Information on EC 1.14.13.165 - nitric-oxide synthase [NAD(P)H]

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
1.14.13.165
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RECOMMENDED NAME
GeneOntology No.
nitric-oxide synthase [NAD(P)H]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 L-arginine + 2 NAD(P)H + 2 H+ + 2 O2 = 2 Nomega-hydroxy-L-arginine + 2 NAD(P)+ + 2 H2O
show the reaction diagram
(1a)
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2 L-arginine + 3 NAD(P)H + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NAD(P)+ + 4 H2O
show the reaction diagram
overall reaction
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2 Nomega-hydroxy-L-arginine + NAD(P)H + H+ + 2 O2 = 2 L-citrulline + 2 nitric oxide + NAD(P)+ + 2 H2O
show the reaction diagram
(1b)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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Arginine biosynthesis
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Biosynthesis of antibiotics
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
L-arginine,NAD(P)H:oxygen oxidoreductase (nitric-oxide-forming)
Binds heme (iron protoporphyrin IX) and tetrahydrobiopterin. Most of the bacterial and archaeal enzymes consist of only an oxidase domain and function together with bacterial ferredoxins [1-2]. The enzyme from the delta-proteobacterium Sorangium cellulosum also includes a reductase domain that binds FAD, FMN and a [2Fe-2S] cluster [3]. The similar enzymes from plants and animals use only NADPH as acceptor (cf. EC 1.14.13.39).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
methicillin-resistant strain
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 L-arginine + 2 NAD(P)H + 2 H+ + 2 O2
2 Nomega-hydroxy-L-arginine + 2 NAD(P)+ + 2 H2O
show the reaction diagram
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1st step of reaction
-
?
2 L-arginine + 3 NAD(P)H + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NAD(P)+ + 4 H2O
show the reaction diagram
2 Nomega-hydroxy-L-arginine + 3 NAD(P)H + 3 H+ + 4 O2
2 L-citrullin + 2 nitric oxide + 3 NAD(P)+ + 4 H2O
show the reaction diagram
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overall reaction. Flavodoxins YkuN and YkuP support catalysis as kinetically competent redox partners. When an NADPH-utilizing bacterial flavodoxin reductase is added to reduce YkuP or YkuN, both support nitric oxide synthesis from either L-arginine or N-hydroxyarginine, with YkuN being more efficient
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?
2 Nomega-hydroxy-L-arginine + NAD(P)H + H+ + 2 O2
2 L-citrulline + 2 nitric oxide + NAD(P)+ + 2 H2O
show the reaction diagram
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2nd step of reaction
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?
additional information
?
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the complex between enzyme and the unusual tryptophanyl-tRNA synthetase TrpRS II catalyzes the regioselective nitration of tryptophan at the 4-position. The enzyme alone will catalyze 4-nitrotryptophan production, but yields are significantly enhanced by TrpRS II and ATP. 4-Nitro-tryptophan formation exhibits saturation behavior with tryptophan and is completely inhibited by the addition of the mammalian nitric-oxide synthase cofactor (6R)-5,6,7,8-tetrahydro-L-biopterin
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
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iron-sulfur centre
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the enzyme's reductase domain utilizes a 2Fe2S cluster for electron transfer
NADH
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small preference for NADH over NADPH
tetrahydrobiopterin
tetrahydrofolate
additional information
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enzyme is able to use several different redox partners
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ngamma-nitro-L-arginine
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competitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tryptophan
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stimulates oxidation of substrate L-arginine. Tryptophan or a derivative thereof may bind in the enzyme's pterin site, participate in arginine oxidation, and become nitrated at the 4-position
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0082
L-arginine
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pH 7.5, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0146
Ngamma-nitro-L-arginine
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pH 7.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
318
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pH 7.5, 25°C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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enzyme contains a catalytic oxygenase domain with a fused reductase domain. The reductase domain utilizes a 2Fe2S cluster for electron transfer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.4 A resolution. Heme and inhibitor S-ethylisothiourea are bound at the active site, while the intersubunit site has NAD+ bound. Enzyme is a dimer, with NAD+ in the interface ligand binding site. Heme is buried in the interior of each monomer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
W66F
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mutation changes midpoint potential from -361 mV for wild-type to -427 mV. Mutant displays 2.5fold lower activity when reaction is supported by flavoproteins or NADPH instead of tetrahydrofolate
W66H
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mutation changes midpoint potential from -361 mV for wild-type to -302 mV. Activity is similar to wild-type
Show AA Sequence (713 entries)
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