Information on EC 1.14.99.39 - ammonia monooxygenase

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

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EC NUMBER
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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
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ammonia oxidation I (aerobic)
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ammonia oxidation III
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Microbial metabolism in diverse environments
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Nitrogen metabolism
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nitrate assimilation
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CAS REGISTRY NUMBER
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95990-35-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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
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
SwissProt
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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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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
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
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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
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
additional information
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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
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
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
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METALS and IONS
ORGANISM
UNIPROT
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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
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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-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
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
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
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.089
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intact cells
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
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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 hide
LITERATURE
4 - 20
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activity range, inactive below and above
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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LOCALIZATION
ORGANISM
UNIPROT
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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
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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
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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
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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
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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
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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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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°C, purified native enzyme, 5 days, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by anion exchange chromatography and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene amoA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
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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 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
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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
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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the functional gene amoA is used to compare the diversity of ammonia oxidizing bacteria in the water column and sediment–water interface of the two freshwater lakes Plusssee and Schoehsee and the Baltic Sea
environmental protection
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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
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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Show AA Sequence (1732 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.99.39)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)