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Information on EC 1.14.99.39 - ammonia monooxygenase
for references in articles please use BRENDA:EC1.14.99.39
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.99 Miscellaneous
1.14.99.39 ammonia monooxygenase
IUBMB Comments
The enzyme catalyses the first reaction in the pathway of ammonia oxidation to nitrite. It contains copper , iron and possibly zinc . The enzyme requires two electrons, which are derived indirectly from the quinone pool via a membrane-bound donor.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 1.14.99.39
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ammonia-oxidizing
-
nitrification
- archaea
- nitrosomonas
-
nitrify
- rrna
-
wastewater
- europaea
- nitrosospira
-
ecosystem
-
reactor
- sludge
- methane
-
ocean
-
nitrous
-
coastal
- thaumarchaeota
- crenarchaeota
-
nitrite-oxidizing
-
autotroph
- n2o
-
wetland
-
phylotypes
-
comammox
-
full-scale
-
eutrophic
- oligotropha
-
crenarchaeal
-
microcosm
-
thaumarchaeal
-
t-rflp
-
estuary
-
betaproteobacterial
-
estuarine
- maritimus
-
anammox
- nitrosococcus
- nitrososphaera
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cometabolic
- methanotrophs
-
biogeochemical
- nitrosopumilus
- analysis
-
biofilter
-
chemolithotrophic
- environmental protection
-
wwtps
-
micropollutants
- nitrobacter
-
methane-oxidizing
-
methylococcus
-
bathypelagic
Reaction Schemes
show+
a reduced acceptor
+
=
+
an acceptor
+
Synonyms
ammonia monooxygenase, cummo, amo-ne, copper-containing membrane-bound monooxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ammonia monooxygenase
AMO
AMO-Ne
amoA
AmoB
copper-containing membrane-bound monooxygenase
CuMMO
low-temperature ammonia monooxygenase
amoA
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copper-containing membrane-bound monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NH3 + a reduced acceptor + O2 = NH2OH + an acceptor + H2O
mechanism, active-site model for ammonia monooxygenase consisting of an NH3-binding site and a second site that binds noncompetitive inhibitors, with oxidation occurring at either site
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NH3 + a reduced acceptor + O2 = NH2OH + an acceptor + H2O
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
ammonia oxidation I (aerobic), ammonia oxidation III
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CAS REGISTRY NUMBER
COMMENTARY
95990-35-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ammonia + AH2 + O2
NH2OH + A + H2O
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Substrates: anaerobic ammonia oxidation
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ammonia + AH2 + O2
NH2OH + A + H2O
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Substrates: electron transfer during the oxidation
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ammonia + AH2 + O2
NH2OH + A + H2O
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Substrates: anaerobic ammonia oxidation
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ammonia + AH2 + O2
NH2OH + A + H2O
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Substrates: -
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ammonia + AH2 + O2
NH2OH + A + H2O
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Substrates: anaerobic ammonia oxidation
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ammonia + AH2 + O2
NH2OH + A + H2O
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Substrates: under both oxic and anoxic conditions, the enzyme is responsible for the oxidation of ammonia to hydroxylamine. NO and NO2 are assumed to act as additional oxidants
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ammonia + AH2 + O2
NH2OH + A + H2O
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Substrates: test of electron donors to ammonia monooxygenase in whole cells of Nitrosomonas europaea. Positive results are obtained with tri- and tetramethylhydroquinone
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ammonia + asulam + O2
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Substrates: -
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ethylene + a reduced acceptor + O2
? + an acceptor + H2O
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ethylene + a reduced acceptor + O2
? + an acceptor + H2O
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NH3 + a reduced acceptor + O2
NH2OH + an acceptor + H2O
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Substrates: -
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NH3 + a reduced acceptor + O2
NH2OH + an acceptor + H2O
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Substrates: -
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NH3 + a reduced acceptor + O2
NH2OH + an acceptor + H2O
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NH3 + a reduced acceptor + O2
NH2OH + an acceptor + H2O
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Substrates: -
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NH3 + a reduced acceptor + O2
NH2OH + an acceptor + H2O
Substrates: -
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NH3 + AH2 + O2
NH2OH + A + H2O
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Substrates: -
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NH3 + duroquinol + O2
NH2OH + duroquinone + H2O
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NH3 + duroquinol + O2
NH2OH + duroquinone + H2O
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additional information
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Substrates: the enzyme can catalyze the oxidation of ammonium without stabilizing agents in vitro at low temperatures
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Substrates: the enzyme catalyzes the oxidation of ammonium without stabilizing agents in vitro at low temperature
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Substrates: the enzyme can catalyze the oxidation of ammonium without stabilizing agents in vitro at low temperatures
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Substrates: the enzyme catalyzes the oxidation of ammonium without stabilizing agents in vitro at low temperature
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additional information
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Substrates: methyl fluoride and dimethyl ether are converted to formaldehyde and a mixture of methanol and formaldehyde, respectively by ammonia monooxygenase
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additional information
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Substrates: active-site model for ammonia monooxygenase consisting of an NH3-binding site and a second site that binds noncompetitive inhibitors, with oxidation occurring at either site
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additional information
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Substrates: ammonia monooxygenase of Nitrosomonas europaea catalyzes the oxidation of alkanes (up to C8) to alcohols and alkenes (up to C5) to epoxides and alcohols in the presence of ammonium ions. Straight-chain, N-terminal alkynes (up to C10) all exhibit a time-dependent inhibition of ammonia oxidation without effects on hydrazine oxidation
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additional information
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Substrates: the affinity of the enzyme for NO2/N2O is higher than for O2. NO2 might be a suitable oxidant for aerobic ammonia oxidation as well
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additional information
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Substrates: identification of organic oxidation products and comparison of the reactivities of monohalogenated ethanes and n-chlorinated C1 to C4 alkanes for oxidation by whole cells of Nitrosomonas europaea. The dehalogenating potential of the ammonia monooxygenase in Nitrosomonas europaea may have practical applications for the detoxification of contaminated soil and groundwater
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additional information
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Substrates: enzyme AMO-Ne in whole cells produces 1- and 2-alcohols from C4-C8n-alkanes, the regioselectivity is dependent on the length of the carbon chain. 2-Alcohols produced from C4-C7n-alkanes are predominantly either the R- or S-enantiomers, while 2-octanol produced from n-octane is racemic. AMO-Ne can discriminate between the prochiral hydrogens at the C-2 position, with the degree of discrimination varying according to the n-alkane, and AMO-Ne shows a distinct ability to discriminate between the orientation of n-butane and n-pentane in the catalytic site, as compared to the particulate methane monooxygenase (pMMO, EC 1.14.18.3) of Methylococcus capsulatus (Bath) and that of Methylosinus trichosporium OB3b
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Substrates: enzyme AMO-Ne in whole cells produces 1- and 2-alcohols from C4-C8n-alkanes, the regioselectivity is dependent on the length of the carbon chain. 2-Alcohols produced from C4-C7n-alkanes are predominantly either the R- or S-enantiomers, while 2-octanol produced from n-octane is racemic. AMO-Ne can discriminate between the prochiral hydrogens at the C-2 position, with the degree of discrimination varying according to the n-alkane, and AMO-Ne shows a distinct ability to discriminate between the orientation of n-butane and n-pentane in the catalytic site, as compared to the particulate methane monooxygenase (pMMO, EC 1.14.18.3) of Methylococcus capsulatus (Bath) and that of Methylosinus trichosporium OB3b
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Substrates: the free ethynyl group of the inactive enzyme-inactivator adduct is conjugated with either a visualization tag (e.g., Alexa Fluor 647 azide) or an affinity purification tag (e.g., biotin-azide) using a copper-catalyzed azide-alkyne cycloaddition (CuAAC) reaction. The resulting enzyme-probe-tag conjugant can then either be (i) visualized using IR fluorescence in SDS-PAGE or (ii) enriched by affinity chromatography, tryptically digested, and identified by LC-MS/MS
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additional information
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Substrates: the free ethynyl group of the inactive enzyme-inactivator adduct is conjugated with either a visualization tag (e.g., Alexa Fluor 647 azide) or an affinity purification tag (e.g., biotin-azide) using a copper-catalyzed azide-alkyne cycloaddition (CuAAC) reaction. The resulting enzyme-probe-tag conjugant can then either be (i) visualized using IR fluorescence in SDS-PAGE or (ii) enriched by affinity chromatography, tryptically digested, and identified by LC-MS/MS
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additional information
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Substrates: analysis of selectivity of ammonia monooxygenase from Nitrosomonas europaea (AMO-Ne) for the oxidation of C4-C8n-alkanes to the corresponding alcohol isomers, ability of enzyme AMO-Ne to recognize the n-alkane orientation within the catalytic site, overview
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additional information
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Substrates: analysis of selectivity of ammonia monooxygenase from Nitrosomonas europaea (AMO-Ne) for the oxidation of C4-C8n-alkanes to the corresponding alcohol isomers, ability of enzyme AMO-Ne to recognize the n-alkane orientation within the catalytic site, overview
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additional information
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Substrates: the free ethynyl group of the inactive enzyme-inactivator adduct is conjugated with either a visualization tag (e.g., Alexa Fluor 647 azide) or an affinity purification tag (e.g., biotin-azide) using a copper-catalyzed azide-alkyne cycloaddition (CuAAC) reaction. The resulting enzyme-probe-tag conjugant can then either be (i) visualized using IR fluorescence in SDS-PAGE or (ii) enriched by affinity chromatography, tryptically digested, and identified by LC-MS/MS
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additional information
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Substrates: enzyme AMO-Ne in whole cells produces 1- and 2-alcohols from C4-C8n-alkanes, the regioselectivity is dependent on the length of the carbon chain. 2-Alcohols produced from C4-C7n-alkanes are predominantly either the R- or S-enantiomers, while 2-octanol produced from n-octane is racemic. AMO-Ne can discriminate between the prochiral hydrogens at the C-2 position, with the degree of discrimination varying according to the n-alkane, and AMO-Ne shows a distinct ability to discriminate between the orientation of n-butane and n-pentane in the catalytic site, as compared to the particulate methane monooxygenase (pMMO, EC 1.14.18.3) of Methylococcus capsulatus (Bath) and that of Methylosinus trichosporium OB3b
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additional information
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Substrates: analysis of selectivity of ammonia monooxygenase from Nitrosomonas europaea (AMO-Ne) for the oxidation of C4-C8n-alkanes to the corresponding alcohol isomers, ability of enzyme AMO-Ne to recognize the n-alkane orientation within the catalytic site, overview
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ammonia + AH2 + O2
NH2OH + A + H2O
-
Substrates: anaerobic ammonia oxidation
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NH3 + a reduced acceptor + O2
NH2OH + an acceptor + H2O
-
Substrates: -
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?
NH3 + a reduced acceptor + O2
NH2OH + an acceptor + H2O
-
Substrates: -
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?
NH3 + a reduced acceptor + O2
NH2OH + an acceptor + H2O
Substrates: -
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?
NH3 + a reduced acceptor + O2
NH2OH + an acceptor + H2O
-
Substrates: -
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NH3 + a reduced acceptor + O2
NH2OH + an acceptor + H2O
Substrates: -
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additional information
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-
Substrates: enzyme AMO-Ne in whole cells produces 1- and 2-alcohols from C4-C8n-alkanes, the regioselectivity is dependent on the length of the carbon chain. 2-Alcohols produced from C4-C7n-alkanes are predominantly either the R- or S-enantiomers, while 2-octanol produced from n-octane is racemic. AMO-Ne can discriminate between the prochiral hydrogens at the C-2 position, with the degree of discrimination varying according to the n-alkane, and AMO-Ne shows a distinct ability to discriminate between the orientation of n-butane and n-pentane in the catalytic site, as compared to the particulate methane monooxygenase (pMMO, EC 1.14.18.3) of Methylococcus capsulatus (Bath) and that of Methylosinus trichosporium OB3b
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additional information
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-
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Substrates: enzyme AMO-Ne in whole cells produces 1- and 2-alcohols from C4-C8n-alkanes, the regioselectivity is dependent on the length of the carbon chain. 2-Alcohols produced from C4-C7n-alkanes are predominantly either the R- or S-enantiomers, while 2-octanol produced from n-octane is racemic. AMO-Ne can discriminate between the prochiral hydrogens at the C-2 position, with the degree of discrimination varying according to the n-alkane, and AMO-Ne shows a distinct ability to discriminate between the orientation of n-butane and n-pentane in the catalytic site, as compared to the particulate methane monooxygenase (pMMO, EC 1.14.18.3) of Methylococcus capsulatus (Bath) and that of Methylosinus trichosporium OB3b
Products: -
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additional information
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Substrates: enzyme AMO-Ne in whole cells produces 1- and 2-alcohols from C4-C8n-alkanes, the regioselectivity is dependent on the length of the carbon chain. 2-Alcohols produced from C4-C7n-alkanes are predominantly either the R- or S-enantiomers, while 2-octanol produced from n-octane is racemic. AMO-Ne can discriminate between the prochiral hydrogens at the C-2 position, with the degree of discrimination varying according to the n-alkane, and AMO-Ne shows a distinct ability to discriminate between the orientation of n-butane and n-pentane in the catalytic site, as compared to the particulate methane monooxygenase (pMMO, EC 1.14.18.3) of Methylococcus capsulatus (Bath) and that of Methylosinus trichosporium OB3b
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
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additional information
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-
Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
Products: -
Products: -
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additional information
?
-
Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
Products: -
Products: -
?
additional information
?
-
Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
Products: -
Products: -
?
additional information
?
-
Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
Products: -
Products: -
?
additional information
?
-
Substrates: ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome c1
-
the gamma-subunit of the alpha3beta3gamma3 enzyme is cytochrome c1
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
Iron
MgCl2
-
stimulates in vitro. Loss of enzyme activity upon lysis of Nitrosomonas europaea results from the loss of copper from the enzyme, generating a catalytically inactive, yet stable and activable, form of the enzyme
Zinc
-
the enzyme contains Cu (9.4 mol per mol enzyme), Fe (3.9 mol per mol enzyme), and Zn (0.5 to 2.6 mol per mol enzyme)
additional information
-
Zn2+, Co2+, Ni2+, Fe2+, Fe3+, Ca2+, Mg2+, Mn2+, Cr3+, and Ag+, are ineffective at stimulating AMO activity
copper
modeling of the CuB and CuC metal-binding sites. The CuB site is found at the bottom of a narrow cleft formed by the interfaces of AmoB and AmoC. The Cu(II) ion is found in a distorted square planar geometry
Cu2+
-
the enzyme contains Cu (9.4 mol per mol enzyme), Fe (3.9 mol per mol enzyme), and Zn (0.5 to 2.6 mol per mol enzyme)
Cu2+
-
the addition of CuCl2 to cell extracts results in 5- to 15-fold stimulation of ammonia-dependent O2 consumption, ammonia-dependent nitrite production, and hydrazine-dependent ethane oxidation. Two populations of AMO in cell extracts. The low, copper-independent (residual) AMO activity is completely inactivated by acetylene in the absence of exogenously added copper. The copper-dependent (activable) AMO activity is protected against acetylene inactivation in the absence of copper. However, in the presence of copper both populations of AMO are inactivated by acetylene
Iron
-
iron capable of forming the S = 3/2 complex is a catalytic component of ammonia monooxygenase of Nitrosomonas europaea, possibly a part of the oxygen-activating center
Iron
-
the enzyme contains Cu (9.4 mol per mol enzyme), Fe (3.9 mol per mol enzyme), and Zn (0.5 to 2.6 mol per mol enzyme)
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-dimethylcyclopropane
-
22 mM, 93% inhibition, mechanism-based inactivator, ammonia enhances the rate of inactivation
1,3-phenylenediamine
-
0.05 mM, 93% inhibition, mechanism-based inactivator, ammonia enhances the rate of inactivation
1,7-octadiyne
17OD, complete inhibition, inactivation of NH4+-dependent O2 uptake by Nitrosomonas europaea in a time- and concentration-dependent manner. The effects of 17OD are specific for ammonia-oxidizing activity (17OD has no inhibitory effect on NH2OH-dependent O2 uptake), and de novo protein synthesis is required to reestablish this activity in cells exposed to 17OD. NH4Cl does not protect against inactivation of ammonia-oxidizing activity by 17OD under the conditions tested. 17OD is an irreversible inactivator of AMO
1-hexyne
-
mechanism-based inactivator, ammonia enhances the rate of inactivation
3-hexyne
-
mechanism-based inactivator, ammonia enhances the rate of inactivation
allylsulfide
-
specific, mechanism-based inactivator, anaerobic conditions or the presence of allylthiourea protect the enzyme from inactivation, ammonia increases the rate of inactivation
chloramphenicol
rate of NO2- production by 1,7-octadiyne-untreated cells is about 30% lower in the presence of chloramphenicol
cyclopropyl bromide
-
0.007 mM, 97% inhibition, mechanism-based inactivator, ammonia slows the rate of inactivation
Dimethylsulfide
-
weak inhibitors of ammonia oxidation. Depletion of dimethylsulfide requires O2 and is prevented with either acetylene or allylthiourea
p-anisidine
-
0.05 mM, 98% inhibition, mechanism-based inactivator, ammonia enhances the rate of inactivation
rifampicin
rate of NO2- production by 1,7-octadiyne-untreated cells is about 15% lower in the presence of rifampin
Acetylene
-
mechanism-based inactivator, ammonia slows the rate of inactivation
Acetylene
-
mechanism-based inhibitor, specifically interacts with catalytically active ammonia monooxygenase
Acetylene
-
two populations of AMO in cell extracts. The low, copper-independent (residual) AMO activity is completely inactivated by acetylene in the absence of exogenously added copper. The copper-dependent (activable) AMO activity is protected against acetylene inactivation in the absence of copper. In the presence of copper both populations of AMO are inactivated by acetylene
Acetylene
-
His191 is part of the acetylene-activating site in AMO or at least directly neighbours this site
phenylacetylene
-
0.05 mM, 55% inhibition, specific and irreversible inhibitor, does not compete with NH3 for binding at the active site
additional information
-
not inhibitory: hex-1-yne, hep-1-yne, oct-1-yne
-
additional information
-
active-site model for ammonia monooxygenase consisting of an NH3-binding site and a second site that binds noncompetitive inhibitors, with oxidation occurring at either site
-
additional information
many alkynes are mechanism-based inactivators of AMO, activity-based protein profiling method for the enzyme using 1,7-octadiyneas a probe. Many organic compounds reversibly inhibit ammonia oxidation through their action as alternative substrates for AMO. These compounds include diverse alkanes, alkenes, aromatics, ethers, and halogenated compounds. The simplest organic AMO substrates, such as methane and ethylene, are competitive inhibitors of ammonia oxidation, while other substrates exhibit more complex inhibition patterns. Mechanism-based enzyme inactivation, overview. The free ethynyl group of the inactive enzyme-inactivator adduct is conjugated with either a visualization tag (e.g., Alexa Fluor 647 azide) or an affinity purification tag (e.g., biotin-azide) using a copper-catalyzed azide-alkyne cycloaddition (CuAAC) reaction. The resulting enzyme-probe-tag conjugant can then either be (i) visualized using IR fluorescence in SDS-PAGE or (ii) enriched by affinity chromatography, tryptically digested, and identified by LC-MS/MS
-
additional information
-
many alkynes are mechanism-based inactivators of AMO, activity-based protein profiling method for the enzyme using 1,7-octadiyneas a probe. Many organic compounds reversibly inhibit ammonia oxidation through their action as alternative substrates for AMO. These compounds include diverse alkanes, alkenes, aromatics, ethers, and halogenated compounds. The simplest organic AMO substrates, such as methane and ethylene, are competitive inhibitors of ammonia oxidation, while other substrates exhibit more complex inhibition patterns. Mechanism-based enzyme inactivation, overview. The free ethynyl group of the inactive enzyme-inactivator adduct is conjugated with either a visualization tag (e.g., Alexa Fluor 647 azide) or an affinity purification tag (e.g., biotin-azide) using a copper-catalyzed azide-alkyne cycloaddition (CuAAC) reaction. The resulting enzyme-probe-tag conjugant can then either be (i) visualized using IR fluorescence in SDS-PAGE or (ii) enriched by affinity chromatography, tryptically digested, and identified by LC-MS/MS
-
additional information
-
ordinary laboratory lighting inhibits ammonia monooxygenase over a period of 1 h. Acetylene is not an inhibitor at 1 mM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
Freshwater Ammonia-Oxidizing Archaea Retain amoA mRNA and 16S rRNA during Ammonia Starvation.
Starvation
Stress response of a marine ammonia-oxidizing archaeon informs physiological status of environmental populations.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0267
NH3
-
whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.52
NH3
-
whole cell assay, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
stoichiometry, ammonia and oxygen uptake, and catalytic kinetics of ammonia oxidation, using an optimized microrespirometry setup, Michaelis-Menten kinetic model, overview
-
additional information
additional information
-
stoichiometry, ammonia and oxygen uptake, and catalytic kinetics of ammonia oxidation using an optimized microrespirometry setup, overview. The ammonia oxidation kinetic does not obey a classical Michaelis-Menten model
-
additional information
additional information
-
stoichiometry, ammonia and oxygen uptake, and catalytic kinetics of ammonia oxidation using an optimized microrespirometry setup, overview
-
additional information
additional information
-
stoichiometry, ammonia and oxygen uptake, and catalytic kinetics of ammonia oxidation using an optimized microrespirometry setup, nitrite oxidation follows a two-site saturation kinetics, overview
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
30
15
-
the enzyme can catalyze the oxidation of ammonium without stabilizing agents in vitro at low temperatures
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 20
4 - 20
-
over 91% activity with in the range of 4-15°C, 15.1% of maximal activity at 20C, complete inactivation above 20°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
archeae living associated to the barrel sponge Xestospongia muta in Carribean reefs, gene amoA encoding the catalytic alpha-subunit of the AMO enzyme
-
-
brenda
gene amoA, uncultured archaeon; gene amoA, Thaumarchaeota
E5KWS2, E5KWS3, E5KWS5, E5KWS7, E5KWS8, E5KWT3, E5KWT6, E5KWT8, E5KWU2, E5KWU5, E5KWU9, E5KWV0, E5KWV5, E5KWV9, E5KWW3, E5KWW5, E5KWW8, E5KWW9, E5KWX4, E5KWY2, E5KWY3, E5KWY6, E5KWZ1, E5KWZ4, E5KX01, E5KX02, E5KX05, E5KX08, E5KX10
UniProt
brenda
water column and sedimentwater interface of the two freshwater lakes Plusssee and Schoehsee and the Baltic Sea
-
-
brenda
-
-
-
brenda
gene amoC1 encoding ammonia monoxygenase subunit C1; gene amoC1 encoding ammonia monoxygenase subunit C1
UniProt
brenda
gene amoC2 encoding ammonia monoxygenase subunit C2; gene amoC2 encoding ammonia monoxygenase subunit C2
UniProt
brenda
gene amoC3 encoding ammonia monoxygenase subunit C3; gene amoC3 encoding ammonia monoxygenase subunit C3
UniProt
brenda
genes amoA1 and amoA2 encoding ammonia monoxygenase subunits A1/A2; genes amoA1 and amoA2 encoding ammonia monoxygenase subunits A1/A2
UniProt
brenda
genes amoB1 and amoB2 encoding ammonia monoxygenase subunits B1/B2; genes amoB1 and amoB2 encoding ammonia monoxygenase subunits B1/B2
SwissProt
brenda
Q04507 i.e. subunit AmoA, Q04508 i.e. subunit AmoB
UniProt
brenda
Q04507 i.e. subunit AmoA, Q04508 i.e. subunit AmoB, H2VFU7 i.e subunit AmoC
UniProt
brenda
Q04507 i.e. subunit AmoA, Q04508 i.e. subunit AmoB
UniProt
brenda
Q04507 i.e. subunit AmoA, Q04508 i.e. subunit AmoB, H2VFU7 i.e subunit AmoC
UniProt
brenda
B0LKZ3 i.e. subunit AmoA, B0LKZ0 i.e. subunit AmoB, A9A4U4 i.e. subunit AmoC
B0LKZ3; B0LKZ0; A9A4U4
UniProt
brenda
fragment; multiple DNA samples drawn from nine coral species and four different reef locations are PCR screened for archaeal and bacterial amoA genes, and archaeal amoA gene sequences are obtained from five different species of coral collected in Bocas del Toro, Panama. The 210 coral-associated archaeal amoA sequences recovered in the study are broadly distributed phylogenetically, with most only distantly related to previously reported sequences from coastal/estuarine sediments and oceanic water columns
A5H9Z0, A5H9Z1, A5H9Z2, A5H9Z3, A5H9Z4, A5H9Z5, A5H9Z7, A5HA00, A5HA01, A5HA02, A5HA03, A5HA04, A5HA05, A5HA06, A5HA07, A5HA09, A5HA11, A5HA13, A5HA14, A5HA15, A5HA16, A5HA18, A5HA19, A5HA20, A5HA21, A5HA22, A5HA23, A5HA24, A5HA25, A5HA26, A5HA28, A5HA30, A5HA31, A5HA32, A5HA37, A5HA39, A5HA41, A5HA42, A5HA44, A5HA45, A5HA46, A5HA47, A5HA48, A5HA49, A5HA50, A5HA51, A5HA52, A5HA54, A5HA56, A5HA57, A5HA58, A5HA59, A5HA60, A5HA61, A5HA62, A5HA63, A5HA64, A5HA66, A5HA67, A5HA68, A5HA69, A5HA72, A5HA74, A5HA76, A5HA77, A5HA79, A5HA82, A5HA83, A5HA86, A5HA88, A5HA89, A5HA92, A5HA94, A5HA95, A5HA97, A5HA98, A5HAA0, A5HAA1, A5HAA4, A5HAA5, A5HAA6, A5HAA7, A5HAA9, A5HAB0, A5HAB1, A5HAB3, A5HAB4, A5HAB6, A5HAB7, A5HAB8, A5HAB9, A5HAC0, A5HAC8, A5HAC9, A5HAD1, A5HAD9, A5HAE2, A5HAE3, A5HAE5, A5HAE6, A5HAE7, A5HAE8, A5HAF0, A5HAF1, A5HAF2, A5HAF3, A5HAF6, A5HAF7, A5HAF8, A5HAG1, A5HAG2, A5HAG3, A5HAG4, A5HAG8, A5HAH1, A5HAH4, A5HAH5, A5HAH7, A5HAH9, A5HAI2, A5HAI3, A5HAI4, A5HAI7, A5HAI8, A5HAI9, A5HAJ2, A5HAJ3, A5HAJ5
SwissProt
brenda
from archaeal communities inhabiting the waste pile of the Sliven uranium mine and the soil of the Buhovo uranium mine in Bulgaria
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
cell growth conditions and ammonia/nitrite ratio, overview
brenda
additional information
-
cell growth conditions and ammonia/nitrite ratio, overview
-
brenda
additional information
-
cell growth conditions and ammonia/nitrite ratio, overview
brenda
additional information
-
cell growth conditions and ammonia/nitrite ratio, overview
-
brenda
additional information
-
cell growth conditions and ammonia/nitrite ratio, overview
brenda
additional information
-
cell growth conditions and ammonia/nitrite ratio, overview
-
brenda
additional information
-
cell growth conditions and ammonia/nitrite ratio, overview
brenda
additional information
-
bacterial community profiles and the abundance of the bacterial ammonia monooxygenase gene (amoA) are analyzed in composts produced from either food waste or cattle manure. Cattle manure composts show greater alpha diversity, contain higher amounts of various rRNA gene fragments than those of food waste composts and contain the amoA gene by relative quantification, and Proteobacteria are abundantly found and nitrifying bacteria are detected in it, quantitative expression analysis of amoA gene
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme resides in the cytoplasm of the bacteria in addition to its location in the membrane and is distributed approximately equally in both subcellular fractions
brenda
-
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
brenda
-
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
brenda
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
brenda
-
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
brenda
-
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
-
brenda
-
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
brenda
-
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
brenda
-
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
brenda
-
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
brenda
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
brenda
-
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
brenda
-
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
-
brenda
-
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
brenda
-
AmoB-protein is located in all genera (Nitrosomonas, Nitrosospira, Nitrosococcus, Methylococcus) on the cytoplasmic membrane. In cells of Nitrosomonas and Nitrosococcus additional but less AmoB-labeling is found on the intracytoplasmic membrane
-
brenda
-
the enzyme resides in the cytoplasm of the bacteria in addition to its location in the membrane and is distributed approximately equally in both subcellular fractions
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
particulate methane monooxygenase and ammonia monooxygenase are evolutionarily related enzymes despite their different physiological roles in these bacteria. Nitrosococcus oceonus AmoA shows higher identity to PmoA (methane monooxygenase) sequences from other members of the gamma-proteobacteria than to AmoA sequences
evolution
phylogenetic diversity of archaea and the archaeal ammonia monooxygenase gene in populations from uranium mining-impacted locations in Bulgaria, phylogenetic analysis. The main pollutants were Cu and Zn, U, Cr, As, Pb, and sulfates, dependent on the location, overview
evolution
-
the enzyme belongs to the ammonia monooxygenase (AMO)/particulate methane monooxygenase (pMMO) superfamily, copper membrane-associated monooxygenases (CuMOs), which is a diverse group of membrane-bound enzymes. The Ny_amoB structure reveals that the fold of the N-terminal domain of the B subunit in the AMO/pMMO superfamily is very well conserved as is the presence of an N-terminal copper binding site
evolution
-
nitrifying bacteria are responsible for ammonia oxidation and mainly belong to the Proteobacteria or Nitrospira phyla, comparison of bacterial community profiles among DNA libraries rom analyzed in Proteobacteria from composts produced from either food waste or cattle manure
evolution
-
reconstruction of AmoA protein sequence evolution during a major evolutionary transition to acidophily in the C14 lineage of Nitrosotalea, and ancestral reconstruction of sequence changes fixed in the AmoA protein during the evolutionary transition to acidophily in the C11 lineage of Nitrososphaera, AmoA protein evolution during ancestral pH adaptation events, nature of selection associated with AmoA evolution, overview. Three pH-adapted lineages are particularly important in terms of their high abundance in contemporary terrestrial ecosystems, i.e. the phylogenetically-distant acidophilic lineages called C11 (within Nitrososphaera) and C14/C15 (within Nitrosotalea) and the alkalinophilic lineage called C1/2 (within Nitrososphaera)
evolution
-
reconstruction of AmoA protein sequence evolution during a major evolutionary transition to acidophily in the C14 lineage of Nitrosotalea, and ancestral reconstruction of sequence changes fixed in the AmoA protein during the evolutionary transition to acidophily in the C11 lineage of Nitrososphaera, AmoA protein evolution during ancestral pH adaptation events, nature of selection associated with AmoA evolution, overview. Three pH-adapted lineages are particularly important in terms of their high abundance in contemporary terrestrial ecosystems, i.e. the phylogenetically-distant acidophilic lineages called C11 (within Nitrososphaera) and C14/C15 (within Nitrosotalea) and the alkalinophilic lineage called C1/2 (within Nitrososphaera)
evolution
-
reconstruction of AmoA protein sequence evolution during a major evolutionary transition to acidophily in the C14 lineage of Nitrosotalea, and ancestral reconstruction of sequence changes fixed in the AmoA protein during the evolutionary transition to acidophily in the C11 lineage of Nitrososphaera, AmoA protein evolution during ancestral pH adaptation events, nature of selection associated with AmoA evolution, overview. Three pH-adapted lineages are particularly important in terms of their high abundance in contemporary terrestrial ecosystems, i.e. the phylogenetically-distant acidophilic lineages called C11 (within Nitrososphaera) and C14/C15 (within Nitrosotalea) and the alkalinophilic lineage called C1/2 (within Nitrososphaera)
evolution
-
global phylogeny of archaeal amoA genes from cultivated and environmental ammonia-oxidizing archaea. amoA sequences show that the global frequency of ammonia-oxidizing archaea is extremely uneven, with few clades dominating ammonia-oxidizing archaea diversity in most ecosystems. Characterised ammonia-oxidizing archaea do not represent most predominant clades in nature, including soils and oceans. The functional role of the most prevalent environmental ammonia-oxidizing archaea clade remains unclear. Ammonia-oxidizing archaea harbour molecular signatures that possibly reflect phenotypic traits
malfunction
two copies of amoA (amoA1 and amoA2), they differ by one nucleotide. Either copy of amoA is sufficient to support growth when the other copy is disrupted. Inactivation of amoA1 results in slower growth
malfunction
two copies of amoA (amoA1 and amoA2), they differ by one nucleotide. Either copy of amoA is sufficient to support growth when the other copy is disrupted. Inactivation of amoA2 does not results in slower growth
metabolism
-
nitrification is a fundamental process in the marine nitrogen cycle that makes fixed nitrogen available in the form of nitrite and nitrate to primary producers and for denitrification and anaerobic ammonium oxidation. Nitrification results from the combination of two processes: ammonia oxidation and nitrite oxidation. The ammonia oxidation process starts with the oxidation of ammonia to hydroxylamine, which is catalyzed by ammonia monoxygenase, AMO
metabolism
Nitrosomonas europaea is an aerobic nitrifying bacterium that oxidizes ammonia (NH3) to nitrite (NO2-) through the sequential activities of ammonia monooxygenase (AMO) and hydroxylamine dehydrogenase (HAO)
metabolism
B0LKZ3; B0LKZ0; A9A4U4
cells rapidly deplete transcripts for the A and B subunits of ammonia monooxygenase in response to ammonia starvation, yet retain relatively high levels of transcripts for the C subunit
metabolism
-
Nitrosomonas europaea is an aerobic nitrifying bacterium that oxidizes ammonia (NH3) to nitrite (NO2-) through the sequential activities of ammonia monooxygenase (AMO) and hydroxylamine dehydrogenase (HAO)
-
physiological function
AmoC3 is involved in the heat shock response. AmoC3 functions in part as an alternative stress response subunit that mediates the stability of ammonia monooxygenase during heat shock and other conditions that cause membrane stress or instability of the ammonia monooxygenase holoenzyme
physiological function
-
enzyme AMO converts ammonia to hydroxylamine in nitrifiers
additional information
-
Nitrosopumilus maritimus is adapted to grow on ammonia concentrations found in oligotrophic open ocean environments, far below the survival threshold of ammonia-oxidizing bacteria. The archaeal AMO oxidizes ammonia to hydroxylamine similar to the bacterial pathway
additional information
-
determination of archaeal diversity present in Caribbean giant barrel sponges undergoing cyclic and fatal bleaching, and the relative expression of the amoA gene in the different tissues, overview
additional information
enzyme expression in stress response, overview
additional information
enzyme expression in stress response, overview
additional information
enzyme expression in stress response, overview
additional information
enzyme expression in stress response, overview
additional information
enzyme expression in stress response, overview
additional information
-
enzyme expression in stress response, overview
additional information
AmoC subunit confers greater enzyme stability. Enzyme expression in stress response, overview
additional information
AmoC subunit confers greater enzyme stability. Enzyme expression in stress response, overview
additional information
AmoC subunit confers greater enzyme stability. Enzyme expression in stress response, overview
additional information
AmoC subunit confers greater enzyme stability. Enzyme expression in stress response, overview
additional information
AmoC subunit confers greater enzyme stability. Enzyme expression in stress response, overview
additional information
-
AmoC subunit confers greater enzyme stability. Enzyme expression in stress response, overview
additional information
-
the enzyme can catalyze the oxidation of ammonium without stabilizing agents in vitro at low temperatures
additional information
-
the pMMO active site is believed to reside in the soluble N-terminal region of the pmoB subunit. Modeling and structure comparisons of the N-terminal domain of the B subunit in the AMO/pMMO superfamily
additional information
-
the enzyme can catalyze the oxidation of ammonium without stabilizing agents in vitro at low temperatures
-
Show AA Sequence and Transmembrane Helices (146 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
-
3 * 27000 (alpha-subunit, AmoA) + 3 * 42000 (beta-subunit, AmoB) + 3 * 24000 (gamma-subunit, cytochrome c1), soluble enzyme, SDS-PAGE
27000
-
3 * 27000 (alpha-subunit, AmoA) + 3 * 42000 (beta-subunit, AmoB) + 3 * 24000 (gamma-subunit, cytochrome c1), soluble enzyme, SDS-PAGE
42000
-
3 * 27000 (alpha-subunit, AmoA) + 3 * 42000 (beta-subunit, AmoB) + 3 * 24000 (gamma-subunit, cytochrome c1), soluble enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
nonamer
-
3 * 27000 (alpha-subunit, AmoA) + 3 * 42000 (beta-subunit, AmoB) + 3 * 24000 (gamma-subunit, cytochrome c1), soluble enzyme, SDS-PAGE
additional information
-
different from the beta-subunit of membrane-bound ammonia monooxygenase, the beta-subunit of soluble ammonia monooxygenase possesses an N-terminal signal sequence
?
-
the membrane-bound, active-site-containing 27000 Da polypeptide of ammonia monooxygenase undergoes an aggregation reaction when cells or membranes are heated in the presence of SDS-PAGE. The aggregated protein can be returned to the monomeric state by incubation at high pH in the presence of SDS. Strongly hydrophobic amino acid sequences present in ammonia monooxygenase are responsible for the aggregation phenomenon
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant Ny_amoB, amino acids 31-186, sitting drop vapor diffusion method, mixing 0.001 ml of 5 mg/ml protein solution with 0.0035 ml of well solution containing 1 M (NH4)2SO4, 100 mM sodium formate, pH 4.0, and 2% PEG 8000, football shaped crystals appear within 2-3 days, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
-
structural model of ammonia monooxygenase, and its accessory proteins AmoD and AmoE. The alpha-helix of AmoC formed by residues 205-222 is found in the center of the AMO homotrimer of heterotrimers and, together with the subsequent loops, interacts with the analogous alpha-helix in the other AmoC monomers. In particular, Ser221 forms an H-bond with Glu217, and van der Waals interactions are formed between residues Leu206, Trp209, Gly210, His211, Phe213, Trp214, and Glu217 from one chain and Trp214, Phe215, Glu218, Ser221, Ala222, Leu224, and Trp226 from an adjacent chain
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of a amoC3 disruption mutant strain, starvation at low cell densities or in the presence of O2 differentially inhibits the recovery of the DELTAamoC3 strain
additional information
construction of a amoC3 disruption mutant strain, starvation at low cell densities or in the presence of O2 differentially inhibits the recovery of the DELTAamoC3 strain
additional information
construction of a amoC3 disruption mutant strain, starvation at low cell densities or in the presence of O2 differentially inhibits the recovery of the DELTAamoC3 strain
additional information
construction of a amoC3 disruption mutant strain, starvation at low cell densities or in the presence of O2 differentially inhibits the recovery of the DELTAamoC3 strain
additional information
construction of a amoC3 disruption mutant strain, starvation at low cell densities or in the presence of O2 differentially inhibits the recovery of the DELTAamoC3 strain
additional information
-
construction of a amoC3 disruption mutant strain, starvation at low cell densities or in the presence of O2 differentially inhibits the recovery of the DELTAamoC3 strain
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loss of AMO activity upon lysis of Nitrosomonas europaea results from the loss of copper from the enzyme, generating a catalytically inactive, yet stable and activable, form of the enzyme
-
the presence of bovine serum albumin (10 mg/ml) or CuCl2 (500 mM) stabilize ammonia-dependent O2 uptake activity for 2 to 3 days at 4°C
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
alcohol productions in C5-C8 n-alkane oxidtions by enzyme AMO-Ne, overview
additional information
-
alcohol productions in C5-C8 n-alkane oxidtions by enzyme AMO-Ne, overview
additional information
-
alcohol productions in C5-C8 n-alkane oxidtions by enzyme AMO-Ne, overview
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4-15°C, the purified enzyme activity is stable when stored at 4°C for five days, at 10°C for two days, and at 15°C for one day
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 9.7fold by by anion-exchange chromatography and gel filtration as membrane-bound monomer
-
recombinant C-terminally Strep-tagged protein, comprising amino acids 31-186, from Escherichia coli strain Rosetta-2 (DE3) by affinity chromatography, ultrafiltration, and gel filtration
-
the free ethynyl group of the inactive enzyme-inactivator adduct is conjugated with either a visualization tag (e.g., Alexa Fluor 647 azide) or an affinity purification tag (e.g., biotin-azide) using a copper-catalyzed azide-alkyne cycloaddition (CuAAC) reaction. The resulting enzyme-probe-tag conjugant can then either be (i) visualized using IR fluorescence in SDS-PAGE or (ii) enriched by affinity chromatography, tryptically digested, and identified by LC-MS/MS
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene amoA, DNA and amino acid sequence determination and analysis of partial archaeal 16S rRNA and amoA, phylogenetic analysis and tree
gene amoA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
-
gene amoA, encoding the enzyme alpha subunit, DNA and amino acid sequence determination and analysis, comparison of bacterial community profiles among DNA libraries
-
gene amoA, genotyping of forest peat soil bacteria possessing ammonia monooxygenase activity, DNA and amino acid sequence determination and analysis, classification and phylogenetic tree, overview
E5KWU5, E5KWU9, E5KWV0, E5KWV5, E5KWV9, E5KWW3, E5KWW5, E5KWW8, E5KWW9, E5KWX4, E5KWS2, E5KWY2, E5KWY3, E5KWY6, E5KWZ1, E5KWZ4, E5KX01, E5KX02, E5KX05, E5KX08, E5KX10, E5KWS3, E5KWS5, E5KWS7, E5KWS8, E5KWT3, E5KWT6, E5KWT8, E5KWU2
gene amoA, the amoCAB operon, having a prototypical C-A-B gene order, encodes ammonia monooxygenase, phylogenetic analysis and unrooted phylogenetic consensus tree
gene amoB, amino acids 31-186, sequence determination and analysis, recombinant expression as C-terminally Strep-tagged protein in Escherichia coli strain Rosetta-2 (DE3) using pASK-IBA2 vector
-
gene amoC1 encoding ammonia monoxygenase subunit C1, quantitative RT-PCR expression analysis
gene amoC2 encoding ammonia monoxygenase subunit C2, quantitative RT-PCR expression analysis
gene amoC3 encoding ammonia monoxygenase subunit C3, quantitative RT-PCR expression analysis
gene pmoA, design of a highly degenerate primer targeting copper-containing membrane-bound monooxygenase genes for community analysis of methane- and ammonia-oxidizing bacteria, two-step PCR strategy employing a tagged highly degenerate primer (THDP), designated THDP-PCR, method development and optimization, overview. DNA and amino acid sequence determination and analysis, phylogenetic analysis
genes amoA1 and amoA2 encoding ammonia monoxygenase subunits A1/A2, quantitative RT-PCR expression analysis
genes amoB1 and amoB2 encoding ammonia monoxygenase subunits B1/B2, quantitative RT-PCR expression analysis
gene amoA, the amoCAB operon, having a prototypical C-A-B gene order, encodes ammonia monooxygenase, phylogenetic analysis and unrooted phylogenetic consensus tree
-
gene amoA, the amoCAB operon, having a prototypical C-A-B gene order, encodes ammonia monooxygenase, phylogenetic analysis and unrooted phylogenetic consensus tree
gene pmoA, design of a highly degenerate primer targeting copper-containing membrane-bound monooxygenase genes for community analysis of methane- and ammonia-oxidizing bacteria, two-step PCR strategy employing a tagged highly degenerate primer (THDP), designated THDP-PCR, method development and optimization, overview. DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene pmoA, design of a highly degenerate primer targeting copper-containing membrane-bound monooxygenase genes for community analysis of methane- and ammonia-oxidizing bacteria, two-step PCR strategy employing a tagged highly degenerate primer (THDP), designated THDP-PCR, method development and optimization, overview. DNA and amino acid sequence determination and analysis, phylogenetic analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cells of Nitrosomonas europaea may be able to support two types of ammonia monooxygenase activity. One of these types appears to provide a base level of enzyme activity which is largely insensitive to changes in the available NH3 concentration. This is the activity which is observed at the start of each incubation and the level to which the cells returned after they underwent an initial stimulation of activity and a subsequent decline. The second type of ammonia monooxygenase can be increased in response to increases in NH3 availability and can be rapidly decreased in response to NH3 limitation. These two differentially regulated forms of enzyme activity could be particularly useful to Nitrosomonas europaea for a rapid response to transient fluctuations in ammonia availability and still allow the organism to maintain a basal level of ammonia monooxygenase activity to generate energy for both cell maintenance and the rapid de novo synthesis of protein once ammonia becomes available
-
heat shock induces expression of amoC3
in cattle manure compost, the bacterial and archaeal ammonia monooxygenase A (amoA) genes are both up-regulated after exposure to ammonia (14fold)
-
when Nitrosomonas cells are grown with pyruvate as the electron donor and nitrite as the electron acceptor under anoxic conditions, the amount of ammonia monooxygenase in the cells decreases. After about 2 weeks, ammonia monooxygenase is no longer detectable in the denitrifying cells
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
degradation
environmental protection
additional information
-
The amoA gene, encoding the catalytic alpha-subunit of the AMO enzyme, is widely used as a genetic marker to detect ammonia-oxidizing bacteria
analysis
-
the functional gene amoA is used to compare the diversity of ammonia oxidizing bacteria in the water column and sedimentwater interface of the two freshwater lakes Plusssee and Schoehsee and the Baltic Sea
analysis
gene amoA, which encodes the key subunit of the AMO enzyme is commonly used as functional biomarker for surveying aerobic methane or ammonia oxidizers in the environment
analysis
gene amoA, which encodes the key subunit of the AMO enzyme is commonly used as functional biomarker for surveying aerobic methane or ammonia oxidizers in the environment
degradation
-
study on the ammonia monooxygenase activity, subunit alpha (amoA) gene abundance, and community structures of ammonia oxidizing archaea and ammonia oxidizing bacteria in river sediments. The inhibition of ammonia monooxygenase activities increases with the increase of decabromodiphenyl ether (BDE 209, 1-100 mg/kg) and copper (Cu, 50-00 mg/kg) concentrations. The combined effects of BDE 209 and Cu result in a higher ammonia monooxygenase activity reduction than the individual pollutant BDE 209. The ammonia monooxygenase amoA copy number declines by 75.9% and 83.2% and ammonia oxidizing bacteria amoA gene abundance declines 82.8% and 90.0% at 20 and 100 mg/kg BDE 209 with a 100 mg/kg Cu cocontamination, respectively
degradation
a coculture of Nitrosomonas europaea and Nitrobacter sp. is capable of biotransforming micropollutants asulam, bezafibrate, fenhexamid, furosemide, indomethacin, and rufinamide. Ammonia monooxygenase is the responsible enzyme for micropollutant transformation that occurs cometabolically. Hydroxylamine, a key intermediate of all aerobic ammonia oxidizers, reacts with several micropollutants at concentrations typically occurring in ammonia-oxidizing bacteria batch cultures. In addition to cometabolism likely carried out by ammonia monooxygenase, an abiotic transformation route indirectly mediated by ammonia monooxygenase might also contribute to micropollutant biotransformation by ammonia-oxidizing bacteria
degradation
-
in cattle manure compost, the bacterial and archaeal ammonia monooxygenase A (amoA) genes are both up-regulated after exposure to ammonia (14fold), and the bacterial and archaeal communities are more homologous after than before exposure to ammonia. The cattle manure compost may be an efficient biological deodorization medium due to the activation of ammonia-oxidizing microbes, and the up-regulation of their amoA genes
degradation
-
strain is able to completely remove ammonia when initial concentrations are below 100 mg/ml. Above 500 mg/ml ammonia, the removal efficiency declines to 30%. Additional expression of merT, merP and merA genes involved in mercury resistance gives a strain which removes 93% HgCl2
degradation
-
a coculture of Nitrosomonas europaea and Nitrobacter sp. is capable of biotransforming micropollutants asulam, bezafibrate, fenhexamid, furosemide, indomethacin, and rufinamide. Ammonia monooxygenase is the responsible enzyme for micropollutant transformation that occurs cometabolically. Hydroxylamine, a key intermediate of all aerobic ammonia oxidizers, reacts with several micropollutants at concentrations typically occurring in ammonia-oxidizing bacteria batch cultures. In addition to cometabolism likely carried out by ammonia monooxygenase, an abiotic transformation route indirectly mediated by ammonia monooxygenase might also contribute to micropollutant biotransformation by ammonia-oxidizing bacteria
-
environmental protection
-
identification of organic oxidation products and comparison of the reactivities of monohalogenated ethanes and n-chlorinated C1 to C4 alkanes for oxidation by whole cells of Nitrosomonas europaea. The dehalogenating potential of the ammonia monooxygenase in Nitrosomonas europaea may have practical applications for the detoxification of contaminated soil and groundwater
environmental protection
gene amoA, which encodes the key subunit of the AMO enzyme is commonly used as functional biomarker for surveying aerobic methane or ammonia oxidizers in the environment
environmental protection
gene amoA, which encodes the key subunit of the AMO enzyme is commonly used as functional biomarker for surveying aerobic methane or ammonia oxidizers in the environment
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arp, D.J.; Sayavedra-Soto, L.A.; Hommes, N.G.
Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea
Arch. Microbiol.
178
250-255
2002
Nitrosomonas europaea
brenda
Hyman, M.R.; Murton, I.B.; Arp, D.J.
Interaction of ammonia monooxygenase from Nitrosomonas europaea with alkanes, alkenes, and alkynes
Appl. Environ. Microbiol.
54
3187-3190
1988
Nitrosomonas europaea
brenda
Keener, W.K.; Arp, D.J.
Kinetic studies of ammonia monooxygenase inhibition in Nitrosomonas europaea by hydrocarbons and halogenated hydrocarbons in an optimized whole-cell assay
Appl. Environ. Microbiol.
59
2501-2510
1993
Nitrosomonas europaea
brenda
Juliette, L.Y.; Hyman, M.R.; Arp, D.J.
Inhibition of ammonia oxidation in Nitrosomonas europaea by sulfur compounds: thioethers are oxidized to sulfoxides by ammonia monooxygenase
Appl. Environ. Microbiol.
59
3718-3727
1993
Nitrosomonas europaea
brenda
Juliette, L.Y.; Hyman, M.R.; Arp, D.J.
Mechanism-based inactivation of ammonia monooxygenase in Nitrosomonas europaea by allylsulfide
Appl. Environ. Microbiol.
59
3728-3735
1993
Nitrosomonas europaea
brenda
Hyman, M.R.; Page, C.L.; Arp, D.J.
Oxidation of methyl fluoride and dimethyl ether by ammonia monooxygenase in Nitrosomonas europaea
Appl. Environ. Microbiol.
60
3033-3035
1994
Nitrosomonas europaea
brenda
Stein, L.Y.; Arp, D.J.; Hyman, M.R.
Regulation of the synthesis and activity of ammonia monooxygenase in Nitrosomonas europaea by altering pH to affect NH3 availability
Appl. Environ. Microbiol.
63
4588-4592
1997
Nitrosomonas europaea
brenda
Beman, J.M.; Roberts, K.J.; Wegley, L.; Rohwer, F.; Francis, C.A.
Distribution and diversity of archaeal ammonia monooxygenase genes associated with corals
Appl. Environ. Microbiol.
73
5642-5647
2007
uncultured crenarchaeote (A5HAI2), uncultured crenarchaeote (A5HA03), uncultured crenarchaeote (A5HA04), uncultured crenarchaeote (A5HA25), uncultured crenarchaeote (A5HA26), uncultured crenarchaeote (A5HAE3), uncultured crenarchaeote (A5HAF1), uncultured crenarchaeote (A5HAG2), uncultured crenarchaeote (A5H9Z3), uncultured crenarchaeote (A5HA42), uncultured crenarchaeote (A5HA77), uncultured crenarchaeote (A5HA92), uncultured crenarchaeote (A5HAA5), uncultured crenarchaeote (A5HA19), uncultured crenarchaeote (A5HA64), uncultured crenarchaeote (A5HA89), uncultured crenarchaeote (A5HA98), uncultured crenarchaeote (A5HAD1), uncultured crenarchaeote (A5HAE2), uncultured crenarchaeote (A5HAE6), uncultured crenarchaeote (A5HA46), uncultured crenarchaeote (A5HA88), uncultured crenarchaeote (A5HAB0), uncultured crenarchaeote (A5HAB8), uncultured crenarchaeote (A5H9Z2), uncultured crenarchaeote (A5HA16), uncultured crenarchaeote (A5HA28), uncultured crenarchaeote (A5HA31), uncultured crenarchaeote (A5HA44), uncultured crenarchaeote (A5HA48), uncultured crenarchaeote (A5HA62), uncultured crenarchaeote (A5HA74), uncultured crenarchaeote (A5HAA6), uncultured crenarchaeote (A5HAH9), uncultured crenarchaeote (A5H9Z0), uncultured crenarchaeote (A5HA05), uncultured crenarchaeote (A5HA09), uncultured crenarchaeote (A5HA14), uncultured crenarchaeote (A5HA51), uncultured crenarchaeote (A5HA58), uncultured crenarchaeote (A5HA66), uncultured crenarchaeote (A5HA83), uncultured crenarchaeote (A5HA86), uncultured crenarchaeote (A5HAJ3), uncultured crenarchaeote (A5HA24), uncultured crenarchaeote (A5HA20), uncultured crenarchaeote (A5HA60), uncultured crenarchaeote (A5HA79), uncultured crenarchaeote (A5HAC8), uncultured crenarchaeote (A5HAI8), uncultured crenarchaeote (A5HA00), uncultured crenarchaeote (A5HA02), uncultured crenarchaeote (A5HA94), uncultured crenarchaeote (A5HAA0), uncultured crenarchaeote (A5HAC0), uncultured crenarchaeote (A5HAE8), uncultured crenarchaeote (A5HAI7), uncultured crenarchaeote (A5HAB1), uncultured crenarchaeote (A5HA76), uncultured crenarchaeote (A5HAB7), uncultured crenarchaeote (A5HA49), uncultured crenarchaeote (A5HA11), uncultured crenarchaeote (A5HA06), uncultured crenarchaeote (A5HAH4), uncultured crenarchaeote (A5H9Z5), uncultured crenarchaeote (A5HAF8), uncultured crenarchaeote (A5HAH1), uncultured crenarchaeote (A5HAG3), uncultured crenarchaeote (A5HAJ5), uncultured crenarchaeote (A5HA32), uncultured crenarchaeote (A5HA67), uncultured crenarchaeote (A5HA01), uncultured crenarchaeote (A5HAB3), uncultured crenarchaeote (A5HA07), uncultured crenarchaeote (A5HAG1), uncultured crenarchaeote (A5H9Z1), uncultured crenarchaeote (A5HA97), uncultured crenarchaeote (A5HAA7), uncultured crenarchaeote (A5HAF2), uncultured crenarchaeote (A5HA52), uncultured crenarchaeote (A5HAI4), uncultured crenarchaeote (A5HA18), uncultured crenarchaeote (A5HAG8), uncultured crenarchaeote (A5H9Z4), uncultured crenarchaeote (A5HA23), uncultured crenarchaeote (A5HA41), uncultured crenarchaeote (A5HA56), uncultured crenarchaeote (A5HA68), uncultured crenarchaeote (A5HA82), uncultured crenarchaeote (A5HA95), uncultured crenarchaeote (A5HAA4), uncultured crenarchaeote (A5HAB6), uncultured crenarchaeote (A5HA22), uncultured crenarchaeote (A5HA37), uncultured crenarchaeote (A5HA72), uncultured crenarchaeote (A5HAE7), uncultured crenarchaeote (A5HAF3), uncultured crenarchaeote (A5HAF7), uncultured crenarchaeote (A5HAJ2), uncultured crenarchaeote (A5HA59), uncultured crenarchaeote (A5HAB4), uncultured crenarchaeote (A5HAB9), uncultured crenarchaeote (A5HAD9), uncultured crenarchaeote (A5HAE5), uncultured crenarchaeote (A5HAH5), uncultured crenarchaeote (A5HAH7), uncultured crenarchaeote (A5HA30), uncultured crenarchaeote (A5HA45), uncultured crenarchaeote (A5HA47), uncultured crenarchaeote (A5HA50), uncultured crenarchaeote (A5HA61), uncultured crenarchaeote (A5HA63), uncultured crenarchaeote (A5HA69), uncultured crenarchaeote (A5HAA1), uncultured crenarchaeote (A5HAA9), uncultured crenarchaeote (A5HAF6), uncultured crenarchaeote (A5HAI3), uncultured crenarchaeote (A5HAI9), uncultured crenarchaeote (A5H9Z7), uncultured crenarchaeote (A5HA13), uncultured crenarchaeote (A5HA21), uncultured crenarchaeote (A5HA57), uncultured crenarchaeote (A5HAC9), uncultured crenarchaeote (A5HAG4), uncultured crenarchaeote (A5HA15), uncultured crenarchaeote (A5HA39), uncultured crenarchaeote (A5HA54), uncultured crenarchaeote (A5HAF0)
brenda
Fiencke, C.; Bock, E.
Immunocytochemical localization of membrane-bound ammonia monooxygenase in cells of ammonia oxidizing bacteria
Arch. Microbiol.
185
99-106
2006
Nitrosomonas europaea (Q04508), Nitrosomonas mobilis, Nitrosospira sp., Nitrosospira multiformis, Nitrosococcus halophilus, Methylococcus capsulatus, Nitrosomonas mobilis Nc 2
brenda
Bergmann, D.J.; Hooper, A.B.
Sequence of the gene, amoB, for the 43-kDa polypeptide of ammonia monooxygenase of Nitrosomonas europaea
Biochem. Biophys. Res. Commun.
204
759-762
1994
Nitrosomonas europaea (Q04508), Nitrosomonas europaea
brenda
Keener, W.K.; Russell, S.A.; Arp, D.J.
Kinetic characterization of the inactivation of ammonia monooxygenase in Nitrosomonas europaea by alkyne, aniline and cyclopropane derivatives
Biochim. Biophys. Acta
1388
373-385
1998
Nitrosomonas europaea
brenda
Whittaker, M.; Bergmann, D.; Arciero, D.; Hooper, A.B.
Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea
Biochim. Biophys. Acta
1459
346-355
2000
Nitrosomonas europaea
brenda
Gilch, S.; Meyer, O.; Schmidt, I.
A soluble form of ammonia monooxygenase in Nitrosomonas europaea
Biol. Chem.
390
863-873
2009
Nitrosomonas europaea
brenda
Hyman, M.R.; Arp, D.J.
An electrophoretic study of the thermal- and reductant-dependent aggregation of the 27 kDa component of ammonia monooxygenase from Nitrosomonas europaea
Electrophoresis
14
619-627
1993
Nitrosomonas europaea
brenda
Moi, J.W.; Crossman, L.C.; Spiro, S.; Richardson, D.J.
The purification of ammonia monooxygenase from Paracoccus denitrificans
FEBS Lett.
387
71-74
1996
Paracoccus denitrificans
brenda
Zahn, J.A.; Arciero, D.M.; Hooper, A.B.; DiSpirito, A.A.
Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea
FEBS Lett.
397
35-38
1996
Nitrosomonas europaea
brenda
Kim, O.S.; Junier, P.; Imhoff, J.F.; Witzel, K.P.
Comparative analysis of ammonia monooxygenase (amoA) genes in the water column and sediment-water interface of two lakes and the Baltic Sea
FEMS Microbiol. Ecol.
66
367-378
2008
unidentified
brenda
Holmes, A.J.; Costello, A.; Lidstrom, M.E.; Murrell, J.C.
Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related
FEMS Microbiol. Lett.
132
203-208
1995
Nitrosococcus oceani
brenda
Shears, J.H.; Wood, P.M.
Tri- and tetramethylhydroquinone as electron donors for ammonia monooxygenase in whole cells of Nitrosomonas europaea
FEMS Microbiol. Lett.
33
281-284
1986
Nitrosomonas europaea
-
brenda
Rasche, M.E.; Hicks, R.E.; Hyman, M.R.; Arp, D.J.
Oxidation of monohalogenated ethanes and n-chlorinated alkanes by whole cells of Nitrosomonas europaea
J. Bacteriol.
172
5368-5373
1990
Nitrosomonas europaea
brenda
Ensign, S.A.
Hyman, M.R.; Arp, D.J.: In vitro activation of ammonia monooxygenase from Nitrosomonas europaea by copper
J. Bacteriol.
175
1971-1980
1993
Nitrosomonas europaea
brenda
Juliette, L.Y.; Hyman, M.R.; Arp, D.J.
Roles of bovine serum albumin and copper in the assay and stability of ammonia monooxygenase activity in vitro
J. Bacteriol.
177
4908-4913
1995
Nitrosomonas europaea
brenda
Hommes, N.G.; Sayavedra-Soto, L.A.; Arp, D.J.
Mutagenesis and expression of amo, which codes for ammonia monooxygenase in Nitrosomonas europaea
J. Bacteriol.
180
3353-3359
1998
Nitrosomonas europaea (O68938), Nitrosomonas europaea (Q7BTP5), Nitrosomonas europaea
brenda
Schmidt, I.
Nitric oxide: interaction with the ammonia monooxygenase and regulation of metabolic activities in ammonia oxidizers
Methods Enzymol.
440
121-135
2008
Nitrosomonas europaea
brenda
Gilch, S.; Vogel, M.; Lorenz, M.W.; Meyer, O.; Schmidt, I.
Interaction of the mechanism-based inactivator acetylene with ammonia monooxygenase of Nitrosomonas europaea
Microbiology
155
279-284
2009
Nitrosomonas europaea
brenda
Stopnisek, N.; Gubry-Rangin, C.; Hoefferle, S.; Nicol, G.W.; Mandic-Mulec, I.; Prosser, J.I.
Thaumarchaeal ammonia oxidation in an acidic forest peat soil is not influenced by ammonium amendment
Appl. Environ. Microbiol.
76
7626-7634
2010
uncultured archaeon (E5KWU5), uncultured archaeon (E5KWU9), uncultured archaeon (E5KWV0), uncultured archaeon (E5KWV5), uncultured archaeon (E5KWV9), uncultured archaeon (E5KWW3), uncultured archaeon (E5KWW5), uncultured archaeon (E5KWW8), uncultured archaeon (E5KWW9), uncultured archaeon (E5KWX4), uncultured archaeon (E5KWS2), uncultured archaeon (E5KWY2), uncultured archaeon (E5KWY3), uncultured archaeon (E5KWY6), uncultured archaeon (E5KWZ1), uncultured archaeon (E5KWZ4), uncultured archaeon (E5KX01), uncultured archaeon (E5KX02), uncultured archaeon (E5KX05), uncultured archaeon (E5KX08), uncultured archaeon (E5KX10), uncultured archaeon (E5KWS3), uncultured archaeon (E5KWS5), uncultured archaeon (E5KWS7), uncultured archaeon (E5KWS8), uncultured archaeon (E5KWT3), uncultured archaeon (E5KWT6), uncultured archaeon (E5KWT8), uncultured archaeon (E5KWU2)
brenda
Martens-Habbena, W.; Stahl, D.A.
Nitrogen metabolism and kinetics of ammonia-oxidizing archaea
Methods Enzymol.
496
465-487
2011
Nitrosopumilus maritimus, Nitrosococcus oceani, Nitrosomonas europaea, Nitrobacter winogradskyi, Nitrosomonas europaea ATCC 19718, Nitrosococcus oceani ATCC 19707, Nitrobacter winogradskyi Nb-255, ATCC 25391
brenda
Lopez-Legentil, S.; Erwin, P.M.; Pawlik, J.R.; Song, B.
Effects of sponge bleaching on ammonia-oxidizing Archaea: distribution and relative expression of ammonia monooxygenase genes associated with the barrel sponge Xestospongia muta
Microb. Ecol.
60
561-571
2010
Thermoproteota
brenda
Zhang, S.; Li, W.; Zhang, D.; Huang, X.; Qin, W.; Gu, J.
Purification and characterization of a low-temperature ammonia monooxygenase from heterotrophic nitrifier Acinetobacter sp. Y16
Desalin. Water Treatment
53
257-262
2013
Acinetobacter sp., Acinetobacter sp. Y16
-
brenda
Tavormina, P.L.; Orphan, V.J.; Kalyuzhnaya, M.G.; Jetten, M.S.; Klotz, M.G.
A novel family of functional operons encoding methane/ammonia monooxygenase-related proteins in gammaproteobacterial methanotrophs
Environ. Microbiol. Rep.
3
91-100
2011
Nitrosomonas europaea (Q04507), Nitrosococcus oceani, Nitrosomonas europaea ATCC 19718 (Q04507), Nitrosococcus oceani ATCC 19707
brenda
Berube, P.M.; Stahl, D.A.
The divergent AmoC3 subunit of ammonia monooxygenase functions as part of a stress response system in Nitrosomonas europaea
J. Bacteriol.
194
3448-3456
2012
Nitrosomonas europaea (Q04508), Nitrosomonas europaea (Q04507), Nitrosomonas europaea (H2VFU7), Nitrosomonas europaea (Q82T63), Nitrosomonas europaea (O85721), Nitrosomonas europaea
brenda
Bennett, K.; Sadler, N.C.; Wright, A.T.; Yeager, C.; Hyman, M.R.
Activity-based protein profiling of ammonia monooxygenase in Nitrosomonas europaea
Appl. Environ. Microbiol.
82
2270-2279
2016
Nitrosomonas europaea (Q04507 AND Q04508), Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718 (Q04507 AND Q04508)
brenda
Radeva, G.; Kenarova, A.; Bachvarova, V.; Flemming, K.; Popov, I.; Vassilev, D.; Selenska-Pobell, S.
Phylogenetic diversity of archaea and the archaeal ammonia monooxygenase gene in uranium mining-impacted locations in Bulgaria
Archaea
2014
196140
2014
uncultured crenarchaeote (B7VFE0), uncultured crenarchaeote (B7VFE1), uncultured crenarchaeote (B7VFE2), uncultured crenarchaeote (B6S4K0), uncultured crenarchaeote (B7VFD4), uncultured crenarchaeote (B7VFD5), uncultured crenarchaeote (Q1HD88), uncultured crenarchaeote (Q1HD41), uncultured crenarchaeote (B7VFD8)
brenda
Wang, J.G.; Xia, F.; Zeleke, J.; Zou, B.; Rhee, S.K.; Quan, Z.X.
An improved protocol with a highly degenerate primer targeting copper-containing membrane-bound monooxygenase genes for community analysis of methane- and ammonia-oxidizing bacteria
FEMS Microbiol. Ecol.
93
doi: 10.1093/femsec/fiw244
2017
uncultured Nitrospirota bacterium (A0A1L2D5S3), uncultured beta proteobacterium (A0A1L2D5R8)
brenda
Kitamura, R.; Ishii, K.; Maeda, I.; Kozaki, T.; Iwabuchi, K.; Saito, T.
Evaluation of bacterial communities by bacteriome analysis targeting 16S rRNA genes and quantitative analysis of ammonia monooxygenase gene in different types of compost
J. Biosci. Bioeng.
121
57-65
2016
Pseudomonadota
brenda
Macqueen, D.J.; Gubry-Rangin, C.
Molecular adaptation of ammonia monooxygenase during independent pH specialization in Thaumarchaeota
Mol. Ecol.
25
1986-1999
2016
Nitrosotalea, Nitrosopumilus, Nitrososphaera
brenda
Miyaji, A.; Miyoshi, T.; Motokura, K.; Baba, T.
Discrimination of the prochiral hydrogens at the C-2 position of n-alkanes by the methane/ammonia monooxygenase family proteins
Org. Biomol. Chem.
13
8261-8270
2015
Nitrosomonas europaea (Q04507 AND Q04508), Nitrosomonas europaea, Nitrosomonas europaea ATCC 19718 (Q04507 AND Q04508)
brenda
Lawton, T.J.; Ham, J.; Sun, T.; Rosenzweig, A.C.
Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily
Proteins
82
2263-2267
2014
Candidatus Nitrosocaldus yellowstonensis
brenda
Li, C.; Zhao, M.; Song, T.; Zhao, X.; Shao, Y.; Zhang, W.
Characterization and construction of Acinetobacter calcoaceticus T32 strain that can remove ammonia nitrogen and mercury
Appl. Biochem. Microbiol.
55
420-426
2019
Acinetobacter calcoaceticus
-
brenda
Wright, C.L.; Schatteman, A.; Crombie, A.T.; Murrell, J.C.; Lehtovirta-Morley, L.E.
Inhibition of ammonia monooxygenase from ammonia-oxidizing Archaea by linear and aromatic alkynes
Appl. Environ. Microbiol.
86
e02388-19
2020
Candidatus Nitrosocosmicus franklandianus, Nitrosomonas europaea
brenda
Wang, L.; Lihua Niu, Y.L.; Zhang, W.; Zhang, H.; Wang, L.; Wang, P
Response of ammonia oxidizing archaea and bacteria to decabromodiphenyl ether and copper contamination in river sediments
Chemosphere
191
858-867
2018
uncultured bacterium
brenda
Yu, Y.; Han, P.; Zhou, L.J.; Li, Z.; Wagner, M.; Men, Y.
Ammonia monooxygenase-mediated cometabolic biotransformation and hydroxylamine-mediated abiotic transformation of micropollutants in an AOB/NOB coculture
Environ. Sci. Technol.
52
9196-9205
2018
Nitrosomonas europaea (Q04507 AND Q04508), Nitrosomonas europaea ATCC 19718 (Q04507 AND Q04508)
brenda
Qin, W.; Amin, S.; Lundeen, R.; Heal, K.; Martens-Habbena, W.; Turkarslan, S.; Urakawa, H.; Costa, K.; Hendrickson, E.; Wang, T.; Beck, D.; Tiquia-Arashiro, S.; Taub, F.; Holmes, A.; Vajrala, N.; Berube, P.; Lowe, T.; Moffett, J.; Devol, A.; Baliga, N.
Stress response of a marine ammonia-oxidizing archaeon informs physiological status of environmental populations
ISME J.
12
508-519
2018
Nitrosopumilus maritimus (B0LKZ3 and B0LKZ0 and A9A4U4)
brenda
Musiani, F.; Broll, V.; Evangelisti, E.; Ciurli, S.
The model structure of the copper-dependent ammonia monooxygenase
J. Biol. Inorg. Chem.
25
995-1007
2020
Nitrosomonas europaea (Q04507 and Q04508 and H2VFU7), Nitrosomonas europaea ATCC 19718 (Q04507 and Q04508 and H2VFU7)
brenda
Kitamura, R.; Kozaki, T.; Ishii, K.; Iigo, M.; Kurokura, T.; Yamane, K.; Maeda, I.; Iwabuchi, K.; Saito, T.
Utilizing cattle manure compost increases ammonia monooxygenase a gene expression and ammonia-oxidizing activity of both bacteria and archaea in biofiltration media for ammonia deodorization
Microbes Environ.
36
ME20148
2021
uncultured bacterium
brenda
Alves, R.; Minh, B.; Urich, T.; Von Haeseler, A.; Schleper, C.
Unifying the global phylogeny and environmental distribution of ammonia-oxidising archaea based on amoA genes
Nat. Commun.
9
1517
2018
Archaea
brenda
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