1.14.14.47: nitric-oxide synthase (flavodoxin)
This is an abbreviated version!
For detailed information about nitric-oxide synthase (flavodoxin), go to the full flat file.
Word Map on EC 1.14.14.47
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1.14.14.47
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familia
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latino
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pacientes
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farmworker
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grupos
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condom
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analysis
- 1.14.14.47
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familia
-
latino
-
pacientes
-
farmworker
-
grupos
-
condom
- analysis
Reaction
2 L-arginine + 2 reduced flavodoxin + 2 O2 = 2 Nomega-hydroxy-L-arginine + 2 oxidized flavodoxin + 2 H2O
Synonyms
bNOS, GK1676, nitric oxide synthetase, NO synthase, NOS, SANOS, YumC
ECTree
1.14.14.47 nitric-oxide synthase (flavodoxin)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.14.14.47 - nitric-oxide synthase (flavodoxin)
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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
2 L-arginine + 2 reduced flavodoxin + 2 O2
2 Nomega-hydroxy-L-arginine + 2 oxidized flavodoxin + 2 H2O
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-
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?
2 L-arginine + 2 tetrahydrobiopterin + 2 O2
2 Nomega-hydroxy-L-arginine + 2 oxidized tetrahydrobiopterin + 2 H2O
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
2 L-arginine + 3 tetrahydrobiopterin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrobiopterin + 4 H2O
2 L-arginine + 3 tetrahydrofolate + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrofolate + 4 H2O
2 Nomega-hydroxy-L-arginine + reduced flavodoxin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized flavodoxin + 2 H2O
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in single turnover experiments with Nomega-hydroxy-L-arginine, NO forms only in the presence of (6R)-tetrahydro-L-biopterin
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?
2 Nomega-hydroxy-L-arginine + tetrahydrobiopterin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized tetrahydrobiopterin + 2 H2O
N-omega-hydroxy-L-arginine + reduced flavodoxin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized flavodoxin + 2 H2O
2 L-arginine + 2 tetrahydrobiopterin + 2 O2
2 Nomega-hydroxy-L-arginine + 2 oxidized tetrahydrobiopterin + 2 H2O
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-
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?
2 L-arginine + 2 tetrahydrobiopterin + 2 O2
2 Nomega-hydroxy-L-arginine + 2 oxidized tetrahydrobiopterin + 2 H2O
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-
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?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
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flavodoxins YkuN and YkuP as well as protein cisJ may be used as redox partners, enzyme uses different available cellular redox partner to support its NO synthesis
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?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
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-
-
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?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
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overall reaction
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?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
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flavodoxins YkuN and YkuP as well as protein cisJ may be used as redox partners, enzyme uses different available cellular redox partner to support its NO synthesis
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?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
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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 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
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overall reaction
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?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
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-
-
-
?
2 L-arginine + 3 reduced flavodoxin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O
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tetrahydrobiopterin or tetrahydrofolate may act as redox partners
overall reaction
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?
2 L-arginine + 3 tetrahydrobiopterin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrobiopterin + 4 H2O
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overall reaction
-
?
2 L-arginine + 3 tetrahydrobiopterin + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrobiopterin + 4 H2O
-
overall reaction
-
?
2 L-arginine + 3 tetrahydrofolate + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrofolate + 4 H2O
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overall reaction
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?
2 L-arginine + 3 tetrahydrofolate + 4 O2
2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrofolate + 4 H2O
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overall reaction
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?
2 Nomega-hydroxy-L-arginine + tetrahydrobiopterin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized tetrahydrobiopterin + 2 H2O
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-
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?
2 Nomega-hydroxy-L-arginine + tetrahydrobiopterin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized tetrahydrobiopterin + 2 H2O
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-
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?
N-omega-hydroxy-L-arginine + reduced flavodoxin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized flavodoxin + 2 H2O
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-
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?
N-omega-hydroxy-L-arginine + reduced flavodoxin + 2 O2
2 L-citrulline + 2 nitric oxide + oxidized flavodoxin + 2 H2O
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-
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?
additional information
?
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ferrous bsNOS reacts with O2 to form a transient heme Fe(II)O2 species in the presence of either Arg or the reaction intermediate N-hydroxy-L-arginine. Disappearance of the Fe(II)O2 species is kinetically and quantitatively coupled to formation of a transient heme Fe(III)NO product, which then dissociates to form ferric NOS. NO formation requires a bound tetrahydropteridine, and the kinetic effects of this cofactor are consistent with it donating an electron to the Fe(II)O2 intermediate during the reaction. Dissociation of the heme Fe(III)NO product is much slower than in mammalian NOS
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?
additional information
?
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NO production requires flavodoxin YkuN and a flavodoxin reductase, YumC fulfilling this requirement
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?
additional information
?
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ferrous bsNOS reacts with O2 to form a transient heme Fe(II)O2 species in the presence of either Arg or the reaction intermediate N-hydroxy-L-arginine. Disappearance of the Fe(II)O2 species is kinetically and quantitatively coupled to formation of a transient heme Fe(III)NO product, which then dissociates to form ferric NOS. NO formation requires a bound tetrahydropteridine, and the kinetic effects of this cofactor are consistent with it donating an electron to the Fe(II)O2 intermediate during the reaction. Dissociation of the heme Fe(III)NO product is much slower than in mammalian NOS
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?
additional information
?
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NO production requires flavodoxin YkuN and a flavodoxin reductase, YumC fulfilling this requirement
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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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?
additional information
?
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addition of oxygen to ferrous NOS results in long-lived heme-oxy complexes in the presence (Soret peak 427 nm) and absence (Soret peak 413 nm) of substrates L-arginine and Nomega-hydroxy-L-arginine. The substrate-induced red shift correlates with hydrogen bonding between substrate and heme-bound oxygen resulting in conversion to a ferric heme-superoxy species
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