Information on EC 1.14.99.39 - ammonia monooxygenase

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

EC NUMBER
COMMENTARY hide
1.14.99.39
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RECOMMENDED NAME
GeneOntology No.
ammonia monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NH3 + a reduced acceptor + O2 = NH2OH + an acceptor + H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ammonia oxidation I (aerobic)
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ammonia oxidation III
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nitrate assimilation
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Nitrogen metabolism
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Microbial metabolism in diverse environments
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CAS REGISTRY NUMBER
COMMENTARY hide
95990-35-5
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ORGANISM
COMMENTARY hide
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
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
gene amoA, uncultured archaeon; gene amoA, Thaumarchaeota
UniProt
Manually annotated by BRENDA team
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A0A1L2D5R8
UniProt
Manually annotated by BRENDA team
water column and sediment–water interface of the two freshwater lakes Plusssee and Schoehsee and the Baltic Sea
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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; 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
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ammonia + AH2 + O2
NH2OH + A + H2O
show the reaction diagram
ethylene + a reduced acceptor + O2
? + an acceptor + H2O
show the reaction diagram
NH3 + a reduced acceptor + O2
NH2OH + an acceptor + H2O
show the reaction diagram
NH3 + duroquinol + O2
NH2OH + duroquinone + H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ammonia + AH2 + O2
NH2OH + A + H2O
show the reaction diagram
NH3 + a reduced acceptor + O2
NH2OH + an acceptor + H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c1
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the gamma-subunit of the alpha3beta3gamma3 enzyme is cytochrome c1
duroquinol
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artificial
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
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contains a labile copper centre
CuCl2
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stimulates enzyme activity in vitro
MgCl2
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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
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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
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Zn2+, Co2+, Ni2+, Fe2+, Fe3+, Ca2+, Mg2+, Mn2+, Cr3+, and Ag+, are ineffective at stimulating AMO activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-dimethylcyclopropane
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22 mM, 93% inhibition, mechanism-based inactivator, ammonia enhances the rate of inactivation
1,3-phenylenediamine
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0.05 mM, 93% inhibition, mechanism-based inactivator, ammonia enhances the rate of inactivation
1,7-octadiyne
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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
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mechanism-based inactivator, ammonia enhances the rate of inactivation
3-Aminophenol
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0.25 mM, 39% inhibition
3-hexyne
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mechanism-based inactivator, ammonia enhances the rate of inactivation
4-chloroaniline
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0.25 mM, 20% inhibition
Acetylene
allylsulfide
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specific, mechanism-based inactivator, anaerobic conditions or the presence of allylthiourea protect the enzyme from inactivation, ammonia increases the rate of inactivation
Allylthiourea
aniline
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0.25 mM, 29% inhibition
anisole
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0.25 mM, 33% inhibition
Bromoethane
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noncompetitive
Chloramphenicol
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rate of NO2- production by 1,7-octadiyne-untreated cells is about 30% lower in the presence of chloramphenicol
chloroethane
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noncompetitive
Chloromethane
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noncompetitive
chloropropane
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noncompetitive
cyclopropyl bromide
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0.007 mM, 97% inhibition, mechanism-based inactivator, ammonia slows the rate of inactivation
cyclopropylamine
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2.5 mM, 22% inhibition
diethyldithiocarbamate
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1 mM, complete inhibition
Dimethyl ether
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inhibits ammonia oxidation
dimethyldisulfide
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weak inhibitor of ammonia oxidation
Dimethylsulfide
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weak inhibitors of ammonia oxidation. Depletion of dimethylsulfide requires O2 and is prevented with either acetylene or allylthiourea
ethane
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noncompetitive
ethylene
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competitive
Iodoethane
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noncompetitive
iodomethane
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noncompetitive
methane
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competitive
methyl fluoride
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inhibits ammonia oxidation
n-butane
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noncompetitive
n-chloropropane
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noncompetitive
p-anisidine
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0.05 mM, 98% inhibition, mechanism-based inactivator, ammonia enhances the rate of inactivation
palmitoleic acid
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propane
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noncompetitive
resorcinol
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0.25 mM, 27% inhibition
rifampicin
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rate of NO2- production by 1,7-octadiyne-untreated cells is about 15% lower in the presence of rifampin
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Serum albumin
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stimulates in vitro
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spermine
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stimulates in vitro
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.85
ammonia
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pH 7.8, 30°C
additional information
additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22 - 0.49
Bromoethane
1.01 - 5.15
chloroethane
0.3 - 1.47
Chloromethane
0.5 - 1.49
chloropropane
0.097
cyclopropyl bromide
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pH 7.8, 30°C
0.22 - 0.89
ethane
0.66
ethylene
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value derived from slope replot
0.03 - 0.29
Iodoethane
0.03 - 0.13
iodomethane
3.24
methane
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value derived from slope replot
0.3 - 0.92
n-butane
0.5 - 1.49
n-chloropropane
1
p-anisidine
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pH 7.8, 30°C
0.44 - 1.43
propane
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.089
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intact cells
23.2
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purified native enzyme, pH 7.5, 15°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 20
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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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
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
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3 * 27000 (alpha-subunit, AmoA) + 3 * 42000 (beta-subunit, AmoB) + 3 * 24000 (gamma-subunit, cytochrome c1), soluble enzyme, SDS-PAGE
27000
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3 * 27000 (alpha-subunit, AmoA) + 3 * 42000 (beta-subunit, AmoB) + 3 * 24000 (gamma-subunit, cytochrome c1), soluble enzyme, SDS-PAGE
31000
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1 * 31000, SDS-PAGE
38000
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x * 38000 + x * 46000, SDS-PAGE
42000
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3 * 27000 (alpha-subunit, AmoA) + 3 * 42000 (beta-subunit, AmoB) + 3 * 24000 (gamma-subunit, cytochrome c1), soluble enzyme, SDS-PAGE
46000
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x * 38000 + x * 46000, SDS-PAGE
283000
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non-denaturing gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
nonamer
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3 * 27000 (alpha-subunit, AmoA) + 3 * 42000 (beta-subunit, AmoB) + 3 * 24000 (gamma-subunit, cytochrome c1), soluble enzyme, SDS-PAGE
additional information
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different from the beta-subunit of membrane-bound ammonia monooxygenase, the beta-subunit of soluble ammonia monooxygenase possesses an N-terminal signal sequence
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 15
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purified native enzyme, stable, over 91% remaining activity
20
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purified native enzyme, inactivation
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
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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 hide
LITERATURE
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
10°C, purified native enzyme, 2 days, stable
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15°C, purified native enzyme, 1 day, stable
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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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4°C, purified native enzyme, 5 days, stable
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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
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native enzyme by anion exchange chromatography and gel filtration
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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
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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 of partial archaeal 16S rRNA and amoA, phylogenetic analysis and tree; 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 of partial archaeal 16S rRNA and amoA, phylogenetic analysis and tree; 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 of partial archaeal 16S rRNA and amoA, phylogenetic analysis and tree; 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 of partial archaeal 16S rRNA and amoA, phylogenetic analysis and tree; 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
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gene amoA, encoding the enzyme alpha subunit, DNA and amino acid sequence determination and analysis, comparison of bacterial community profiles among DNA libraries
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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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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; 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
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
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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; 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 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
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
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heat shock induces expression of amoC3
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
environmental protection
additional information
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The amoA gene, encoding the catalytic alpha-subunit of the AMO enzyme, is widely used as a genetic marker to detect ammonia-oxidizing bacteria
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