1.14.99.39: ammonia monooxygenase
This is an abbreviated version!
For detailed information about ammonia monooxygenase, go to the full flat file.
Word Map on EC 1.14.99.39
-
1.14.99.39
-
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
-
cometabolic
-
methanotrophs
-
biogeochemical
-
nitrosopumilus
-
analysis
-
biofilter
-
chemolithotrophic
-
environmental protection
-
wwtps
-
micropollutants
-
nitrobacter
-
methane-oxidizing
-
methylococcus
-
bathypelagic
- 1.14.99.39
-
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
-
cometabolic
- methanotrophs
-
biogeochemical
- nitrosopumilus
- analysis
-
biofilter
-
chemolithotrophic
- environmental protection
-
wwtps
-
micropollutants
- nitrobacter
-
methane-oxidizing
-
methylococcus
-
bathypelagic
Reaction
Synonyms
ammonia monooxygenase, AMO, AMO-Ne, amoA, AmoB, AmoC3, copper-containing membrane-bound monooxygenase, CuMMO, low-temperature ammonia monooxygenase, Ny_amoB
ECTree
1.14.99.39 ammonia monooxygenaseAdvanced search results
results (
results (Metals Ions
Metals Ions 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.
top
METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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
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)
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)
