Information on EC 1.14.99.39 - ammonia monooxygenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
1.14.99.39
-
RECOMMENDED NAME
GeneOntology No.
ammonia monooxygenase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonia + AH2 + O2 = NH2OH + A + H2O
show the reaction diagram
-
-
-
-
ammonia + AH2 + O2 = NH2OH + A + H2O
show the reaction diagram
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
-
PATHWAY
KEGG Link
MetaCyc Link
ammonia oxidation I (aerobic)
-
ammonia oxidation III
-
ammonia oxidation IV (autotrophic ammonia oxidizers)
-
Microbial metabolism in diverse environments
-
Nitrogen metabolism
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AMO
Nitrobacter winogradskyi Nb-255, ATCC 25391
-
-
-
amoA
-
gene name
AmoB
-
gene name
AmoB
Nitrosococcus mobilis Nc 2
-
gene name
-
AmoB
-
gene name
CAS REGISTRY NUMBER
COMMENTARY
95990-35-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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
-
-
Manually annotated by BRENDA team
Nitrobacter winogradskyi Nb-255, ATCC 25391
-
-
-
Manually annotated by BRENDA team
Nitrosococcus mobilis Nc 2
-
-
-
Manually annotated by BRENDA team
gene amoA, uncultured archaeon; gene amoA, Thaumarchaeota
UniProt
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
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
malfunction
O68938, Q7BTP5
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
-
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
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ammonia + AH2 + O2
NH2OH + A + H2O
show the reaction diagram
-
-
-
-
?
ammonia + AH2 + O2
NH2OH + A + H2O
show the reaction diagram
-
-
-
-
?
ammonia + AH2 + O2
NH2OH + A + H2O
show the reaction diagram
-
anaerobic ammonia oxidation
-
-
?
ammonia + AH2 + O2
NH2OH + A + H2O
show the reaction diagram
-
electron transfer during the oxidation
-
-
?
ammonia + AH2 + O2
NH2OH + A + H2O
show the reaction diagram
-
test of electron donors to ammonia monooxygenase in whole cells of Nitrosomonas europaea. Positive results are obtained with tri- and tetramethylhydroquinone
-
-
?
ammonia + AH2 + O2
NH2OH + A + H2O
show the reaction diagram
-
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
-
-
?
additional information
?
-
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
ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
-
-
-
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
?
-
-
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
-
-
-
additional information
?
-
-
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
?
-
-
methyl fluoride and dimethyl ether are converted to formaldehyde and a mixture of methanol and formaldehyde, respectively by ammonia monooxygenase
-
-
-
additional information
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ammonia + AH2 + O2
NH2OH + A + H2O
show the reaction diagram
-
-
-
-
?
ammonia + AH2 + O2
NH2OH + A + H2O
show the reaction diagram
-
anaerobic ammonia oxidation
-
-
?
additional information
?
-
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
ammonia oxidation is the first and rate-limiting step of chemoautotrophic nitrification
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cytochrome c1
-
the gamma-subunit of the alpha3beta3gamma3 enzyme is cytochrome c1
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
copper
-
contains a labile copper centre
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
-
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)
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
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)
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
additional information
-
Zn2+, Co2+, Ni2+, Fe2+, Fe3+, Ca2+, Mg2+, Mn2+, Cr3+, and Ag+, are ineffective at stimulating AMO activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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-hexyne
-
mechanism-based inactivator, ammonia enhances the rate of inactivation
3-Aminophenol
-
0.25 mM, 39% inhibition
3-hexyne
-
mechanism-based inactivator, ammonia enhances the rate of inactivation
4-chloroaniline
-
0.25 mM, 20% inhibition
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
allylsulfide
-
specific, mechanism-based inactivator, anaerobic conditions or the presence of allylthiourea protect the enzyme from inactivation, ammonia increases the rate of inactivation
Allylthiourea
-
0.5 mM, complete inhibition
Aniline
-
0.25 mM, 29% inhibition
anisole
-
0.25 mM, 33% inhibition
Bromoethane
-
noncompetitive
chloroethane
-
noncompetitive
Chloromethane
-
noncompetitive
chloropropane
-
noncompetitive
cyclopropyl bromide
-
0.007 mM, 97% inhibition, mechanism-based inactivator, ammonia slows the rate of inactivation
cyclopropylamine
-
2.5 mM, 22% inhibition
diethyldithiocarbamate
-
1 mM, complete inhibition
Dimethyl ether
-
inhibits ammonia oxidation
dimethyldisulfide
-
weak inhibitor of ammonia oxidation
Dimethylsulfide
-
weak inhibitors of ammonia oxidation. Depletion of dimethylsulfide requires O2 and is prevented with either acetylene or allylthiourea
ethane
-
noncompetitive
ethylene
-
competitive
Iodoethane
-
noncompetitive
Iodomethane
-
noncompetitive
methane
-
competitive
n-butane
-
noncompetitive
n-chloropropane
-
noncompetitive
p-anisidine
-
0.05 mM, 98% inhibition, mechanism-based inactivator, ammonia enhances the rate of inactivation
palmitoleic acid
-
-
propane
-
noncompetitive
resorcinol
-
0.25 mM, 27% inhibition
methyl fluoride
-
inhibits ammonia oxidation
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
-
no inhibition by 0.6 mM cyclopropane
-
additional information
-
ordinary laboratory lighting inhibits ammonia monooxygenase over a period of 1 h. Acetylene is not an inhibitor at 1 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Serum albumin
-
stimulates in vitro
-
spermine
-
stimulates in vitro
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.85
-
ammonia
-
pH 7.8, 30°C
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
-
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, Michaelis-Menten kinetic model, overview
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.22
-
Bromoethane
-
value derived from intercept replot
0.49
-
Bromoethane
-
value derived from slope replot
1.01
-
chloroethane
-
value derived from intercept replot
1.41
-
chloroethane
-
value derived from slope replot
1.42
-
chloroethane
-
value derived from intercept replot
5.15
-
chloroethane
-
value derived from slope replot
0.3
-
Chloromethane
-
value derived from slope replot
1.47
-
Chloromethane
-
value derived from intercept replot
0.5
-
chloropropane
-
value derived from slope replot
1.49
-
chloropropane
-
value derived from intercept replot
0.097
-
cyclopropyl bromide
-
pH 7.8, 30°C
0.22
-
ethane
-
value derived from slope replot
0.89
-
ethane
-
value derived from intercept replot
0.66
-
ethylene
-
value derived from slope replot
0.03
-
Iodoethane
-
value derived from intercept replot
0.29
-
Iodoethane
-
value derived from slope replot
0.03
-
Iodomethane
-
value derived from intercept replot
0.13
-
Iodomethane
-
value derived from slope replot
3.24
-
methane
-
value derived from slope replot
0.3
-
n-butane
-
value derived from intercept replot
0.92
-
n-butane
-
value derived from slope replot
0.5
-
n-chloropropane
-
value derived from slope replot
1.49
-
n-chloropropane
-
value derived from intercept replot
1
-
p-anisidine
-
pH 7.8, 30°C
0.44
-
propane
-
value derived from intercept replot
1.43
-
propane
-
value derived from slope replot
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.089
-
-
intact cells
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
-
cell growth conditions and ammonia/nitrite ratio, overview
Manually annotated by BRENDA team
additional information
Nitrobacter winogradskyi Nb-255, ATCC 25391, Nitrosococcus oceani ATCC 19707, Nitrosomonas europaea ATCC 19718
-
cell growth conditions and ammonia/nitrite ratio, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
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
Manually annotated by BRENDA team
-
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
-
Manually annotated by BRENDA team
Nitrosococcus mobilis Nc 2
-
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
-
-
Manually annotated by BRENDA team
-
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
-
Manually annotated by BRENDA team
Nitrosococcus mobilis Nc 2
-
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
-
-
Manually annotated by BRENDA team
-
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
283000
-
-
non-denaturing gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
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
nonamer
-
3 * 27000 (alpha-subunit, AmoA) + 3 * 42000 (beta-subunit, AmoB) + 3 * 24000 (gamma-subunit, cytochrome c1), soluble enzyme, SDS-PAGE
?
-
x * 38000 + x * 46000, 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
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene amoA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
-
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
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
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
analysis
-
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
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