-
N2 atmosphere causes 28% inhibition
Ni2+
Methylocystis sp.
-
causes protein aggregation; sMMO
o-phenanthroline
-
-
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
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
-
Thiosemicarbazide
-
-
trichlorethylene
-
non-competitively; pMMO
Zn2+
Methylocystis sp.
-
causes protein aggregation; sMMO
methylamine
-
slightly
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
-
different chlorinated hydrocarbons cause different inhibition patterns
-
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
-
when cultivated in nutrients deficiency culture, activity of sMMO in strain OB3b decreases, whereas activity of sMMO in strain IMV3011 does not decrease
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
regulatory protein MMOB
-
the native regulatory protein MMOB is required for maximum enzyme activity
-
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
-
additional information
synthetic construct
-
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
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
methane
-
-
0.0064
NADH
Methylocystis sp.
-
sMMO component C reductase
0.0558
NADH
-
with methane
5.2
NADPH
Methylocystis sp.
-
sMMO component C reductase
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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 4C and 20C, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.23
propylene
-
25C, purified enzyme
additional information
additional information
-
turnover numbers of component A
-
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00011
-
purified enzyme, using propylene and duroquinol as substrates
0.0008
Methylocystis sp.
-
sMMO, substrate chloronaphthalene
0.0012
Methylocystis sp.
-
sMMO, substrate naphthalene
0.0029
-
membrane-bound enzyme, using propylene and NADH as substrates
0.003
-
membrane-bound enzyme, using propylene and duroquinol as substrates
0.0039
Methylocystis sp.
-
sMMO, substrate chloropentane
0.0122
Methylocystis sp.
-
sMMO, low copper growth concentration, growth substrate nitrate
0.0191
Methylocystis sp.
-
sMMO, substrate butylene
0.02 - 0.04
-
purified MMOH, substrate propylene
0.0254
Methylocystis sp.
-
sMMO, substrate propylene
0.0336
Methylocystis sp.
-
sMMO, substrate ethylene
0.072
-
component A
0.1
-
about, all 3 components individually
0.185
-
component A
0.205
Methylocystis sp.
-
sMMO, substrate diethylic ether
0.208
-
purified component A hydroxylase
0.265
-
protein A after reconstitution of iron
0.3 - 0.45
-
pH 7.0, 45C
0.334
Methylocystis sp.
-
sMMO, substrate propane
0.604
-
purified enzyme, substrate propylene
0.764
-
all components, substrate propene
1.66
-
sMMO protein B triple mutant G10A/G13Q/G16A
2.284
-
His-tagged sMMO protein B triple mutant G10A/G13Q/G16A
3.99
-
sMMO protein B mutant G13Q
5.09
-
sMMO, wild-type enzyme
5.71
-
purified component C
6
-
purified protein C
11.37
-
purified protein B
17.5
-
component C
26.1
-
purified enzyme, substrate propene
additional information
-
overview
additional information
-
-
additional information
-
-
additional information
-
recombinant shows higher activity than the wild-type
additional information
Methylocystis sp.
-
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
additional information
-
-
additional information
-
quantitative modeling of substrate hydroxylation via mixed quantum mechanics/molecular mechanics techniques, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.6
-
assay at
7
-
assay at; enzyme form sMMO
7.2
Methylocystis sp.
-
assay at
7.5
-
furan, propene
8.5 - 9
-
component C
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at; enzyme form sMMO
30
-
assay at, hydroxylase component
45
-
assay at, protein B
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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 4-33C with the optimum at 20-23C
Manually annotated by BRENDA team
additional information
Methyloferula stellata gen. nov., sp. nov., Methyloferula stellata SOP9, Methyloferula stellata LAY, Methyloferula stellata AR4T
-
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 4-33C with the optimum at 20-23C
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Methylocystis sp.
-
-
Manually annotated by BRENDA team
-
enzyme from cells grown under conditions of low copper availability
Manually annotated by BRENDA team
-
enzyme from cells grown under conditions of low copper availability
Manually annotated by BRENDA team
Methylocystis sp.
-
enzyme from cells grown under conditions of low copper availability
Manually annotated by BRENDA team
-
cytoplasmatic, soluble enzyme form termed sMMO
Manually annotated by BRENDA team
-
cytoplasmatic, soluble enzyme form termed sMMO
Manually annotated by BRENDA team
Methylocystis sp.
-
cytoplasmatic, soluble enzyme form termed sMMO
Manually annotated by BRENDA team
Methylosinus sporium 5
-
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus Bath
-
enzyme from cells grown under conditions of low copper availability, cytoplasmatic, soluble enzyme form termed sMMO
-
Manually annotated by BRENDA team
Methylococcus capsulatus HD6T
-
sMMO
-
Manually annotated by BRENDA team
Methylocystis sp. WI 14
-
enzyme from cells grown under conditions of low copper availability, cytoplasmatic, soluble enzyme form termed sMMO
-
Manually annotated by BRENDA team
methylotrophic bacterium
-
bound
Manually annotated by BRENDA team
-
membrane-bound particulate enzyme form termed pMMO
Manually annotated by BRENDA team
-
soluble enzyme, sMMO
-
Manually annotated by BRENDA team
Methylococcus capsulatus Bath
-
soluble enzyme, sMMO
-
-
Manually annotated by BRENDA team
Methyloferula stellata gen. nov., sp. nov., Methyloferula stellata SOP9, Methyloferula stellata LAY, Methylovulum miyakonense HT12, Methyloferula stellata AR4T
-
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9400
-
component: small protein, native PAGE
438921
13000
-
component: CO-binding cytochrome c, native PAGE
438921
15100
-
component B, gel filtration
438924
15800
-
component B containing FAD and [Fe2-S2]-cluster, gel filtration
438941
15850
-
component protein B of sMMO, mass spectrometry
438945, 438949
17000
-
component: protein B, gel filtration
438923
18000
Methylocystis sp.
-
component protein B of sMMO
438947
24000
-
component D of sMMO, forms homodimers, gel filtration
438943
32000
Methylocystis sp.
-
component B
438950
38000 - 38550
-
component: protein C, gel filtration
438923
38300 - 38400
-
component C: reductase, gel filtration
438924
39700
-
component C NADH-reductase, gel filtration
438941
40000
-
component C acceptor reductase
438925
41000
Methylocystis sp.
-
component C reductase of sMMO
438947
42000
-
component C
438939
47000
-
component: copper-containing protein, native PAGE
438921
201300
-
gel filtration
672690
210000
-
component A, analytical ultracentrifugation
438931
220000
-
component: protein A, gel filtration
438923
220000
-
component A: hydroxylase, gel filtration
438925
220000
-
component A: hydroxylase, gel filtration
438926
229000
Methylocystis sp.
-
component A hydroxylase of sMMO
438947
240000
-
component A hydroxylase
438935
241000 - 246000
-
protein A hydroxylase, gel filtration
438924
245000
-
protein A hydroxylase, gel filtration
438941
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
438921
additional information
-
enzyme system consists of 3 protein components A, B, C; see under subunits: molecular weights of the subunits of components
438922
additional information
-
enzyme system consists of 3 protein components A, B, C; see under subunits: molecular weights of the subunits of components
438923
additional information
-
enzyme system consists of 3 protein components A, B, C; see under subunits: molecular weights of the subunits of components
438924
additional information
-
enzyme system consists of 3 protein components A, B, C; see under subunits: molecular weights of the subunits of components
438925
additional information
-
enzyme system consists of 3 protein components A, B, C; see under subunits: molecular weights of the subunits of components
438926
additional information
-
see under subunits: molecular weights of the subunits of components
438931
additional information
-
enzyme system consists of 3 protein components A, B, C
438932
additional information
-
enzyme system consists of 3 protein components A, B, C; structure, review
438932
additional information
-
enzyme system consists of 3 protein components A, B, C
438932
additional information
-
complex formation of protein components; enzyme system consists of 3 protein components A, B, C
438933
additional information
-
enzyme system consists of 3 protein components A, B, C
438934, 438935
additional information
-
enzyme system consists of 3 protein components A, B, C
438938, 438939
additional information
Methylocystis sp.
-
sMMO is a multicomponent enzyme consisting of a hydroxylase, a protein B and a reductase
438947
additional information
-
protein B shows unusual behaviour in gel filtration
438949
additional information
Methylocystis sp.
-
sMMO is a multicomponent enzyme consisting of a hydroxylase, a protein B and a reductase
438950
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Methylocystis sp.
-
-
?
Methylocystis sp.
-
component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE
?
-
protein A: 2 * 54000-60630, alpha+ 2 * 42000-44720, beta + 2 * 17000-19840, gamma
?
-
component A: 2 * 56000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
?
-
component A: 2 * 55000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
?
-
component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation
?
-
component A: 2 * 54400 alpha, 2 * 43000 beta + 2 * 22700 gamma, sedimentation velocity, SDS-PAGE, amino acid analysis
?
Methylosinus sporium 5
-
component A: 2 * 56000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
-
?
Methylococcus capsulatus Bath
-
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
-
?
Methylocystis sp. WI 14
-
component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE
-
dimer
-
component D of sMMO: 2 * 12000, SDS-PAGE
dimer
Methylocystis sp.
-
component B: 2 * 15100, SDS-PAGE
dimer
Methylococcus capsulatus Bath
-
component D of sMMO: 2 * 12000, SDS-PAGE
-
heterotrimer
-
-
heterotrimer
-
1 * 42000 + 1 * 24000 + 1 * 22000, SDS-PAGE
hexamer
-
2 * 58000, alpha-subunit, + 2 * 36000, beta-subunit, + 2 * 23000, gamma-subunit, (alphabetagamma)2, SDS-PAGE
hexamer
Methylosinus trichosporium IMV 3011
-
2 * 58000, alpha-subunit, + 2 * 36000, beta-subunit, + 2 * 23000, gamma-subunit, (alphabetagamma)2, SDS-PAGE
-
additional information
-
complex formation of protein components
additional information
-
see under molecular weight for the size of the protein components
additional information
-
see under molecular weight for the size of the protein components
additional information
-
see under molecular weight for the size of the protein components
additional information
-
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
-
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
-
structure, review
additional information
-
3 components: 1 soluble CO-binding cytochrome c, 1 copper-containing protein, and 1 small protein, SDS-PAGE
additional information
-
component A is a hydroxylase
additional information
-
component A is a hydroxylase
additional information
Methylocystis sp.
-
sMMO is a multicomponent enzyme consisting of a hydroxylase, a protein B and a reductase
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
-
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
-
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 CH bond cleavage reaction for methane, selectively increasing the rate for this substrate, overview
additional information
Methylosinus sporium 5
-
see under molecular weight for the size of the protein components, enzyme system consists of 3 protein components A, B, C
-
additional information
Methylococcus capsulatus Bath
-
see under molecular weight for the size of the protein components, structure, review, enzyme system consists of 3 protein components A, B, C, component A is a hydroxylase, sMMO consists of 4 components: a hydroxylase, a reductase, a protein B and a protein D, 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
Methylosinus trichosporium IMV 3011
-
the enzyme mainly exists of alpha-helical regions, circular dichroism measurement
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
-
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
-
protein B, stable, rapid loss of activity above and below
438930
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
protein B, half-life: 10.2 min
438930
55
-
protein A, 10 min
438939
additional information
Methylocystis sp.
-
N-terminal truncated sMMO component B increases the heat stability of the sMMO hydroxylase
438950
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
5 mM thioglycollate, 5 mM dithiothreitol, 5 mM NADH stabilize component C at 0C
-
instability of enzyme in crude extract
-
protein A unstable to successive freezing and thawing
-
protein B stable to successive freezing and thawing
-
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
-
sMMO is more stable and easier to purify than pMMO
-
Fe2+ stabilizes component C of sMMO
Methylocystis sp.
-
instability of enzyme in crude extract
-
instability of the enzyme during purification is probably due to loss of iron
-
no component of the enzyme is stable to freezing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% glycerol, component A, stable for several weeks
-
0C, protein C, loss of 60-90% of activity within 20 h
-
0C, proteins A and B, stable for at least 24 h
-
4C, sMMO component C reductase, 90% loss of activity after 120 h, can be restored by Fe2+
Methylocystis sp.
-
sMMO component A hydroxylase is very unstable, splits into inactive subunits when stored frozen even for short periods
Methylocystis sp.
-
sMMO component protein B is stable when stored frozen
Methylocystis sp.
-
-80C, more than 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydroxylase component
-
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 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
-
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
-
component B of sMMO
Methylocystis sp.
-
sMMO with all components
Methylocystis sp.
-
protein A and C
-
3 components: a soluble CO-binding cytochrome c, a copper-containing protein, another small protein
-
hydroxylase component A
-
improved purification protocol using stabilizing agents
-
native enzyme 8.08fold by anion exchange chromatography, ultrafiltration, gel filtration, and again anion exchange chromatography, to 95% purity
-
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
-
Source 15Q column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative expression analysis
Q2LI72
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
-
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
-
expressed in Escherichia coli
Methylocystis sp.
-
expression in Escherichia coli, determination of complete sMMO DNA gene sequence, phylogenetic analysis
Methylocystis sp.
-
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
E0WMN6, E0WMN7, E0WMN8
expressed in Escherichia coli
-
mutants are expressed in sMMO-negative cells of Methylosinus trichosporium
-
overexpression of enzyme component MMOB in Escherichia coli
-
phylogenetic analysis
-
transcription of sMMO is repressed at Cu2+ concentration above 0.00086 mM per g dry cell weight
-
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
E1CBX4
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
activity of pMMO in whole cells is approximately 10fold greater than that of the purified sample
-
sMMO is expressed at low copper/biomass ratios
-
sMMO is produced when the copper/biomass ratio is low
-
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
Methylococcus capsulatus Bath
-
-
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+)
Methylococcus capsulatus Bath
-
-
activity of pMMO in whole cells is approximately 10fold greater than that of the purified sample
Methylococcus capsulatus Bath
-
-
sMMO is expressed at low copper/biomass ratios
Methylococcus capsulatus HD6T
-
-
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
Methylocystis sp.
-
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+)
Methylocystis sp.
-
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+)
-
-
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+)
-
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+)
-
-
sMMO is expressed at low copper/biomass ratios
-
necessary for the expression are a sigma(54)-dependent transcriptional activator, MmoR, and a putative GroEL-like chaperone, MmoG
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G10A/G13Q/G16A
-
reduced activity, 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
G13Q
-
reduced activity
G13Q
-
enhanced temperature stability compared to wild-type, site-directed mutagenesis
G10A/G13Q/G16A
Methylococcus capsulatus Bath
-
reduced activity, 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
-
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
R133C
-
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
-
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
-
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
-
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
-
the T111Y variant of MMOB causes only a small increase in reactivity
V39C
-
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
-
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
G13Q
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sMMO, alteration of a cleavage site in component protein B
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
G13Q
Methylococcus capsulatus Bath
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reduced activity, sMMO, alteration of a cleavage site in component protein B
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additional information
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mutagenesis of MMOB potentially broadening the substrate range of the enzyme
L110Y
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mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl and ethylbenzene as a substrate compared to the wild type 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
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
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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
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
biotechnology
Methylococcus capsulatus HD6T
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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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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
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
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
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
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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method by which sMMO can be produced by strain OB3b while growing on methanol in copper-containing medium