Information on EC 1.7.2.8 - hydrazine dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
1.7.2.8
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RECOMMENDED NAME
GeneOntology No.
hydrazine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrazine + 4 ferricytochrome c = N2 + 4 ferrocytochrome c
show the reaction diagram
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-
-
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hydroxylamine + NH3 + acceptor = N2 + H2O + reduced acceptor
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ammonia oxidation II (anaerobic)
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Microbial metabolism in diverse environments
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Nitrogen metabolism
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SYSTEMATIC NAME
IUBMB Comments
hydrazine:ferricytochrome c oxidoreductase
The enzyme, which is involved in the pathway of anaerobic ammonium oxidation in anammox bacteria, has been purified from the bacterium Candidatus Kuenenia stuttgartiensis. The electrons derived from hydrazine are eventually transferred to the quinone pool.
CAS REGISTRY NUMBER
COMMENTARY hide
9075-43-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hydrazine + 2,6-dichloroindophenol
? + reduced 2,6-dichloroindophenol
show the reaction diagram
-
-
-
?
hydrazine + 2,6-dichlorophenolindophenol
N2 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
hydrazine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
? + reduced methylthiazolyltetrazolium bromide
show the reaction diagram
reduction of 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide via phenazine methosulfate
-
-
?
hydrazine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
N2 + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
show the reaction diagram
-
-
-
-
?
hydrazine + ferricyanide
? + ferrocyanide
show the reaction diagram
-
-
-
?
hydrazine + ferricyanide
N2 + ferrocyanide
show the reaction diagram
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ferricyanide as the electron acceptor results in the highest specific activity. Hydrazine is solely converted to N2
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-
?
hydrazine + ferricytochrome
N2 + ferrocytochrome
show the reaction diagram
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horse heart cytochrome. Hydrazine is solely converted to N2
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-
?
hydrazine + ferricytochrome c
? + ferrocytochrome c
show the reaction diagram
-
-
-
?
hydrazine + ferricytochrome c
N2 + ferrocytochrome c
show the reaction diagram
hydrazine + methylthiazolyltetrazolium bromide
? + reduced methylthiazolyltetrazolium bromide
show the reaction diagram
reduction of methylthiazolyltetrazolium bromide via phenazine methosulfate
-
-
?
hydrazine + methylthiazolyltetrazolium bromide
N2 + reduced methylthiazolyltetrazolium bromide
show the reaction diagram
-
reduction of methylthiazolyltetrazolium bromide via phenazine methosulfate. Hydrazine is solely converted to N2
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-
?
hydrazine + NH3 + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
?
show the reaction diagram
-
-
-
?
hydrazine + NH3 + phenazine methosulfate
?
show the reaction diagram
-
-
-
?
hydrazine + phenazine methosulfate
? + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
hydroxylamine + 2 acceptor + H2O
nitrite + 2 reduced acceptor + H+
show the reaction diagram
-
-
-
-
?
hydroxylamine + 2,6-dichlorophenolindophenol
N2O + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
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horse heart cytochrome. The conversion of hydroxylamine by the enzyme results in the formation of NO and N2O. A small amount of NO2- is measured, but this is probably due to the chemical reaction of NO. No other nitrogen compounds are detected
small amounts of NO are also formed
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?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
? + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
show the reaction diagram
reduction of methylthiazolyltetrazolium bromide via phenazine methosulfate
-
-
?
hydroxylamine + ferricyanide
N2O + ferrocyanide
show the reaction diagram
-
ferricyanide as the electron acceptor results in the highest specific activity. The conversion of hydroxylamine by the enzyme results in the formation of NO and N2O. A small amount of NO2- is measured, but this is probably due to the chemical reaction of NO. No other nitrogen compounds are detected
small amounts of NO are also formed
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?
hydroxylamine + ferricytochrome
N2O + ferrocytochrome
show the reaction diagram
-
horse heart cytochrome. The conversion of hydroxylamine by the enzyme results in the formation of NO and N2O. A small amount of NO2- is measured, but this is probably due to the chemical reaction of NO. No other nitrogen compounds are detected
small amounts of NO are also formed
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?
hydroxylamine + methylthiazolyltetrazolium bromide
N2O + reduced methylthiazolyltetrazolium bromide
show the reaction diagram
-
the conversion of hydroxylamine by the enzyme results in the formation of NO and N2O. A small amount of NO2- is measured, but this is probably due to the chemical reaction of NO. No other nitrogen compounds are detected
small amounts of NO are also formed
-
?
hydroxylamine + NH3 + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
?
show the reaction diagram
-
-
-
?
hydroxylamine + NH3 + cytochrome c-554
NO2 + H2O + reduced cytochrome c-554
show the reaction diagram
hydroxylamine + NH3 + phenazine methosulfate
NO2 + H2O + reduced phenazine methosulfate
show the reaction diagram
-
-
-
?
additional information
?
-
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
hydrazine + ferricytochrome c
N2 + ferrocytochrome c
show the reaction diagram
hydroxylamine + 2 acceptor + H2O
nitrite + 2 reduced acceptor + H+
show the reaction diagram
-
-
-
-
?
hydroxylamine + NH3 + cytochrome c-554
NO2 + H2O + reduced cytochrome c-554
show the reaction diagram
-
the ammonia-oxidizing bacterium Nitrosomonas europaea normally catalyzes the four-electron oxidation of hydroxylamine to nitrite, which is the second step in ammonia-dependent respiration. In the presence of methyl viologen monocation radical, HAO can catalyze the reduction of nitric oxide to ammonia, reaction of by cytochrome c nitrite reductase , EC 1.7.2.2, overview
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c554
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a soluble 26.1-kDa tetraheme protein that is quite abundant in the periplasm of Nitrosomas europaea and is the acceptor of the electrons from HAO in vivo
cytochrome P460
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cytochrome P468
chromophore; the enzyme has a cytochrome P468 chromophore
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phenazine methosulfate
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additional information
the sequence deduced from the hao gene indicates eight c-type heme binding motifs
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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as Fe(II)NO in the c-type heme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyanide
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addition of 0.035 mM, 0.085 mM, or 0.35 mM cyanide results in 25%, 50%, and 95% inhibition, respectively
H2O2
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0.0004 mM, 0.004 mM, and 0.04 mM results in a loss of activity of 30%, 75%, and 90%, respectively
hydrazine
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competes strongly with hydroxylamine. Addition of 0.015 mM, 0.035 mM, and 0.35 mM results in 15%, 50%, and 85% inhibition, respectively
hydroxylamine
nitric oxide
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strong competitive inhibitor
SDS
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activity in the presence of 0.75%, 3%, and 8% SDS is reduced by 20%, 50%, and 95%, respectively
additional information
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sodium azide, methanol, sodium nitrite, and the chelating agent EDTA do not inhibit enzyme activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0055 - 0.025
hydrazine
0.026 - 0.127
hydroxylamine
additional information
additional information
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kinetics, both reaction steps show first-order dependence on nitric oxide
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 6
hydrazine
Candidatus Kuenenia stuttgartiensis
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at pH 7.0 and 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3500
hydrazine
Candidatus Kuenenia stuttgartiensis
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at pH 7.0 and 37C
684
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0024 - 0.0079
hydroxylamine
0.0025
nitric oxide
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at pH 7.0 and 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.46
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pH 8.0, temperature not specified in the publication
0.55
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crude extract, at pH 7.0 and 37C
5.8
reaction with ferricytochrome c
8.4
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after 15fold purification, at pH 7.0 and 37C
9.6
; partially purified native enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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x * 54900, calculated, without predicted signalpeptide, x * 50000, SDS-PAGE
53000
2 * 53000, SDS-PAGE
54900
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x * 54900, calculated, without predicted signalpeptide, x * 50000, SDS-PAGE
58000
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2 * 58000, SDS-PAGE
62000
2 * 62000, SDS-PAGE
67100
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3 * 67100, calculated from amino acid sequence
118000
gel filtration
130000
gel filtration
150000
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gel filtration
183000
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nondenaturing PAGE
201800
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MALDI-TOF mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 54900, calculated, without predicted signalpeptide, x * 50000, SDS-PAGE
homotrimer
trimer
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complicate arrangement of heme groups in three subunits. As a distinctive feature, the protein has a covalent linkage between a tyrosyl residue of one subunit and a meso carbon atom of the heme active site of another
additional information
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arrangement of the eight hemes within one subunit of hydroxylamine oxidoreductase, structure, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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sequence contains a predicted signal peptide
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
microbatch-under-oil method, using 0.1 M potassium nitrate, 0.1 M MES pH 7.5 and 46%(v/v) PEG 400
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
35C, 20 min, stable
699041
6 - 9
35C, 10 min, stable
695734
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
pH 8.0, 2 min, stable below
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Sepharose CL-6B column chromatography, Sephadex G-100 gel filtration, and DEAE-Sephacel column chromatography
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hydroxylamine oxidoreductase (HAO) is purified from anammox sludge in which an anammox bacterium, strain KSU-1, is dominant; native enzyme 15fold by anion exchange chromatography and gel filtration
partial, enzyme shows a deep orange-red colour
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Q Sepharose column chromatography and hydroxyapatite column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hao gene, indicating DNA and amino acid sequence determination and analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a nitrite shock of 500 mg leads to a decrease in mRNA level; nitrite shocks of up to 400 mg lead to an increase in mRNA level
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
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the application of anammox to nitrogen removal would lead to a reduction of operational costs of up to 90%. The process targets wastewaters that contain much ammonium and little organic material, such as sludge digestor effluents. Anammox would replace the conventional denitrification step completely and would also save half of the nitrification aeration costs
additional information