Information on EC 1.14.12.17 - nitric oxide dioxygenase

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

EC NUMBER
COMMENTARY hide
1.14.12.17
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RECOMMENDED NAME
GeneOntology No.
nitric oxide dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 nitric oxide + 2 O2 + NAD(P)H = 2 nitrate + NAD(P)+ + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
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-
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reduction
SYSTEMATIC NAME
IUBMB Comments
nitric oxide,NAD(P)H:oxygen oxidoreductase
A flavohemoglobin (FAD). It has been proposed that FAD functions as the electron carrier from NADPH to the ferric heme prosthetic group.
CAS REGISTRY NUMBER
COMMENTARY hide
214466-78-1
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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heterologous expression within a lentiviral delivery system results in markedly increased NADPH consumption, which is dependent on the addition of exogenous NO. Expression does not exhibit any noticeable toxicity or growth suppression in several tested mammalian cell types. Flavohemoglobin metabolizes endogenously synthesized NO to NO3- in mammalian cells without affecting NO synthesis itself
additional information
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the enzyme is distinct from the microsomal NOD activity
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 nitric oxide + 2 O2 + NADPH
2 nitrate + NADP+ + H+
show the reaction diagram
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via an Cygb-NOD intermediate, putative ascorbate-binding site in Cygb, overview
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-
?
nitric oxide + O2 + NAD(P)H
nitrate + NAD(P)+ + H+
show the reaction diagram
NO + O2 + e-
NO3-
show the reaction diagram
NO + O2 + NAD(P)H
NO3- + NAD(P)+ + H+
show the reaction diagram
NO + O2 + NADH
NO3- + NAD+
show the reaction diagram
NO + O2 + NADH
NO3- + NAD+ + H+
show the reaction diagram
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-
-
-
?
NO + O2 + NADPH
NO3- + NADP+
show the reaction diagram
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-
-
-
?
NO + O2 + NADPH
NO3- + NADP+ + H+
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
nitric oxide + O2 + NAD(P)H
nitrate + NAD(P)+ + H+
show the reaction diagram
NO + O2 + e-
NO3-
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome
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flavin
NAD(P)H
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NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
carbon monoxide
clotrimazole
cyanide
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causes slow inactivation
diphenylene iodonium
econazole
imidazole
ketoconazol
ketoconazole
miconazole
phenylhydrazine
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quercetin
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Superoxide dismutase
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additional information
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anions competitively inhibit activity. Increasing the sodium phosphate concentration or including sodium phosphate or NaCl in a 25 mM sodium citrate buffer also competitively inhibits the activity and increases the Km value of ascorbate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
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stimulates NOD activity, reduces the oxidized Cygb-NOD intermediate with a second order rate of 1000 M/s, Km is 0.25 mM
cytochrome b5
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stimulates NOD activity, reduces the oxidized Cygb-NOD intermediate with a second order rate of 3 x 1000000 M/s, Km is 0.3 mM
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Hemin
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maximal activity at 0.001 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.0048
NADH
0.002 - 0.18
NADPH
0.00004
nitric oxide
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pH 7.0, 37C
0.00011 - 0.0003
NO
0.00002 - 0.1
O2
additional information
additional information
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Michaelis-Menten behavior of the Cygb-NOD activity with ascorbate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
50 - 83
NADH
94 - 670
NO
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00065 - 0.05
clotrimazole
0.000225 - 0.03
econazole
0.005 - 0.1
ketoconazole
0.00008 - 0.012
miconazole
additional information
carbon monoxide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0058
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strain DH5alpha
0.015
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strain AB1157
0.2095
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strain DH5alpha after NO-exposition
0.865
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mutant strain PG118
additional information
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0.02 nmol of NO heme-1 s-1, Escherichia coli RB9096; 0.04 nmol of NO heme-1 s-1, Escherichia coli RB9096, VHb mutant Y95F; 0.05 nmol of NO heme-1 s-1, Escherichia coli RB9096, VHb mutant Y95L; 0.61 nmol of NO heme-1 s-1, Escherichia coli RB9096, VHb wild-type; 0.86 nmol of NO heme-1 s-1, Escherichia coli RB9096, VHb mutant Y126F; 0.94 nmol of NO heme-1 s-1, Escherichia coli RB9096, VHb mutant Y126L
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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assay at
7.4 - 8
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activity with NADH and NADPH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
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stopped-flow experiments
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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endothelial cells
Manually annotated by BRENDA team
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from aorta
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12800
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2 * 12800, SDS-PAGE
25000
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SDS-PAGE
43000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 12800, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilizing of activity during gel filtration by adding 10 mM NaN3
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose CL4B column chromatography and Superdex 75 column gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain JM109
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functional expression of human cytoglobin in rat hepatocytes and effects on the cell NO metabolism, overview. Expression in Escherichia coli strain BL21(DE3)
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heterologous expression within a lentiviral delivery system
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Medicago sativa root cultures expressing sense and antisense barley hemoglobin
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plasmids pUC8 or pNKD1 are utilized for wild-type VHb expression in Escherichia coli JM109, DH5alpha and YCM10 cells, for cloning of the mutants the plasmid pVDX18 is used
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y126F
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mutant, displays little change in oxygen affinity indicating a crucial role of Tyr95 in protein function
Y126L
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mutant, displays little change in oxygen affinity indicating a crucial role of Tyr95 in protein function
Y95F
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mutant, enzyme shows no stable oxyform and nitric oxide dioxygenase activity
Y95L
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mutant, enzyme shows no stable oxyform and nitric oxide dioxygenase activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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heterologous expression of Escherichia coli flavohemoglobin within a lentiviral delivery system boosts endogenous cellular consumption of NO, thus providing a simple and efficacious approach to studying mammalian NO-biology
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