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Enzyme Nomenclature
Information on EC 1.7.5.2 - nitric oxide reductase (menaquinol)
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The expected taxonomic range for this enzyme is: Bacillus azotoformans
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EC NUMBER 
COMMENTARY 
1.7.5.2
-
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RECOMMENDED NAME
GeneOntology No.
nitric oxide reductase (menaquinol)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 nitric oxide + menaquinol = nitrous oxide + menaquinone + H2O
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the ability of qCuANOR to accept electrons from both menaquinol and cytochrome c551 may be related to the regulation of the rate of NO reduction especially as a defense mechanism of B. azotoformans against the toxicity of NO. The menaquinol pathway, which has a 4-fold greater maximal activity than the pathway via cytochrome c551, is used for NO detoxification, whereas electron donation via the endogenous cytochrome c involves the cytochrome b6f complex serving the bioenergetic needs of the organism
physiological function
-
the menaquinol-linked pathway is involved in the detoxification of nitric oxide
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nitric oxide + cytochrome c551
?
-
the menaquinol pathway has a 4fold greater maximal activity than the pathway via cytochrome c551
-
-
?
nitric oxide + menaquinol
nitrous oxide + menaquinone + H2O
-
highest activity with menaquinol
-
-
?
nitric oxide + menaquinol
nitrous oxide + menaquinone + H2O
-
the menaquinol pathway has a 4fold greater maximal activity than the pathway via cytochrome c551
-
-
?
nitric oxide + menaquinol
nitrous oxide + menaquinone + H2O
-
highest activity with menaquinol
-
-
?
additional information
?
-
-
no activity with horse heart ferrocytochrome c
-
-
-
additional information
?
-
-
no activity with lapachol, reduced horse heart cytochrome c, cytochrome c550, and cytochrome c552
-
-
-
additional information
?
-
-
the activity using sodium borohydride-reduced menaquinone is about 2times higher than obtained in the presence of ascorbic acid, phenazine methosulfate, and horse heart cytochrome c
-
-
-
additional information
?
-
-
the bifunctional qCuANOR can accept electrons from two donors, a specific cytochrome c551 and menaquinol
-
-
-
additional information
?
-
-
no activity with horse heart ferrocytochrome c
-
-
-
additional information
?
-
-
the activity using sodium borohydride-reduced menaquinone is about 2times higher than obtained in the presence of ascorbic acid, phenazine methosulfate, and horse heart cytochrome c
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
the enzyme contains two b-type hemes per enzyme complex. The heme b content of the purified NO reductase is 25.7 nmol/mg. Heme c is absent
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
Iron
-
the enzyme contains one non-heme iron per enzyme complex. The non-heme iron content is 13.7 nmol/mg
Cu2+
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copper A containing enzyme with two copper atoms per enzyme complex, the copper content is 26.7 nmol/mg of protein
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome c551
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noncompetitive inhibitor of nitric oxide reduction when menaquinol is used as an electron donor
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ferricytochrome c
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NOR activity is stimulated by ferrocytochrome c when phenazine methosulfate and ascorbate are both present
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0045
cytochrome c551
-
pH and temperature not specified in the publication
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
41
nitric oxide
Bacillus azotoformans
-
using cytochrome c551 as electron donor, pH and temperature not specified in the publication
118
nitric oxide
Bacillus azotoformans
-
using juglone as electron donor, pH and temperature not specified in the publication
150
nitric oxide
Bacillus azotoformans
-
using plumbagin as electron donor, pH and temperature not specified in the publication
153
nitric oxide
Bacillus azotoformans
-
using menaquinol as electron donor, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.67
-
crude membrane extract, pH and temperature not specified in the publication
40.7
-
after 60.5fold purification, pH and temperature not specified in the publication
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography, Sephadex G25 gel filtration, and Bio-Scale Ceramic CHT20-I hydroxyapatite column chromatography
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LINKS TO OTHER DATABASES (specific for EC-Number 1.7.5.2)
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