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1,4-bis-[[2-(dimethylamino-N-oxide)ethyl]amino]-5,8-dihydroxyanthracene-9,10-dione + NADPH
1-[[2-(dimethylamino-N-oxide)ethyl]amino]-4-[[2-(dimethylamino)ethyl]amino]-5,8-dihydroxyanthracene-9,10-dione + ?
-
-
-
ir
1-butyl-2-hydroxyguanidine + NADPH + O2
? + NO + NADP+
-
-
-
?
1-[[2-(dimethylamino-N-oxide)ethyl]amino]-4-[[2-(dimethylamino)ethyl]amino]-5,8-dihydroxyanthracene-9,10-dione + NADPH
1,4-bis[[2-(dimethylamino)ethyl]amino]-5,8-dihydroxyanthracene-9,10-dione + ?
-
-
-
ir
2 L-arginine + 2 NADPH + 2 H+ + 2 O2
2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
2,6-dichlorophenolindophenol + NADPH + O2
? + NO + NADP+
2-hydroxy-1-(4-hydroxyphenyl)guanidine + NADPH + O2
? + NO + NADP+
-
-
-
?
2-hydroxy-1-isopropylguanidine + NADPH + O2
? + NO + NADP+
-
-
-
?
adriamycin + NADPH + O2
? + NO + NADP+
-
-
-
-
?
ferricyanide + NADPH + O2
ferrocyanide + NADP+ + ?
ferricytochrome c + NADPH + O2
ferrocytochrome c + NO + NADP+
-
-
-
-
?
L-Ala-L-Arg + NADPH + O2
?
L-Arg-L-Arg + NADPH + O2
?
L-Arg-L-Arg-L-Arg + NADPH + O2
?
L-Arg-L-Phe + NADPH + O2
?
L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
L-arginine + H2O2 + tetrahydrobiopterin
? + NO + NADP+
-
-
-
-
?
L-arginine + NADPH + O2 + tetrahydrobiopterin
citrulline + NO + NADP+ + ?
L-homoarginine + NADPH + O2
?
menadione + NADPH + O2
? + NO + NADP+
-
-
-
-
?
mitomycin c + NADPH + O2
? + NO + NADP+
-
-
-
-
?
N-hydroxy-L-arginine + H2O2 + tetrahydrobiopterin
? + NADP+
-
-
-
-
?
N-hydroxy-L-arginine + NADPH + O2
? + NO + NADP+
Ngamma-hydroxy-L-arginine + H2O2
citrulline + Ndelta-cyanoornithine + NO2- + NO3-
-
tetrahydrobiopterin-free
NO2-/NO3- as aerobic decomposition products from NO-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
nitroblue tetrazolium + 2 NADPH
nitroblue tetrazolium formazan + 2 NADP+
Nomega-hydroxy-L-arginine + 2',3'-dialdehyde-NADPH + H+ + O2
2 L-citrulline + nitric oxide + 2',3'-dialdehyde-NADP+ + H2O
-
-
-
-
r
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
L-citrulline + NADP+ + NO + H2O
-
second half reaction
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
peroxynitrite + 4-hydroxyphenylacetic acid + NADPH + H+
4-hydroxyl-3-nitro-phenylacetic acid + NADP+ + H2O
-
oxidation and nitration, although H4B binding seems unable to affect iNOSoxy capacity to activate peroxynitrite decomposition, the binding of Arg and citrulline at the distal side of the heme pocket drastically reduces peroxynitrite activation
product dimers
-
?
additional information
?
-
2 L-arginine + 2 NADPH + 2 H+ + 2 O2
2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O
-
first half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
?
2 L-arginine + 2 NADPH + 2 H+ + 2 O2
2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O
-
first half reaction via intermediate Nomega-hydroxy-L-arginine with consecutive appearance of heme-dioxy, ferric heme-NO, and ferric heme species, overview
-
-
?
2 L-arginine + 2 NADPH + 2 H+ + 2 O2
2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O
-
first half reaction
-
-
ir
2 L-arginine + 2 NADPH + 2 H+ + 2 O2
2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O
-
first half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
?
2 L-arginine + 2 NADPH + 2 H+ + 2 O2
2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O
first half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
?
2 L-arginine + 2 NADPH + 2 H+ + 2 O2
2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O
-
first half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
overall reaction
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
overall reaction, the interactions between heme-bound NO and the substrates are finely tuned by the geometry of the Fe-ligand structure, overview
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
overall reaction, two-step oxidation of L-arginine using an O2-dependent mechanism, detailed overview
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
NO is an important signalling molecule, released by numerous cells, that acts in many tissues to regulate a diverse range of physiological and biological processes, including neurotransmission, immune defence and the regulation of apoptosis. NO plays a major role in the killing of intracellular pathogens as part of the innate immune response
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-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
the electron transfer between cofactors FMN and FAD is reversible
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
overall reaction, overview
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
regulatory mechanism, overview
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
conserved residue Arg1329 of nNOS enables bound NADPH to stabilize the FMN-shielded conformation, overview
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
NO from acetylsalicylic acid-activated enzyme is involved in thrombolysis, overview
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-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
NOS catalyzes the formation of NO via a consecutive two-step reaction. In the first step, L-arginine is converted to N-hydroxy-L-arginine, in the second step, N-hydroxy-L-arginine is further converted to citrulline and nitric oxide, two different mechanisms, overview. During catalysis, mediated by calcium/calmodulin, electrons flow from NADPH through FAD and FMN in the reductase domain of one subunit of the homodimer to the oxygenase domain of the other subunit, substrate-ligand interaction in the Fe2+-O2 complex, overview
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?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
substrate and product binding analysis
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
complete reaction, during Arg hydroxylation, H4B acts as a one-electron donor and is then presumed to redox cycle, i.e. be reduced back to H4B, within NOS before further catalysis can proceed. Calmodulin-dependent reduction of a tetrahydrobiopterin radical, mechanism involving the NOS flavoprotein domain, reaction scheme, overview
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-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
complete reaction, oxygen stoichiometry, effects of substrate/cofactor binding on the endothelial NOS isoform, eNOS, overview
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
conversion of L-arginine to citrulline and nitric oxide takes place in two steps with N(G)-hydroxy-L-arginine as an intermediate product
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
overall reaction, the interactions between heme-bound NO and the substrates are finely tuned by the geometry of the Fe-ligand structure, overview
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
overall reaction, two-step oxidation of L-arginine using an O2-dependent mechanism, detailed overview
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
endothelial nitric oxide synthase (eNOS) is responsible for maintaining systemic blood pressure, vascular remodeling and angiogenesis
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
overall reaction
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
overall reaction
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
overall reaction
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
overall reaction
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
overall reaction
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
the enzyme plays an important role in host defense system by catalyzing the production of nitric oxide
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-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
overall reaction
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
overall reaction
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
overall reaction
-
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
overall reaction
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
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-
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?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
the enzyme forms a five-coordinate, high-spin complex with L-arginine and analogues, e.g. N-hydroxy-L-arginine
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?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
physiological functions and pathophysiology of the isoforms
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?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
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-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
the product is a guanylyl-cyclase-relaxing factor, that is identical with nitric oxide or a NO-releasing compound
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
physiological functions and pathophysiology of the isoforms
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-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
a cytokine-inducible, calcium independent and a constitutive, calcium dependent form
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
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-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
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-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
probably via Nomega-hydroxy-L-arginine
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
the overall reaction proceeds via 2 partial reactions: reaction 1 converts L-arginine into L-Ngamma-hydroxyarginine, reaction 2 converts L-Ngamma-hydroxyarginine into citrulline and nitric oxide
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
capacity to synthesize NO only through dimerization and binding of heme and tetrahydrobiopterin
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
dimeric structure is required for enzyme activity
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
dimeric structure is required for enzyme activity
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
tetrahydrobiopterin is absolutely required for partial reaction 1
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
specific for NADPH, 5-electron oxidation of L-arginine
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
physiological functions and pathophysiology of the isoforms
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
acts as signal molecule for neurotransmission, vasorelaxation, and cytotoxity
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
enzyme of mammalian immune, cardiovascular and neural systems, synthesizing the free radical nitric oxide or a NO-releasing product
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
soluble cytochrome P-450 enzyme in eukaryotes
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
the product is a guanylyl-cyclase-relaxing factor, that is identical with nitric oxide or a NO-releasing compound
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
the product is a guanylyl-cyclase-relaxing factor, that is identical with nitric oxide or a NO-releasing compound
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
probably via Nomega-hydroxy-L-arginine
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
guanidino-nitrogen of L-arginine is oxidized to form NO and citrulline
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
the overall reaction proceeds via 2 partial reactions: reaction 1 converts L-arginine into L-Ngamma-hydroxyarginine, reaction 2 converts L-Ngamma-hydroxyarginine into citrulline and nitric oxide
-
ir
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
specific for NADPH, 5-electron oxidation of L-arginine
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
physiological functions and pathophysiology of the isoforms
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
acts as signal molecule for neurotransmission, vasorelaxation, and cytotoxity
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
soluble cytochrome P-450 enzyme in eukaryotes
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
mitochondrial nitric oxide production is involved in modulation of several organelle functions, such as transmembrane potential and matrix pH, inhibition of respiration by competitive inhibition with oxygen in cytochrome c oxidase, inhibition of ATP synthesis, permeability transition pore (PTP) opening, apoptosis and cell death, overview
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
the product is a guanylyl-cyclase-relaxing factor, that is identical with nitric oxide or a NO-releasing compound
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
-
the product is a guanylyl-cyclase-relaxing factor, that is identical with nitric oxide or a NO-releasing compound
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
physiological functions and pathophysiology of the isoforms
-
-
?
2,6-dichlorophenolindophenol + NADPH + O2
? + NO + NADP+
-
best substrate, about 10-fold increase in activity in presence of calmodulin
-
-
?
2,6-dichlorophenolindophenol + NADPH + O2
? + NO + NADP+
-
-
-
-
?
2,6-dichlorophenolindophenol + NADPH + O2
? + NO + NADP+
-
-
-
-
?
ferricyanide + NADPH + O2
ferrocyanide + NADP+ + ?
-
-
-
-
?
ferricyanide + NADPH + O2
ferrocyanide + NADP+ + ?
-
-
-
-
?
L-Ala-L-Arg + NADPH + O2
?
-
endothelial microsomes, macrophage
-
-
?
L-Ala-L-Arg + NADPH + O2
?
-
endothelial microsomes, macrophage
-
-
?
L-Arg-L-Arg + NADPH + O2
?
-
endothelial, microsomes, macrophage
-
-
?
L-Arg-L-Arg + NADPH + O2
?
-
endothelial, microsomes, macrophage
-
-
?
L-Arg-L-Arg-L-Arg + NADPH + O2
?
-
endothelial microsomes
-
-
?
L-Arg-L-Arg-L-Arg + NADPH + O2
?
-
endothelial microsomes
-
-
?
L-Arg-L-Phe + NADPH + O2
?
-
-
-
-
?
L-Arg-L-Phe + NADPH + O2
?
-
-
-
-
?
L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
-
-
?
L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
overall reaction
-
-
?
L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
nitric-oxide synthase (NOS) is required in mammals to generate nitric-oxide for regulating blood pressure, synaptic response, and immune defense
-
-
?
L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
synthesis of the signaling molecule nitric oxide
-
-
?
L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
proposed conformational model for nitric oxide synthesis by the enzyme. Nitric oxide synthesis involves two distinct changes in the holoenzyme complex: 1. an extended-to-closed conformational equilibrium that brings the reductase domains together in a cross-monomer arrangement, and 2. release and rotation of the FMN domain triggered by CaM binding that positions the FMN cofactor for electron transfer across to the adjacent oxygenase domain in the closed state
-
-
?
L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
overall reaction
-
-
?
L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
overall reaction
-
-
?
L-arginine + NADPH + O2 + tetrahydrobiopterin
citrulline + NO + NADP+ + ?
-
-
-
-
?
L-arginine + NADPH + O2 + tetrahydrobiopterin
citrulline + NO + NADP+ + ?
-
-
-
?
L-arginine + NADPH + O2 + tetrahydrobiopterin
citrulline + NO + NADP+ + ?
-
-
-
-
?
L-arginine + NADPH + O2 + tetrahydrobiopterin
citrulline + NO + NADP+ + ?
-
-
-
-
?
L-homoarginine + NADPH + O2
?
-
constitutive endothelial membrane-bound and inducible soluble macrophage enzyme
-
-
?
L-homoarginine + NADPH + O2
?
-
constitutive endothelial membrane-bound and inducible soluble macrophage enzyme
-
-
?
L-homoarginine + NADPH + O2
?
-
poor substrate
-
-
?
L-homoarginine + NADPH + O2
?
-
poor substrate
-
-
?
N-hydroxy-L-arginine + NADPH + O2
? + NO + NADP+
-
-
-
?
N-hydroxy-L-arginine + NADPH + O2
? + NO + NADP+
-
-
-
?
N-hydroxy-L-arginine + NADPH + O2
? + NO + NADP+
-
-
-
-
?
N-hydroxy-L-arginine + NADPH + O2
? + NO + NADP+
-
-
-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
-
-
-
-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
-
best substrate
-
-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
-
-
-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
-
-
-
-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
-
best substrate
-
-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
-
substrate is intermediate between reaction 1 and 2 to form citrulline and NO from L-arginine
-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
-
reaction is possible without tetrahydrobiopterin, can also use H2O2 instead of NADPH and O2
-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
-
substrate is intermediate between reaction 1 and 2 to form citrulline and NO from L-arginine
-
-
ir
nitroblue tetrazolium + 2 NADPH
nitroblue tetrazolium formazan + 2 NADP+
-
NADPH-diaphorase reaction
-
?
nitroblue tetrazolium + 2 NADPH
nitroblue tetrazolium formazan + 2 NADP+
-
NADPH-diaphorase reaction
-
?
nitroblue tetrazolium + 2 NADPH
nitroblue tetrazolium formazan + 2 NADP+
-
-
-
-
?
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
-
second half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
?
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
-
second half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
?
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
-
second half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
?
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
second half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
?
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
-
second half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
?
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
-
second half reaction via intermediate Nomega-hydroxy-L-arginine, FeII and FeII-NO complexes bind Nomega-hydroxy-L-arginine, overview
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
-
-
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
-
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
-
-
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
-
-
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
-
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
-
wild-type and mutants
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
-
reaction is enhanced by addition of calmodulin at 0.0002 mM
-
-
?
additional information
?
-
-
the enzyme is involved in a multi-turnover process that results in NO as a product, NO is important in various pathological and physiological processes, NO produced by Bacillus anthracis may also have a pivotal pathophysiological role in anthrax infection
-
-
?
additional information
?
-
-
the bacterial enzyme, bNOS, lacks an essential reductase domain, that supplies electrons during NO biosynthesis, and is thus limited with respect to a pool of available redox partners, but does produce NO in living cells and accomplish this task by hijacking available cellular redox partners that are not normally committed to NO production, bacterial reductase also supports NO synthesis by the oxygenase domain of mammalian NOS expressed in Escherichia coli, overview
-
-
?
additional information
?
-
-
the bacterial enzyme, bNOS, lacks an essential reductase domain, that supplies electrons during NO biosynthesis, and is thus limited with respect to a pool of available redox partners, but does produce NO in living cells and accomplish this task by hijacking available cellular redox partners that are not normally committed to NO production, bacterial reductase also supports NO synthesis by the oxygenase domain of mammalian NOS expressed in Escherichia coli, overview
-
-
?
additional information
?
-
-
mechanisms of oxygen activation by NOSs, overview
-
-
?
additional information
?
-
-
the bacterial NOS enzymes have no attached flavoprotein domain to reduce their heme and so must rely on unknown bacterial proteins for electrons
-
-
?
additional information
?
-
-
enzyme shows also superoxide formation activity, uneffected by L-arginine, inhibited by tetrahydrobiopterin and diphenyleneiodonium
-
-
?
additional information
?
-
-
enzyme shows also superoxide formation activity
-
-
?
additional information
?
-
-
endothelial NOS has a 6fold lower NO synthesis activity and 6-16fold lower cytochrome c reductase activity than neuronal NOS due to a significantly different electron transfer capacities, substrate specificity and mechanism, oveview
-
-
?
additional information
?
-
-
postsynaptic density 95 proteins mediate the complex formation of neuronal nitric oxide synthase and N-methyl-D-aspartate receptors
-
-
?
additional information
?
-
-
dNOS participates in essential developmental and behavioral aspects of the fruit fly
-
-
?
additional information
?
-
-
Drosophila dNOS is a more efficient and active NO synthase than the mammalian NOS enzymes, which may allow it to function more broadly in cell signaling and immune functions in the fruit fly
-
-
?
additional information
?
-
-
a oxygenase domain of dNOS complex with ferrous heme-NO is relatively unreactive toward O2
-
-
?
additional information
?
-
-
crude, boiled or ethanolic and dried extracts of Ganoderma applanatum show antioxidant activity, inhibition of lipid peroxidation, and potent hydroxylradical scavenging activity, overview
-
-
?
additional information
?
-
-
enzyme can also Ca2+/calmodulin-dependently produce superoxide in absence of tetrahydropterin and in depletion of L-arginine, which is inhibited by tetrahydropterin, cyanide and imidazole
-
-
?
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
?
additional information
?
-
-
neuronal NO synthase may be involved in the pathogenesis of acute lung injury after smoke inhalation injury followed by bacterial instillation in the airway
-
-
?
additional information
?
-
-
Pseudomonas aeruginosa stimulates expression of inducible nitric oxide synthase by A-549 cells. NO may be the mediator of epithelial damage caused by Pseudomonas aeruginosa
-
-
?
additional information
?
-
calmodulin-controlled isoforms are signal generators, overview
-
-
?
additional information
?
-
-
cell-specific gene regulation mechanism of the endothelial isozyme in the vascular endothelium involving endothelial-specific promoter, binding sites for AP-1, high affinity Sp1-binding sites and GATA promoter sites, and several, e.g. octameric, transcriptional regulators, epigenetic regulatory mechanisms in vascular endothelial cell-specific gene expression, genetic, endothelial-specific regulation model, overview
-
-
?
additional information
?
-
-
genetic regulation, mechanism, eNOS expression is controlled by both histone acetylation and lysine 4 methylation of histone H3 at eNOS proximal promoter regions, overview
-
-
?
additional information
?
-
both oxyFMN and oxygenase domain activity are measured by following H2O2-supported oxidation of Nomega-hydroxy-L-Arg, L-NOHA, overview
-
-
?
additional information
?
-
-
the enzyme interacts with Vac14, the activator of the PtdIns(3)P 5-kinase PIKfyve, the beta-finger independent interaction is based on an internal motif, sequence -G-D-H-L-D-, for PDZ recognition, PDZ domains are protein interaction modules found in single or multiple copies in a variety of proteins involved in multiprotein signaling complexes, interaction study with wild-type and mutant Vac14 proteins, binding is not abolished by deletion of the last five amino acids, but is abolished with deletions of the last 53 or last 10 residues of Vac14, overview
-
-
?
additional information
?
-
-
NOS has also nitrite reductase activity, the release of free nitric oxide from anoxic nitrite solutions at 0.015 mM is specific to the eNOS isoform and does not occur with the nNOS or iNOS isoforms
-
-
?
additional information
?
-
NOS has also nitrite reductase activity, the release of free nitric oxide from anoxic nitrite solutions at 0.015 mM is specific to the eNOS isoform and does not occur with the nNOS or iNOS isoforms
-
-
?
additional information
?
-
NOS has also nitrite reductase activity, the release of free nitric oxide from anoxic nitrite solutions at 0.015 mM is specific to the eNOS isoform and does not occur with the nNOS or iNOS isoforms
-
-
?
additional information
?
-
the bioavailability of substrates (L-arginine and O2) and the cofactor BH4 are important elements of enzyme activity
-
-
-
additional information
?
-
-
the bioavailability of substrates (L-arginine and O2) and the cofactor BH4 are important elements of enzyme activity
-
-
-
additional information
?
-
each monomer contains an oxygenase domain in the N-terminal section and a reductase domain in the C-terminal section. The oxygenase domain has binding sites for FAD, FMN and NADPH and is linked through a calmodulin recognition site to the reductase domain which has binding sites for heme, tetrahydrobiopterin (BH4), and L-arginine. In functional NOS, electrons are released by NADPH in the reductase domain and are transferred through FAD and FMN to the heme group of the opposite dimer. At this point, in the presence of L-arginine and the cofactor BH4, the electrons enable the reduction of O2 and the formation of NO and L-citrulline. The formation of NO requires electron flow, starting at the flavin level in the reductase domain, and ending at the heme level, on the oxygenase domain of the enzyme. The oxidized heme is able to bind O2 and L-arginine to synthesize NO and L-citrulline
-
-
-
additional information
?
-
-
each monomer contains an oxygenase domain in the N-terminal section and a reductase domain in the C-terminal section. The oxygenase domain has binding sites for FAD, FMN and NADPH and is linked through a calmodulin recognition site to the reductase domain which has binding sites for heme, tetrahydrobiopterin (BH4), and L-arginine. In functional NOS, electrons are released by NADPH in the reductase domain and are transferred through FAD and FMN to the heme group of the opposite dimer. At this point, in the presence of L-arginine and the cofactor BH4, the electrons enable the reduction of O2 and the formation of NO and L-citrulline. The formation of NO requires electron flow, starting at the flavin level in the reductase domain, and ending at the heme level, on the oxygenase domain of the enzyme. The oxidized heme is able to bind O2 and L-arginine to synthesize NO and L-citrulline
-
-
-
additional information
?
-
-
the enzyme might be involved in the infectivity and/or escaping mechanism of the parasite
-
-
?
additional information
?
-
-
Ngamma-hydroxylation is the first step of the reaction, Ngamma-hydroxy-L-arginine being an intermediate in the L-arginine to NO pathway
-
-
?
additional information
?
-
-
dimeric enzyme and subunits are equivalent in catalyzing electron transfer from NADPH to cytochrome c, dichlorophenolindiphenol, and ferricyanide
-
-
?
additional information
?
-
-
D-arginine is no substrate
-
-
?
additional information
?
-
-
calmodulin-controlled isoforms are signal generators, overview
-
-
?
additional information
?
-
-
both oxyFMN and oxygenase domain activity are measured by following H2O2-supported oxidation of Nomega-hydroxy-L-Arg, L-NOHA, overview
-
-
?
additional information
?
-
-
inducible nitric-oxide synthase-derived NO contributes to the pathophysiology of intestinal inflammation in the colon
-
-
?
additional information
?
-
-
iNOS modulates endothelin-1-dependent release of prostacyclin and inhibition of platelet aggregation ex vivo in the mouse, overview
-
-
?
additional information
?
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nitric-oxide synthase 2 interacts with CD74 and inhibits its cleavage by caspase during dendritic cell development
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the enzyme exclusively performs the nitric oxide synthesis, an essential biological mediator, and of peroxynitrite, a well known cytotoxic agent involved innumerouspathophysiological processes, NOSs have the unique ability to both produce and activate peroxynitrite, overview
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interaction between peroxynitrite and the oxygenase domain of inducible NOS
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eNOS is an important negative regulator of AMP-activated protein kinase phosphorylation and intracellular H2O2 generation in endothelial cells
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the enzyme exhibits NADPH-diaphorase activity, uncoupled from nitric oxide synthase activity
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D-arginine is no substrate
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NO represents the endogenous activator of soluble guanylyl cyclase
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NO represents the endogenous activator of soluble guanylyl cyclase
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calmodulin-controlled isoforms are signal generators, overview
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caveolin-1 is a prominent NOS-interacting protein in rat polymorphonuclear neutrophils
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NO is implicated in the pathogenesis of liver cirrhosis, overview
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both oxyFMN and oxygenase domain activity are measured by following H2O2-supported oxidation of Nomega-hydroxy-L-Arg, L-NOHA, overview
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eNOS uncoupling is known to be controlled by substrate/cofactor availability, and the uncoupled reactions play important roles under various physiological/pathological conditions, such as atherosclerosis and septic shock
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increased iNOS expression due to ethanol intake is responsible for gender differences in the vascular effects elicited by chronic ethanol consumption, while ovarian hormones do not play a role, overview
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three unique structural elements are involved in the catalytic suppression of NOS: an autoinhibitory element in the FMN binding module, a CD2A loop in the connecting subdomain, and a C-terminal extension or tail, the C-terminal tail of nNOS is a regulatory element that suppresses nNOS activities in the absence of bound calmodulin, it may help stabilize the FMN-shielded conformation by holding the FMN module up against the FNR module as required for inter-flavin electron transfer, mechanism, overview
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nitric-oxide synthases are catalytically self-sufficient flavo-heme enzymes that generate NO from L-arginine and display an utilization of their tetrahydrobiopterin cofactor, overview
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the reduced recombinant trunaction mutant nNOSr performs autooxidation in presence of NADPH, interactions, overview
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the similar spatial distribution of NADPH diaphorase and nitric oxide synthase (NOS) in aldehyde-treated tissues has lead to the postulation that the catalytic activity of NOS promotes NADPH-dependent reduction of nitro-blue tetrazolium (NBT) to insoluble readily visualized diformazan particles. Since NADPH cannot directly reduce NBT, it is argued that NBT binds to NOS at the flavin electron transport domain and is reduced by a NOS form, which is previously reduced by beta-NADPH. However, paraformaldehyde fixation of rat brain abolishes NOS activity in particulate and cytosolic fractions and although fixation abolishes NADPH diaphorase in the particulate fraction, 50-60% of NADPH diaphorase activity remains in the cytosolic fraction. This suggests that cytosolic NADPH diaphorase in aldehyde-treated tissues results from a factor other than NOS. NOS contains heme iron, flavin adenine dinucleotide and flavin mononucleotide. NADPH-dependent reduction of NBT in aldehyde-treated tissues is not directly due to NOS because metal chelators that inhibit activity of metalloenzymes and deflavinating agents do not eliminate NADPH diaphorase. While the NOS active site is not required to promote the NADPH-dependent reduction of NBT, some other reactive site of the protein could still be involved. SNOs exist in cytoplasmic vesicles of endothelial cells of rat small mesenteric arteries, SNOs promote the NADPH-dependent reduction of NBT, both alpha-NADPH and beta-NADPH promote the reduction of NBT to diformazan and since alpha-NADPH will not donate electrons to NOS, it is unlikely that diformazan is the result of an increase in the catalytic activity of NOS, prior depletion of SNOs in tissues markedly reduces subsequent NADPH diaphorase staining. NADPH diaphorase activity in aldehyde-treated tissues is due to preformed pools of SNOs that facilitate NADPH-dependent reduction of NBT to diformazan
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additional information
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the enzyme exhibits NADPH-diaphorase activity, uncoupled from nitric oxide synthase activity
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additional information
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NO represents the endogenous activator of soluble guanylyl cyclase
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additional information
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the similar spatial distribution of NADPH diaphorase and nitric oxide synthase (NOS) in aldehyde-treated tissues has lead to the postulation that the catalytic activity of NOS promotes NADPH-dependent reduction of nitro-blue tetrazolium (NBT) to insoluble readily visualized diformazan particles. Since NADPH cannot directly reduce NBT, it is argued that NBT binds to NOS at the flavin electron transport domain and is reduced by a NOS form, which is previously reduced by beta-NADPH. However, paraformaldehyde fixation of rat brain abolishes NOS activity in particulate and cytosolic fractions and although fixation abolishes NADPH diaphorase in the particulate fraction, 50-60% of NADPH diaphorase activity remains in the cytosolic fraction. This suggests that cytosolic NADPH diaphorase in aldehyde-treated tissues results from a factor other than NOS. NOS contains heme iron, flavin adenine dinucleotide and flavin mononucleotide. NADPH-dependent reduction of NBT in aldehyde-treated tissues is not directly due to NOS because metal chelators that inhibit activity of metalloenzymes and deflavinating agents do not eliminate NADPH diaphorase. While the NOS active site is not required to promote the NADPH-dependent reduction of NBT, some other reactive site of the protein could still be involved. SNOs exist in cytoplasmic vesicles of endothelial cells of rat small mesenteric arteries, SNOs promote the NADPH-dependent reduction of NBT, both alpha-NADPH and beta-NADPH promote the reduction of NBT to diformazan and since alpha-NADPH will not donate electrons to NOS, it is unlikely that diformazan is the result of an increase in the catalytic activity of NOS, prior depletion of SNOs in tissues markedly reduces subsequent NADPH diaphorase staining. NADPH diaphorase activity in aldehyde-treated tissues is due to preformed pools of SNOs that facilitate NADPH-dependent reduction of NBT to diformazan
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D-arginine is no substrate
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mechanisms of oxygen activation by NOSs, overview
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the reductase domain has a broad substrate specificity, catalyzes a moderate Ca2+/calmodulin independent hydroxylation when the enzyme is reconstituted with purified P-450
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additional information
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NO represents the endogenous activator of soluble guanylyl cyclase
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