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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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
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
-
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
-
-
-
-
?
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
-
-
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
?
-
-
nitric-oxide synthase 2 interacts with CD74 and inhibits its cleavage by caspase during dendritic cell development
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
interaction between peroxynitrite and the oxygenase domain of inducible NOS
-
-
?
additional information
?
-
eNOS is an important negative regulator of AMP-activated protein kinase phosphorylation and intracellular H2O2 generation in endothelial cells
-
-
?
additional information
?
-
-
the enzyme exhibits NADPH-diaphorase activity, uncoupled from nitric oxide synthase activity
-
-
?
additional information
?
-
-
D-arginine is no substrate
-
-
?
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
?
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
?
additional information
?
-
calmodulin-controlled isoforms are signal generators, overview
-
-
?
additional information
?
-
-
caveolin-1 is a prominent NOS-interacting protein in rat polymorphonuclear neutrophils
-
-
?
additional information
?
-
NO is implicated in the pathogenesis of liver cirrhosis, 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
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
the reduced recombinant trunaction mutant nNOSr performs autooxidation in presence of NADPH, interactions, overview
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
the enzyme exhibits NADPH-diaphorase activity, uncoupled from nitric oxide synthase activity
-
-
?
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
D-arginine is no substrate
-
-
?
additional information
?
-
-
mechanisms of oxygen activation by NOSs, overview
-
-
?
additional information
?
-
-
the reductase domain has a broad substrate specificity, catalyzes a moderate Ca2+/calmodulin independent hydroxylation when the enzyme is reconstituted with purified P-450
-
-
?
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
additional information
?
-
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
-
-
?
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
-
NO from acetylsalicylic acid-activated enzyme is involved in thrombolysis, 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 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
-
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
the enzyme plays an important role in host defense system by catalyzing the production of nitric oxide
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
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
-
-
-
-
?
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
-
-
?
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
overall reaction
-
-
?
L-arginine + 3 NADPH + 3 H+ + 4 O2
2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
overall reaction
-
-
?
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
?
-
-
enzyme shows also superoxide formation activity
-
-
?
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
?
-
-
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
?
-
-
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
?
-
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
?
-
-
the enzyme might be involved in the infectivity and/or escaping mechanism of the parasite
-
-
?
additional information
?
-
-
calmodulin-controlled isoforms are signal generators, 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
?
-
-
nitric-oxide synthase 2 interacts with CD74 and inhibits its cleavage by caspase during dendritic cell development
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
eNOS is an important negative regulator of AMP-activated protein kinase phosphorylation and intracellular H2O2 generation in endothelial cells
-
-
?
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
?
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
?
additional information
?
-
calmodulin-controlled isoforms are signal generators, overview
-
-
?
additional information
?
-
-
caveolin-1 is a prominent NOS-interacting protein in rat polymorphonuclear neutrophils
-
-
?
additional information
?
-
NO is implicated in the pathogenesis of liver cirrhosis, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
?
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(6R)-5,6,7,8-tetrahydro-L-biopterin
-
2',3'-dialdehyde analogue of NADPH
-
activation, can substitute for NADPH at low concentrations, inhibitory at concentrations of 40times the apparent Km-value or after prolonged incubation
2,6-dichlorophenolindophenol
-
activation
5,6,7,8-tetrahydro-L-biopterin
flavodoxin
-
reduced YkuN and YkuP containing FMN, YkuN is more efficient in supporting bsNOS catalysis, Km for YkuN is 0.0016 mM, for YkuP 0.022 mM, overview
-
flavodoxin I
binding site sequence, overview
-
NADP+
-
binding mechanism
nitroblue tetrazolium
-
activation
(6R)-tetrahydrobiopterin
-
-
(6R)-tetrahydrobiopterin
-
(6R)-tetrahydrobiopterin
-
required
(6R)-tetrahydrobiopterin
-
enzyme-bound
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
5,6,7,8-tetrahydro-L-biopterin
-
5,6,7,8-tetrahydro-L-biopterin
-
5,6,7,8-tetrahydro-L-biopterin
-
5,6,7,8-tetrahydro-L-biopterin
-
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
stimulates
5,6,7,8-tetrahydro-L-biopterin
-
required
5,6,7,8-tetrahydro-L-biopterin
-
required
5,6,7,8-tetrahydro-L-biopterin
-
required
5,6,7,8-tetrahydro-L-biopterin
-
required
5,6,7,8-tetrahydro-L-biopterin
-
enzyme purified in absence of biopterin contains substoichiometric concentration, if purified in presence of biopterin it contains 1 mol biopterin per mol MW 130000 subunit
5,6,7,8-tetrahydro-L-biopterin
-
presumably tightly enzyme-bound
5,6,7,8-tetrahydro-L-biopterin
-
0.19 mol bound per mol of dimer
5,6,7,8-tetrahydro-L-biopterin
-
stimulates 9fold
5,6,7,8-tetrahydro-L-biopterin
-
absolute requirement, recombinant from Pichia pastoris
5,6,7,8-tetrahydro-L-biopterin
-
enhances initial rate of NO-formation
5,6,7,8-tetrahydro-L-biopterin
-
activity is correlated directly to bound biopterin concentration
5,6,7,8-tetrahydro-L-biopterin
-
not required for activity
5,6,7,8-tetrahydro-L-biopterin
-
required for the first partial reaction, formation of NG-hydroxy-L-arginine
5,6,7,8-tetrahydro-L-biopterin
-
i.e. (6R)-2-amino-4-hydroxy-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydropteridine, 6R-isomer, requirement, biopteroflavoprotein, 1 mol tetrahydrobiopterin per mol enzyme dimer
5,6,7,8-tetrahydro-L-biopterin
-
stimulates 4fold at 0.001 mM
5,6,7,8-tetrahydro-L-biopterin
-
0.04 mol per mol of subunit
5,6,7,8-tetrahydro-L-biopterin
-
only wild-type
5,6,7,8-tetrahydro-L-biopterin
0.003 mM
Calmodulin
-
-
Calmodulin
-
dependent on
Calmodulin
-
murine macrophage enzyme is Ca2+/calmodulin independent
Calmodulin
-
the enzyme bears a Ca2+/calmodulin dependent FAD and FMN containing reductase domain which transfers electrons from NADPH to a variety of acceptors
Calmodulin
-
rat neutrophil enzyme is calmodulin independent
Calmodulin
-
activation, potent stimulator of purified, not crude, enzyme preparation
Calmodulin
-
Ca2+/calmodulin is required for superoxide formation in absence of tetrahydropterin
Calmodulin
-
Ca2+/calmodulin stimulates cytochrome c reductase activity
Calmodulin
-
Ca2+/calmodulin stimulates cytochrome c reductase activity
Calmodulin
-
enzyme-bound is required, supplemented stimulates
Calmodulin
-
dependent on, endothelial enzyme
Calmodulin
-
dependent on, endothelial enzyme
Calmodulin
-
no stimulation with exogenous calmodulin, inducible isoform from liver
Calmodulin
-
15fold stimulation of cytochrome c reduction of wild-type and mutants C415A and C415H
Calmodulin
-
NADPH-diaphorase activity of the enzyme is Ca2+/calmodulin independent
Calmodulin
-
enzyme-bound, the binding sequence links the two enzyme domains
Calmodulin
in the absence of calmodulin, the wild type enzyme activity is less than 15% of the maximum calmodulin-dependent values
Calmodulin
maximum calmodulin-dependent activity is measured at 1.5 mM CaCl2, phosphorylation within an autoinhibitory domain in endothelial nitric oxide synthase reduces the Ca2+ concentrations required for calmodulin to bind and activate the enzyme
cytochrome c
-
-
cytochrome c
-
activation
FAD
-
-
FAD
-
tightly enzyme-bound
FAD
-
2.2 mol FAD per mol of enzyme dimer
FAD
-
1 mol FAD per mol enzyme dimer
FAD
-
the enzyme bears Ca2+/calmodulin dependent FAD and FMN containing reductase domain which transfers electrons from NADPH to a variety of acceptors
FAD
-
wild-type and mutant C415H contain1 mol per mol of subunit
FAD
-
1 mol per mol of enzyme subunit
FAD
-
non-covalently bound FAD
FAD
-
FAD containing flavoprotein
FAD
-
FAD containing flavoprotein
FAD
-
0.56 mol per mol of recombinant enzyme
FAD
-
absolute requirement for FAD
FAD
-
major source of superoxide production in absence of tetrahydrobiopterin
FAD
-
slight activation by exogeneous FAD
FAD
-
no activation by the addition of exogenous FAD
FAD
-
0.49 mol per mol of dimer
FAD
binding site sequence, overview
FAD
-
required for catalysis
FAD
-
electron flow within the neuronal nitric oxide synthase reductase domain includes hydride transfer from NADPH to FAD followed by two one-electron transfer reactions from FAD to FMN. Binding of the second NADPH is necessary to drive the full reduction of FMN and charge transfer and the subsequent interflavin electron transfer have distinct spectral features that can be monitored separately with stopped flow spectroscopy. Interflavin electron transfer reported at 600 nm is not limiting in nitric oxide synthase catalysis
FAD
during catalysis, NADPH-derived electrons are transfered into FAD and then distributed into the FMN domain for further transfer to internal or external heme groups. Conformational freedom of the FMN domain is essential for the electron transfer
FAD
in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation
FMN
-
-
FMN
-
tightly enzyme-bound
FMN
-
the enzyme bears Ca2+/calmodulin dependent FAD and FMN containing reductase domain which transfers electrons from NADPH to a variety of acceptors
FMN
-
1 mol per mol of enzyme subunit
FMN
-
wild-type and mutant C415H contain 0.8 and 0.9 mol per mol of subunit, respectively
FMN
-
1 mol FMN per mol enzyme dimer
FMN
-
no activation by the addition of exogenous FMN
FMN
-
1.1 mol FMN per mol enzyme dimer
FMN
-
FMN containing flavoprotein
FMN
-
FMN containing flavoprotein
FMN
-
0.79 mol per mol of recombinant enzyme
FMN
-
0.71 mol per mol of dimer
FMN
-
FMN/heme electron transfer, FMN is capable of serving as a one electron heme reductant
FMN
FMN/heme electron transfer, FMN is capable of serving as a one electron heme reductant
FMN
FMN/heme electron transfer, FMN is capable of serving as a one electron heme reductant
FMN
-
an inverse correlation exists between FMN shielding and the cytochrome c reductase activity
FMN
-
regulation of the FMN module conformational equilibrium, overview
FMN
-
required for catalysis
FMN
-
determination of FMN-heme intraprotein electron transfer kinetics in full length and oxygenase/FMN construct of human inducible nitric oxide synthase. The rate constant increases considerably with temperature. The FMN domain in the holoenzyme needs to sample more conformations before the intraprotein electron transfer takes place, and the FMN domain in the oxyFMN construct is better poised for efficient intraprotein electron transfer
FMN
during catalysis, NADPH-derived electrons are transfer into FAD and then distributed into the FMN domain for further transfer to internal or external heme groups. Conformational freedom of the FMN domain is essential for the electron transfer
FMN
in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation
FMN
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
heme
-
-
heme
-
an inverse correlation exists between FMN shielding and the cytochrome c reductase activity
heme
-
frequencies of electron transfer, overview
heme
-
frequencies of electron transfer, overview
heme
-
the heme is coordinated by a cysteine residue on the proximal side, and the substrates, Arg or N-hydroxy-L-arginine, bind above the heme iron atom in the distal pocket, while the cofactor, tetrahydrobiopterin, binds along the side of the heme
heme b
-
bound, quantitative determination
heme b
-
bound, quantitative determination
NADPH
-
-
NADPH
-
-
440192, 440193, 440195, 440198, 440200, 440201, 440206, 440209, 440217, 440221, 440222, 440225, 440234, 440236, 440238, 440239, 672016, 673662, 674558, 684317, 686293, 687548, 687727, 688600, 696643
NADPH
-
-
440190, 440191, 440192, 440198, 440203, 440208, 440213, 440220, 440228, 440230, 440236, 658119, 659257, 659330, 671278, 671728, 672363, 672524, 675257, 686293, 687615, 699997
NADPH
-
requirement, specific for, NADPH-diaphorase activity requires higher NADPH concentrations than nitric oxide formation
NADPH
-
at high concentration inhibits dimer reconstitution from subunits
NADPH
-
NADPH-dependent dioxygenase
NADPH
-
NADPH-dependent dioxygenase
NADPH
-
crude preparation requires only NADPH as cofactor
NADPH
-
binding mechanism
NADPH
binding site sequence, overview
NADPH
-
binding structure of NADP(H) to wild-type and truncation mutant enzyme lacking parts of the C-terminus, overview
NADPH
-
required for catalysis
NADPH
-
electron flow within the neuronal nitric oxide synthase reductase domain includes hydride transfer from NADPH to FAD followed by two one-electron transfer reactions from FAD to FMN. Binding of the second NADPH is necessary to drive the full reduction of FMN and charge transfer and the subsequent interflavin electron transfer have distinct spectral features that can be monitored separately with stopped flow spectroscopy. Interflavin electron transfer reported at 600 nm is not limiting in nitric oxide synthase catalysis
NADPH
in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation. Binding of NADPH and calmodulin influence interdomain distance relationships as well as reaction chemistry
NADPH
provided from the nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH diaphorase) activity. In the brain, NADPH diaphorase (NADPH-d) and nNOS are strictly co-localized
tetrahydrobiopterin
-
-
tetrahydrobiopterin
-
required
tetrahydrobiopterin
-
oxidation product of BH4 is a protonated BH3 radical, key role of BH4 in protonation of Fe(II)-O2-, overview
tetrahydrobiopterin
-
oxidation product of BH4 is a protonated BH3 radical, key role of BH4 in protonation of Fe(II)-O2-, overview
tetrahydrobiopterin
-
binding analysis
tetrahydrobiopterin
-
the cofactor tetrahydrobiopterin binds along the side of the heme
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(4S)-N-(4-amino-5-[aminoethyl]aminopentyl)-N''-nitroguanidine
-
1,5,6,7-tetrahydro-2H-azepin-2-imines
-
-
1-phenylimidazole
-
reversible inhibition of endothelial enzyme, competitive versus L-arginine and tetrahydrobiopterin, no inhibition of cytochrome c reduction
2',3'-dialdehyde of NADPH
-
at concentrations of 40times the apparent Km-value or after prolonged incubation, independent of Ca2+/calmodulin, L-arginine or tetrahydrobiopterin, NADPH prevents inhibition, the NADPH-diaphorase activity of the enzyme is less sensitive than the nitric oxide synthase activity
2-aminopyridine derivatives
highly selective inhibitors
-
3,4-dihydro-1-isoquinolinamines
-
-
3-bromo-7-nitroindazole
nNOS-specific inhibitor, complete inhibition at 0.01 mM
3-[cis-4'-[(6''-aminopyridin-2''-yl)methyl]pyrrolidin-3'-ylamino]propan-1-ol
-
4-(3-amino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
4-(3-amino-propoxy)-6-chloro-1H-quinolin-2-one trifluoroacetic acid salt
IC50: 410 nM, pharmacokinetic profile
4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
4-(3-dimethylamino-propoxy)-1H-quinolin-2-one
4-oxononenal
ONE, a highly bioreactive agent, able to inhibit eNOS activity and NO production. It can posttranslationally modify the enzyme in the placenta
-
5,6,7,8-tetrahydrobiopterin
-
quenches the uncoupled reactions and results in much less reactive oxygen species formation, whereas the presence of redox-incompetent 7,8-dihydrobiopterin demonstrates little quenching effect
6(R,S)-methyl-5-deazatetrahydropterin
-
-
6-([[(3R,5S)-5-[[(6-amino-4-methylpyridin-2-yl)methoxy]methyl]pyrrolidin-3-yl]oxy]methyl)-4-methylpyridin-2-amine
exhibits antimicrobial properties
6-chloro-4-(3-aminopropoxy)-1-benzopyran-2-one trifluoroacetic acid salt
6-chloro-4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
6-chloro-4-(3-methylamino-propoxy)-1-benzopyran-2-one trifluoroacetic acid salt
6-n-propyl-2-thyouracil
0.1 mg 6-n-propyl-2-thyouracil decreases nNOS activity to 45% compared to control
6-[[(2S,3S)-2-amino-3-[(6-amino-4-methylpyridin-2-yl)methoxy]butoxy]methyl]-4-methylpyridin-2-amine
exhibits antimicrobial properties
A-23187
high levels of A-23187 inhibit nNOS activity
agmatine
-
at lower concentration than the Ki value agmatine leads to time-, concentration-, NADPH- and calmodulin-dependent inhibition of the neuronal enzyme in presence of calmodulin; causes an increase in NADPH oxidase activity of the enzyme
carbon monoxide
carbon monoxide down-regulates iNOS activity by reducing its expression level or by inhibiting its activity by converting it to an inactive P420 form, the presence of dithiothreitol, L-Arg, or H4B partially inhibits the iNOSP450 to iNOSP420 conversion, whereas the presence of both L-Arg and 5,6,7,8-tetrahydro-L-biopterin completely prevents the transition
CO/O2
-
80%:20%, mixture
-
Di-2-thienyliodonium
-
competitive, irreversible, complete, time and temperature dependent inhibition
ethylene glycol bis(beta-amino-ethylether)-N,N,N',N'-tetraacetic acid
Gly-methyl-L-arginine
-
inhibition of the isozymes in absence or presence of L-arginine
H2O2
-
alters heme group, decrease in activity
Iodoniumdiphenyl
-
competitive, irreversible, complete, time and temperature dependent inhibition
L-arginine methyl ester
-
L-Asn-methyl-L-arginine
-
inhibition of the isozymes in absence or presence of L-arginine
L-N-methylarginine
NOS inhibitor, complete inhibition at 0.5 mM; NOS inhibitor, complete inhibition at 0.5 mM; NOS inhibitor, complete inhibition at 0.5 mM
L-N6-(1-iminoethyl)lysine dihydrochloride
-
5 mM, 78% inhibition
L-NG-monomethyl arginine
L-NMMA
-
L-NG-nitro-arginine-methylester
-
-
L-Nomega-nitroarginine-(4R)-amino-L-proline amide
-
L-Nomega-nitroarginine-2,4-L-diaminobutyramide
-
L-omega-monomethyl L-arginine
potent competitive eNOS inhibitor, complete inhibition at 10 mM
MeHg
methylmercury, impact of chronic MeHg intoxication on NADPH diaphorase (NADPH-d) activity and astrocyte mobilization in the visual cortex of the rat, overview. MeHg accumulates in the central nervous system (CNS) and preferentially accumulates in astrocytes, and it causes several neurotoxic effects, such as visual-field constriction, cerebellar ataxia and multimodal sensory disorders. MeHg-intoxicated animals display a significant decrease of NADPH-d neuropil reactivity across the visual cortex when compared to controls. The decreased neuropil reactivity to NADPH-d may also be related to MeHg-induced astrocytic dysfunction
-
methylisothiourea
-
0.01 mM, about 80% residual activity
N(G),N(G)-dimethyl-L-arginine
-
asymmetric dimethyl arginine
N(G)-nitroarginine methyl ester
-
N-(4-aminobutyl)-5-chloro-2-naphthalene sulfonamide
-
-
N-(6-Aminohexyl)-1-naphthalene sulfonamide
-
-
N-(6-aminohexyl)-5-chloro-1-naphthalene sulfonamide
-
calmodulin antagonist above 0.01 mM; i.e. W-7
N-iminoethyl-L-lysine
no isozyme specificity
N-iminoethyl-L-ornithine
no isozyme specificity
N-monomethyl-L-arginine
-
0.01 mM, about 55% residual activity
N-nitro-L-arginine methyl ester
N-omega-nitro-L-arginine
-
N-[(1,3-benzodioxol-5-yl)methyl]-1-[2-(1H-imidazol-1-yl)pyrimidin-4-yl]-4-(methoxycarbonyl)-piperazine-2-acetamide
inhibition of dimer formation in vivo and in vitro, efficiency is dependent on enzyme source
N1-[cis-4'-[(6''-amino-4''-methylpyridin-2''-yl)methyl]pyrrolidin-3'-yl]-N2-(4'-chlorobenzyl)ethane-1,2-diamine
-
N1-[cis-4'-[(6''-aminopyridin-2''-yl)methyl]pyrrolidin-3'-yl]ethane-1,2-diamine
-
N1-[trans-4'-[(6''-amino-4''-methylpyridin-2''-yl)methyl]pyrrolidin-3'-yl]-N2-(3'-chlorobenzyl)ethane-1,2-diamine
-
nanoshutter NS1
mixture of (2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-2-([2-(ethyl(4-[(E)-2-(4-nitrophenyl)ethenyl]phenyl)amino)ethyl]carbamoyl)-4-hydroxyoxolan-3-yl dihydrogen phosphate and (2R,3R,4R,5S)-2-(6-amino-9H-purin-9-yl)-5-([2-(ethyl(4-[(E)-2-(4-nitrophenyl)ethenyl]phenyl)amino)ethyl]carbamoyl)-4-hydroxyoxolan-3-yl dihydrogen phosphate. The NOS inhibitor targets the reductase domain of the enzyme
-
NG-methyl arginine
-
specific inhibition
NG-methyl-L-arginine
no isozyme specificity
Ng-monomethy-L-arginine
-
-
Ngamma,Ngamma-dimethyl-L-arginine
Ngamma-amino-L-arginine
-
-
Ngamma-hydroxy-Ngamma-methyl-L-arginine
-
preincubation at 37°C leads to irreversible inactivation, substrates protect
Ngamma-iminoethyl-L-ornithine
-
competitive inhibitor
Ngamma-monomethyl-L-arginine
Ngamma-nitro-L-arginine methyl ester
Nomega-nitro-L-arginine methyl ester
Nomega-nitro-L-arginine methylester
-
NXN-188
-
a dual-action oral therapeutic being developed for the treatment of acute migraine. The pharmacological mechanism of action of NXN-188 involves inhibition of both the neuronal nitric oxide synthase enzyme isoform and affinity for serotonin receptors. Clinical studies and pharmacokinetics, detailed overview
PIN
-
human protein enzyme inhibitor, recombinantly expressed in Escherichia coli, the recombinant CREB-binding protein-bound inhibitor protein is purified by calmodulin affinity and inhibits the enzyme to a high extent at 0.001 mM
-
tetrahydrobiopterin
-
inhibits peroxynitrite activation
W7 hydrochloride
-
5 mM, 50% inhibition
4-(3-amino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.0076 mM
4-(3-amino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
IC50: 0.0119 mM
4-(3-amino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.0091 mM
4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.004 mM
4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
IC50: 0.01 mM
4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.01 mM
4-(3-dimethylamino-propoxy)-1H-quinolin-2-one
-
IC50: 0.0026 mM
4-(3-dimethylamino-propoxy)-1H-quinolin-2-one
IC50: 0.0104 mM
4-(3-dimethylamino-propoxy)-1H-quinolin-2-one
-
IC50: 0.010 mM
6-chloro-4-(3-aminopropoxy)-1-benzopyran-2-one trifluoroacetic acid salt
-
IC50: 90 nM, pharmacokinetic profile
6-chloro-4-(3-aminopropoxy)-1-benzopyran-2-one trifluoroacetic acid salt
IC50: 60 nM, pharmacokinetic profile
6-chloro-4-(3-aminopropoxy)-1-benzopyran-2-one trifluoroacetic acid salt
-
IC50: 0.00056 mM, pharmacokinetic profile
6-chloro-4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.0041 mM
6-chloro-4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
IC50: 0.0012 mM
6-chloro-4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.008 mM
6-chloro-4-(3-methylamino-propoxy)-1-benzopyran-2-one trifluoroacetic acid salt
-
IC50: 0.00011mM
6-chloro-4-(3-methylamino-propoxy)-1-benzopyran-2-one trifluoroacetic acid salt
IC50: 0.00025mM
6-chloro-4-(3-methylamino-propoxy)-1-benzopyran-2-one trifluoroacetic acid salt
-
IC50: 0.00053mM
7-nitroindazole
-
7-nitroindazole
-
reversible inhibition of endothelial enzyme, competitive versus tetrahydrobiopterin, no inhibition of cytochrome c reduction
7-nitroindazole
-
weak inhibition
7-nitroindazole
-
neuronal NOS inhibitor
7-nitroindazole
-
inhibits the neuronal NOS in vivo and reduces L-DOPA-induced dyskinesias in a rat model of parkinsonism. The rats show a lack of tolerance for the anti-dyskinetic effects
aminoguanidine
-
-
aminoguanidine
-
0.01 mM, about 40% residual activity
AR-C102222
1,2-dihydro-4-quinazolinamine derivative
AR-C102222
-
1,2-dihydro-4-quinazolinamine derivative
AR-C85016
1,2-dihydro-4-quinazolinamine derivative
AR-C85016
-
1,2-dihydro-4-quinazolinamine derivative
AR-R17477
-
-
Ca2+
-
preincubation at 37°C leads to time-dependent inhibition of the enzyme
Ca2+
high levels of Ca2+ inhibit nNOS activity
Calmidazolium
-
-
Calmidazolium
-
calmodulin antagonist; complete inhibition
Calmidazolium
-
calmodulin antagonist
Calmidazolium
-
in absence of calmodulin
CO
-
-
CO
-
partially purified rat cerebellum enzyme
cyanide
-
heme-blocker inhibits superoxide formation after pretreatment of the enzyme
diphenylene iodonium
-
inhibition of superoxide production of recombinant isoform III
diphenylene iodonium
-
competitive, irreversible, complete, time and temperature dependent inhibition
EDTA
-
inhibits at concentrations above 0.01 mM
ethylene glycol bis(beta-amino-ethylether)-N,N,N',N'-tetraacetic acid
-
i.e. EGTA, complete inhibition of cytosolic enzyme, partial inhibition of particulate enzyme
ethylene glycol bis(beta-amino-ethylether)-N,N,N',N'-tetraacetic acid
-
-
ethylene glycol bis(beta-amino-ethylether)-N,N,N',N'-tetraacetic acid
-
i.e. EGTA, complete inhibition of cytosolic enzyme, partial inhibition of particulate enzyme
ethylene glycol bis(beta-amino-ethylether)-N,N,N',N'-tetraacetic acid
-
i.e. EGTA, complete inhibition of cytosolic enzyme, partial inhibition of particulate enzyme
imidazole
-
the enzyme forms a sixcoordinate low-spin complex with inhibitor imidazole, interaction analysis
imidazole
-
inhibition of the endothelial enzyme, competitive versus L-arginine, no inhibition of cytochrome c reduction
imidazole
-
heme-blocker inhibits superoxide formation after pretreatment of the enzyme
inhibitor NS1
-
is a new prototype of a reversible inhibitor of constitutive NOS targeting their reductase domain. NS1 is designed by molecular modelling, by replacing the imbedded NADP cofactor in neuronal NOS reductase domain. NS1 shares with NADPH the nucleotide moiety that allows proper targeting to the NADPH site. NS1 competes with NADPH binding
inhibitor NS1
is a new prototype of a reversible inhibitor of constitutive NOS targeting their reductase domain. NS1 is designed by molecular modelling, by replacing the imbedded NADP cofactor in neuronal NOS reductase domain. NS1 shares with NADPH the nucleotide moiety that allows proper targeting to the NADPH site. NS1 competes with NADPH binding
L-arginine
-
inhibits peroxynitrite activation
L-arginine
-
L-arginine strongly stimulates oxygen consumption of eNOS and inhibits that of nNOS
L-canavanine
-
not inhibitory
L-canavanine
-
liver enzyme, slight inhibition of brain enzyme
L-thiocitrulline
-
5 mM, above 95% inhibition
L-thiocitrulline
no isozyme specificity
N-nitro-L-arginine methyl ester
-
0.5 mM, 65% inhibition
N-nitro-L-arginine methyl ester
-
1 mM, about 50% residual activity
N-nitro-L-arginine methyl ester
-
competitive NOS inhibitor
N-nitro-L-arginine methyl ester
-
0.01 mM, about 40% residual activity
NG-Nitro-L-arginine
no isozyme specificity
NG-Nitro-L-arginine
complete inhibition at 1 mM, non-selective NOS inhibitor; complete inhibition at 1 mM, non-selective NOS inhibitor
Ngamma,Ngamma-dimethyl-L-arginine
-
-
Ngamma,Ngamma-dimethyl-L-arginine
-
-
Ngamma-monomethyl-L-arginine
-
-
Ngamma-monomethyl-L-arginine
-
inhibits citrulline formation, not cytochrome c reduction
Ngamma-monomethyl-L-arginine
-
-
Ngamma-monomethyl-L-arginine
-
-
Ngamma-monomethyl-L-arginine
-
-
Ngamma-monomethyl-L-arginine
-
endothelial and neuronal isoforms: reversible inhibition; L-arginine protects against enzyme inactivation, thus inactivation occurs at or near active site
Ngamma-monomethyl-L-arginine
-
-
Ngamma-monomethyl-L-arginine
-
inducible isoform: after preincubation irreversible, time- and concentration-dependent inactivation, without preincubation reversible inhibition; L-arginine protects against enzyme inactivation, thus inactivation occurs at or near active site
Ngamma-monomethyl-L-arginine
-
slightly
Ngamma-monomethyl-L-arginine
-
-
Ngamma-monomethyl-L-arginine
-
not D-isomer, strong, competitive
Ngamma-monomethyl-L-arginine
-
slightly
Ngamma-monomethyl-L-arginine
-
endothelial and neuronal isoforms: reversible inhibition; in presence of tetrahydrobiopterin 0.004 mM the neuronal isoform is inactivated; L-arginine protects against enzyme inactivation, thus inactivation occurs at or near active site
Ngamma-nitro-L-arginine
-
-
Ngamma-nitro-L-arginine
-
inhibits citrulline formation, not cytochrome c reduction
Ngamma-nitro-L-arginine
-
-
Ngamma-nitro-L-arginine
-
-
Ngamma-nitro-L-arginine
-
-
Ngamma-nitro-L-arginine
-
irreversible inactivation of neuronal and endothelial isoform after preincubation, unaffected by tetrahydrobiopterin; L-arginine protects against enzyme inactivation, thus inactivation occurs at or near active site
Ngamma-nitro-L-arginine
-
-
Ngamma-nitro-L-arginine
-
L-arginine protects against enzyme inactivation, thus inactivation occurs at or near active site; reversible inhibitor of inducible isoform from macrophage
Ngamma-nitro-L-arginine
-
-
Ngamma-nitro-L-arginine
-
-
Ngamma-nitro-L-arginine
-
competitive inhibitor
Ngamma-nitro-L-arginine
-
irreversible inactivation of neuronal and endothelial isoform after preincubation, unaffected by tetrahydrobiopterin; L-arginine protects against enzyme inactivation, thus inactivation occurs at or near active site
Ngamma-nitro-L-arginine methyl ester
-
-
Ngamma-nitro-L-arginine methyl ester
-
complete inhibition
Ngamma-nitro-L-arginine methyl ester
-
only L-isomer, inhibits NO and citrulline production from L-arginine as well as superoxide formation in absence of tetrahydropterin
Ngamma-nitro-L-arginine methyl ester
-
-
Ngamma-nitro-L-arginine methyl ester
-
-
Ngamma-nitro-L-arginine methyl ester
-
very slightly, only L-isomer and in presence of tetrahydrobiopterin and NADPH
Ngamma-nitro-L-arginine methyl ester
-
nearly complete inhibition at 0.5 mM
nitroblue tetrazolium
-
-
nitroblue tetrazolium
-
potent non-competitive inhibitor, partially reversible by tetrahydrobiopterin
nitroblue tetrazolium
-
-
Nomega-nitro-L-arginine methyl ester
-
nonselective NOS inhibitor
Nomega-nitro-L-arginine methyl ester
-
Nomega-nitro-L-arginine methylester
L-NAME, the NOS inhibitor targets the oxygenase domain of the enzyme
-
Nomega-nitro-L-arginine methylester
L-NAME, an inhibitor of iNOS
-
S-ethylisothiourea
-
5 mM, 85% inhibition
S-ethylisothiourea
-
inducible NOS inhibitor
thiocoumarin
-
IC50: 0.018 mM
thiocoumarin
weak inhibitor
Trifluoperazine
-
inhibits cytochrome c reductase activity
Trifluoperazine
-
inhibition in the presence of Ca2+, reversible by calmodulin
Trifluoperazine
-
no inhibitor of macrophage enzyme
Trifluoperazine
-
no inhibitor of macrophage enzyme
Trifluoperazine
-
in absence of calmodulin
additional information
-
not inhibitory: N-nitro-D-arginine methyl ester at 0.5 mM
-
additional information
a protein-based system is developed in which ligand inhibition can be rapidly evaluated in vitro
-
additional information
-
Ngamma,Ngamma'-dimethyl-L-arginine has no inhibitory effect
-
additional information
-
no inhibition by 4-(3-amino-propoxy)-6-chloro-1H-quinolin-2-one trifluoroacetic acid salt
-
additional information
interleukin-1 induces the degradation of isozyme iNOS, iNOS protein levels in osteoarthritic chondrocytes decreases to 45.4% of the control upon treatment with interleukin-1 for 15 min, and are further reduced to 41.5% when the treatment period is extended to 2 h; tissue necrosis factor-alpha induces nNOS disappearance, interleukin-1 induces the degradation of nNOS
-
additional information
interleukin-1 induces the degradation of isozyme iNOS, iNOS protein levels in osteoarthritic chondrocytes decreases to 45.4% of the control upon treatment with interleukin-1 for 15 min, and are further reduced to 41.5% when the treatment period is extended to 2 h; tissue necrosis factor-alpha induces nNOS disappearance, interleukin-1 induces the degradation of nNOS
-
additional information
-
interleukin-1 induces the degradation of isozyme iNOS, iNOS protein levels in osteoarthritic chondrocytes decreases to 45.4% of the control upon treatment with interleukin-1 for 15 min, and are further reduced to 41.5% when the treatment period is extended to 2 h; tissue necrosis factor-alpha induces nNOS disappearance, interleukin-1 induces the degradation of nNOS
-
additional information
-
fibroblast growth factor-2 treatment up-regulates the enzyme in tectume, but down-regulates it in the optic nerve, overview
-
additional information
-
the macrophage enzyme is not inhibited by calmodulin antagonists (N-4-aminobutyl-), (N-6-aminohexyl)-5-chloro-2-naphthalene sulfonamide
-
additional information
-
not inhibitory: N-nitro-L-arginine methyl ester, or specific inhibitor of inducible NOS, 1400W
-
additional information
inhibitory activity for coumarin derivatives, inhibitor screening, overview
-
additional information
-
inhibitory activity for coumarin derivatives, inhibitor screening, overview
-
additional information
-
inhibition of PSD-95/nNOS interaction by the nNOSalpha beta-finger antibody
-
additional information
-
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
-
additional information
there is decreased eNOS activity in tight-skin 1-mouse skin tissue
-
additional information
-
there is decreased eNOS activity in tight-skin 1-mouse skin tissue
-
additional information
-
no inhibitor of NADPH-diaphorase activity: methotrexate
-
additional information
-
the macrophage enzyme is not inhibited by calmodulin antagonists (N-4-aminobutyl-), (N-6-aminohexyl)-5-chloro-2-naphthalene sulfonamide; the macrophage enzyme is not inhibited by calmodulin antagonists (N-6-aminohexyl)-1-naphthalene sulfonamide
-
additional information
-
the macrophage enzyme is not inhibited by calmodulin antagonists (N-4-aminobutyl-), (N-6-aminohexyl)-5-chloro-2-naphthalene sulfonamide; the macrophage enzyme is not inhibited by calmodulin antagonists (N-6-aminohexyl)-1-naphthalene sulfonamide
-
additional information
-
no inhibition by 4-(3-amino-propoxy)-6-chloro-1H-quinolin-2-one trifluoroacetic acid salt and thiocoumarin
-
additional information
-
ethanol intake reduces eNOS and increases iNOS protein levels, while mRNA levels remain unaffected in female rat aorta
-
additional information
-
inhibition of PSD-95/nNOS interaction by the nNOSalpha beta-finger antibody
-
additional information
anthrax lethal factor potentially cleaves the regions (L191-Q192 and D264-N265) close to the NH2-terminus of neuronal nitric oxide synthase; inducible nitric oxide synthase is resistant to anthrax lethal factor-mediated cleavage
-
additional information
anthrax lethal factor potentially cleaves the regions (L191-Q192 and D264-N265) close to the NH2-terminus of neuronal nitric oxide synthase; inducible nitric oxide synthase is resistant to anthrax lethal factor-mediated cleavage
-
additional information
paraformaldehyde fixation of rat brain abolishes NOS activity in particulate and cytosolic fractions
-
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brenda
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-
brenda
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axenic, high enzyme expression level
brenda
-
brenda
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isozyme NOS3
brenda
-
-
brenda
-
brenda
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iNOS
brenda
-
brenda
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-
brenda
-
-
brenda
high expression
brenda
-
-
brenda
-
main nervous structures (buccal nerve and nerve plate) in the bud of the tentacle
brenda
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cell line ME-180, constitutive expression
brenda
-
-
brenda
-
two populations of NADPH diaphorase-positive neurons exist in the human claustrustrum. One is comprised of large and medium cells consistent with a projection neuron phenotype, the other is represented by small cells resembling the interneuron phenotype as defined by previous Golgi impregnation studies. NADPH diaphorase-reactive neurons are heterogenously distributed throughout the claustrum
brenda
-
iNOS
brenda
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bone marrow-derived
brenda
-
brenda
-
-
brenda
-
mainly in the lateral soma rind, surrounding the sensory glomeruli, partially in association with the antennal mechanosensory and motor neuropil
brenda
-
nNOS
brenda
-
-
brenda
-
NADPH-diaphorase activity is found in the midpiece of the spermatozoa tail and epithelial cells of all intratesticular and excurrent ducts analyzed, except for nonciliated cells of the efferent ductules. Immunostaining shows cell-specific localization in the efferent ductules and region- and cell-specific localization in the epididymal duct
brenda
-
brenda
-
brenda
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synaptosomal fraction
brenda
-
brenda
-
cell line A-172, american type
brenda
-
brenda
-
-
brenda
highest expression in hemocytes, followed by the tissues of hepatopancreas, brain and intestine. Relatively low transcriptional levels are detected in the tissues of eyestalk, gill, heart and muscle
brenda
-
brenda
-
brenda
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leaf extract
brenda
-
-
brenda
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constitutive expression of full length nitric oxide synthase isoforms. Lymphocytes express more inducible nitric oxide synthase transcripts and protein than neuronal nitric oxide synthase and endothelial nitric oxide synthase
brenda
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isozyme NOS1
brenda
-
NADPH-diaphorase is found in large and small neurons in the sensory, autonomic, and motor nuclei. In contrast to NADPH-diaphorase, nitric oxide synthase in the corresponding nuclei is always present in smaller quantities of mainly smaller neurons. In some nuclei (the nucleus ambiguus, the nucleus of the hypoglossal nerve) containing large numbers of NADPH-diaphorase-positive neurons, nitric oxide synthase immunoreactive cells are particularly rare
brenda
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-
brenda
-
-
brenda
-
-
brenda
-
brenda
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constitutive expression of full length nitric oxide synthase isoforms. Isolated monocytes express more endothelial nitric oxide synthase transcript and protein as compared to neuronal nitric oxide synthase and inducible nitric oxide synthase
brenda
-
brenda
-
three isoforms of nitric oxide synthase are mainly localized in the uterine luminal and glandular epithelium and myometrium, and the intensity of immunostaining for inducible nitric oxide synthase and endothelial nitric oxide synthase increases gradually with temporal development of the postnatal uterus. The total nitric oxide synthase and inducible nitric oxide synthase activities are significantly increased at postnatal days 21 and 35. Although constitutive nitric oxide synthase activity is increased at postnatal day 21, it decreases subsequently at postnatal day 35. Inducible nitric oxide synthase protein expression is significantly increased at postnatal days 21 and 35
brenda
-
type I neurons are generated during early corticogenesis, whereas type II cells are produced over a wide prenatal time window persisting until birth. Type II nitrinergic neurons may undergo a period of development/differentiation, for over 1 month, before being NADPH-diaphorase reactive
brenda
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-
brenda
high expression
brenda
constitutive expression of Ca22+/calmodulin-dependent neuronal nitric oxide synthase in the central and peripheral nervous system
brenda
-
NOS1
brenda
of central ganglia
brenda
-
nNOS
brenda
-
-
brenda
high expression
brenda
-
-
brenda
-
brenda
-
constitutive expression of full length nitric oxide synthase isoforms with the highest expression of inducible nitric oxide synthase in comparison to neuronal nitric oxide synthase and endothelial nitric oxide synthase
brenda
-
-
brenda
-
-
brenda
-
brenda
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-
brenda
-
-
brenda
-
brenda
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-
brenda
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-
brenda
n the skin, eNOS is present in the epidermal layer, hair follicles and also in the endothelial cells lining the blood vessels
brenda
-
brenda
-
brenda
-
distribution, overview, before and after axotomy and fibroblast growth factor-2 application
brenda
-
-
brenda
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-
brenda
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i.e. HUVEC cells
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
-
brenda
-
three isoforms of nitric oxide synthase are mainly localized in the uterine luminal and glandular epithelium and myometrium, and the intensity of immunostaining for inducible nitric oxide synthase and endothelial nitric oxide synthase increases gradually with temporal development of the postnatal uterus. The total nitric oxide synthase and inducible nitric oxide synthase activities are significantly increased at postnatal days 21 and 35. Although constitutive nitric oxide synthase activity is increased at postnatal day 21, it decreases subsequently at postnatal day 35. Inducible nitric oxide synthase protein expression is significantly increased at postnatal days 21 and 35
brenda
-
brenda
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Pseudomonas aeruginosa stimulates expression of inducible nitric oxide synthase by A-549 cells
brenda
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-
brenda
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isoform I
brenda
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-
brenda
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isoform I
brenda
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-
-
brenda
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isoform I
brenda
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brenda
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thoracic, muscle
brenda
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brenda
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brenda
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-
-
brenda
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-
brenda
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-
brenda
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-
brenda
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brenda
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-
brenda
-
isoform I
brenda
-
Ca2+-dependent isoform
brenda
-
neuronal enzyme
brenda
-
-
brenda
-
brenda
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-
-
brenda
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brenda
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-
440190, 440191, 440192, 440196, 440197, 440198, 440203, 440210, 440212, 440213, 440220, 440228, 440232, 440236, 671278, 686293 brenda
-
brenda
-
isoform I
brenda
-
Ca2+-dependent isoform
brenda
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neuronal enzyme
brenda
-
nNOS
brenda
nNOS is the predominant isozyme in brain
brenda
-
from rats with unilateral depletion of dopamine in the substantia nigra compacta treated with L-DOPA at 30 mg/kg body weight for 34 days, nNOS expression is restricted to neurons
brenda
hypothalamic paraventricular nucleus and tanycytes
brenda
visual cortex, use of the NADPH-d histochemistry technique to evaluate the expression of NOS across the nervous system
brenda
-
-
-
brenda
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-
-
brenda
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Ca2+-dependent isoform
-
brenda
-
from rats with unilateral depletion of dopamine in the substantia nigra compacta treated with L-DOPA at 30 mg/kg body weight for 34 days, nNOS expression is restricted to neurons
-
brenda
-
hypothalamic paraventricular nucleus and tanycytes
-
brenda
-
visual cortex, use of the NADPH-d histochemistry technique to evaluate the expression of NOS across the nervous system
-
brenda
-
-
brenda
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isoform I
brenda
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-
brenda
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cerebrum shows higher activity than cerebellum
brenda
-
-
brenda
-
brenda
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cerebrum shows higher activity than cerebellum
brenda
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cerebrum shows higher activity than cerebellum
-
brenda
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-
-
brenda
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-
brenda
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-
brenda
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the localization of NADPH-diaphorase and NO synthase is identical in the snail nervous system
brenda
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-
brenda
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brenda
the localization of NADPH-diaphorase and NO synthase is identical in the snail nervous system
brenda
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-
brenda
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-
brenda
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-
brenda
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-
brenda
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nNOS
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-
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-
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brenda
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brenda
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-
brenda
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brenda
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brenda
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nNOS
brenda
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-
brenda
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-
-
brenda
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brenda
iNOS is more frequently expressed in osteoarthritic than in normal chondrocytes, iNOS expression and activity in osteoarthritic chondrocytes is sub-maximal
brenda
nNOS is more frequently expressed in normal than in osteoarthritic chondrocytes
brenda
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-
brenda
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-
brenda
dental papilla cells (DPCs) are mesenchymal cells that are surrounded by the enamel organ during tooth development
brenda
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dental papilla cells (DPCs) are mesenchymal cells that are surrounded by the enamel organ during tooth development
-
brenda
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-
brenda
human umbilical vein endothelial cells
brenda
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NOS3
brenda
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brenda
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-
brenda
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-
brenda
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constitutive, from pulmonary artery
brenda
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isoform III
brenda
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aorta, cell culture
brenda
comparison of endothelial and neuronal isoform
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-
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brenda
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-
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umbilical vein cells
brenda
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isoform III
brenda
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liver, lung, adrenal glandcolon, isoform II
brenda
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lung, uterus, stomach
brenda
-
endothelial enzyme
brenda
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specific isozyme eNOS
brenda
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vascular, constitutive expression of the endothelial isozyme in endothelial cells
brenda
-
-
brenda
-
isoform III
brenda
-
aorta, cell culture
brenda
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liver, lung, adrenal glandcolon, isoform II
brenda
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eNOS, endothelial cells of blood vessels
brenda
-
-
brenda
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isoform III
brenda
-
liver, lung, adrenal glandcolon, isoform II
brenda
-
lung, uterus, stomach
brenda
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endothelial enzyme
brenda
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-
-
brenda
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isoform III
brenda
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lung, uterus, stomach
brenda
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-
brenda
-
brenda
coeliac ganglia
brenda
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coeliac ganglia
-
brenda
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subesophageal and prothoracic
brenda
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eNOS
brenda
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brenda
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-
brenda
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isoform II
brenda
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isoform II
brenda
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brenda
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isoform II
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-
brenda
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brenda
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brenda
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-
brenda
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brenda
-
estradiol regulates the nitrergic system in the supraoptic and paraventricular hypothalamic nuclei under acute osmotic stress conditions, but the effects specifically depend on the anatomical subregions and different estrogen receptors
brenda
neurons of several nuclei of the hypothalamus, such as the arcuate nucleus (ARC) and paraventricular nucleus (PVN)
brenda
-
neurons of several nuclei of the hypothalamus, such as the arcuate nucleus (ARC) and paraventricular nucleus (PVN)
-
brenda
-
macula densa cells, isoform I
brenda
-
anterior, iNOS
brenda
-
-
brenda
-
-
brenda
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brenda
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renal cortex
brenda
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macula densa cells, isoform I
brenda
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renal cortex
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brenda
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macula densa cells, isoform I
brenda
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-
brenda
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-
brenda
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-
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brenda
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inducible isoform
brenda
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-
brenda
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-
-
brenda
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-
brenda
temporal expression of hepatic iNOS in liver cirrhosis, induced in rats by chronic bile duct ligation, overview
brenda
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brenda
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brenda
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brenda
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brenda
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-
brenda
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brenda
alveolar
brenda
-
-
brenda
-
in liver, lung, kidney, isoform II
brenda
-
inducible enzyme
brenda
-
NOS2
brenda
-
-
brenda
-
in liver, lung, kidney, isoform II
brenda
-
RAW 264.7 cells
brenda
RAW 264.7 cells
brenda
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Ca2+-independent form
brenda
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cytokine-activated
brenda
cytokine-activated
brenda
-
bone marrow-derived
brenda
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iNOS
brenda
-
-
brenda
-
in liver, lung, kidney, isoform II
brenda
-
cytokine-activated
brenda
-
inducible enzyme
brenda
iNOS is the predominant isozyme in macrophages
brenda
-
-
-
brenda
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strong histohemical labelling in sensory fibre branches of segmental nerves and in each of the sensory longitudinal axon bundles of ventral nerve cord ganglia. NADPH-diaphorase positive central sensory cells can be identified from among which the putative tactile receptors are characterized by constant, strong staining
brenda
-
isozyme NOS1
brenda
-
strong histohemical labelling in sensory fibre branches of segmental nerves and in each of the sensory longitudinal axon bundles of ventral nerve cord ganglia. NADPH-diaphorase positive central sensory cells can be identified from among which the putative tactile receptors are characterized by constant, strong staining
brenda
-
-
brenda
comparison of endothelial and neuronal isoform
brenda
-
-
brenda
-
-
brenda
-
-
brenda
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peripheral nitrergic nerves, isoform I
brenda
-
isozyme NOS1
brenda
-
amacrine
brenda
-
-
brenda
-
brenda
-
central nervous system, natural variant with 105-amino acid deletion in the heme-binding domain
brenda
-
neuronal NOS, nNOS
brenda
-
nNOS
brenda
-
-
brenda
-
brenda
-
peripheral nitrergic nerves, isoform I
brenda
-
neuronal NOS, nNOS
brenda
neurons of several nuclei of the hypothalamus, such as the arcuate nucleus (ARC) and paraventricular nucleus (PVN)
brenda
nitrergic neurons in the rat stomach, the myenteric cell bodies have single axons, type I morphology and a wide range of sizes. Nitrergic terminals do not provide baskets of terminals around myenteric neurons. The nitrergic neuron populations in the stomach supply the muscle layers and intramural arteries, but, unlike in the intestine, gastric interneurons do not express nNOS
brenda
the NADPH-d histochemistry stains a selective population of neurons in the brain. The staining allows the visualization of the dendritic tree, resembling a Golgi impregnation, and the cells are distributed sparsely in the cortical tissue, allowing their unbiased identification and reconstruction, quantitative analysis, overview
brenda
-
nitrergic neurons in the rat stomach, the myenteric cell bodies have single axons, type I morphology and a wide range of sizes. Nitrergic terminals do not provide baskets of terminals around myenteric neurons. The nitrergic neuron populations in the stomach supply the muscle layers and intramural arteries, but, unlike in the intestine, gastric interneurons do not express nNOS
-
brenda
-
-
-
brenda
-
neurons of several nuclei of the hypothalamus, such as the arcuate nucleus (ARC) and paraventricular nucleus (PVN)
-
brenda
-
the NADPH-d histochemistry stains a selective population of neurons in the brain. The staining allows the visualization of the dendritic tree, resembling a Golgi impregnation, and the cells are distributed sparsely in the cortical tissue, allowing their unbiased identification and reconstruction, quantitative analysis, overview
-
brenda
-
peripheral nitrergic nerves, isoform I
brenda
-
of central ganglia
brenda
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polymorphonuclear
brenda
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peritoneal polymorphonuclear
brenda
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polymorphonuclear neutrophils, PMN
brenda
from rats at different ages. Odontoblasts are strongly stained for NADPH-d. The staining intensity of odontoblasts near the future cusp and root is higher than that of other locations of the first molar. Odontoblasts in the first molar from 3-month-old rats are also positive for NADPH-d staining. Odontoblasts in the first molar from 8-month-old rats are weakly positive for NADPH-d staining. Semiquantitative evaluation results of NADPH-d staining suggests that NOS may be involved in the differentiation and function of odontoblasts
brenda
-
from rats at different ages. Odontoblasts are strongly stained for NADPH-d. The staining intensity of odontoblasts near the future cusp and root is higher than that of other locations of the first molar. Odontoblasts in the first molar from 3-month-old rats are also positive for NADPH-d staining. Odontoblasts in the first molar from 8-month-old rats are weakly positive for NADPH-d staining. Semiquantitative evaluation results of NADPH-d staining suggests that NOS may be involved in the differentiation and function of odontoblasts
-
brenda
-
-
brenda
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islet cells, isoform I
brenda
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islet cells, isoform I
brenda
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islet cells, isoform I
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
-
brenda
-
distribution, overview, in retinorecipient tectal layer, before and after axotomy and fibroblast growth factor-2 application
brenda
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constitutive, soluble form
brenda
-
constitutive, soluble form
-
brenda
-
isozyme NOS3
brenda
-
-
brenda
-
lumbar spinal cord
brenda
-
isoform I
brenda
-
nNOS, nerve cell bodies and neuronal fibers
brenda
-
isoform I
brenda
-
isoform I
brenda
-
red pulp, eosinophils and neutrophils, isoform II
brenda
-
red pulp, eosinophils and neutrophils, isoform II
brenda
-
iNOS
brenda
-
red pulp, eosinophils and neutrophils, isoform II
brenda
nitrergic neurons in the rat stomach comprising similar proportions of myenteric neurons, about 30%, in all gastric regions, e.g. the longitudinal, circular and oblique layers of the external muscle, the muscularis mucosae and arteries within the gastric wall
brenda
-
nitrergic neurons in the rat stomach comprising similar proportions of myenteric neurons, about 30%, in all gastric regions, e.g. the longitudinal, circular and oblique layers of the external muscle, the muscularis mucosae and arteries within the gastric wall
-
brenda
-
isoform I
brenda
-
isoform I
brenda
-
isoform I
brenda
-
brenda
-
-
-
brenda
-
main nervous structures (buccal nerve and nerve plate) in the bud of the tentacle
brenda
high expression in cephalic tentacle
brenda
-
NADPH-diaphorase activity is found in the midpiece of the spermatozoa tail and epithelial cells of all intratesticular and excurrent ducts analyzed, except for nonciliated cells of the efferent ductules. Immunostaining shows cell-specific localization in the efferent ductules and region- and cell-specific localization in the epididymal duct
brenda
eNOS immunoreactivity is detected in germ cells, Sertoli cells, Leydig cells and vascular endothelial cells of the testis
brenda
iNOS positive cells are detected in seminiferous epithelial cells, especially in germ cells of the testis
brenda
additional information
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3 isoforms: 1. neuronal, soluble isoform I is constitutively expressed in brain and other tissues and Ca2+-regulated, 2. soluble isoform II is usually not constitutively expressed, but inducible in macrophages and other cells, 3. isoform III is membrane-bound and expressed in endothelial cells
brenda
additional information
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localization and distribution of nitric oxide synthase and other neuronal markers in the podia of Holothuria arguinensis, detailed overview. The podia terminal end is the most specialized area and is characterized by a specific nervous arrangement, consisting of a distinct nerve plate, rich in cells and fibers containing potential sensory cells staining positively for neuronal markers. In sea cucumbers, cells with morphological characteristics typical of sensory cells have been described in the tentacles, tube feet, and papillae. NADPH-diaphorase histochemistry and NOS immunohistochemistry. The NADPH-diaphorase staining and the anti-NOS antibody show an overall similar distribution in the tentacle. In the stem, the longitudinal buccal nerve and the buccal nerve are strongly reactive to both markers. The mesothelium is also positive for NADPH-d and anti-NOS. In the bud, the two methods reveal that NOS is present in both the buccal nerve and mesothelium
brenda
additional information
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3 isoforms: 1. neuronal, soluble isoform I is constitutively expressed in brain and other tissues and Ca2+-regulated, 2. soluble isoform II is usually not constitutively expressed, but inducible in macrophages and other cells, 3. isoform III is membrane-bound and expressed in endothelial cells
brenda
additional information
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3 isoforms: 1. neuronal, soluble isoform I is constitutively expressed in brain and other tissues and Ca2+-regulated, 2. soluble isoform II is usually not constitutively expressed, but inducible in macrophages and other cells, 3. isoform III is membrane-bound and expressed in endothelial cells
brenda
additional information
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3 distinct isoforms: 1. a membrane-associated, constitutive enzyme from tha vascular endothelium, 2. a soluble, constitutive enzyme from neuronal cells, 3. an endotoxin- and cytokine-inducible enzyme exemplified by that from murine macrophages
brenda
additional information
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activity of constitutive enzymes is regulated by binding of calmodulin and Ca2+, the inducible enzyme is regulated by binding of calmodulin, not by Ca2+
brenda
additional information
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nNOS splicing variants tissue distribution, immunohistochemic analysis, overview
brenda
additional information
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no activity in gill, intestine, and liver
brenda
additional information
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3 isoforms: 1. neuronal, soluble isoform I is constitutively expressed in brain and other tissues and Ca2+-regulated, 2. soluble isoform II is usually not constitutively expressed, but inducible in macrophages and other cells, 3. isoform III is membrane-bound and expressed in endothelial cells
brenda
additional information
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3 isoforms: 1. neuronal, soluble isoform I is constitutively expressed in brain and other tissues and Ca2+-regulated, 2. soluble isoform II is usually not constitutively expressed, but inducible in macrophages and other cells, 3. isoform III is membrane-bound and expressed in endothelial cells
brenda
additional information
expression analysis in isolated hepatocytes, healthy liver, and cirrhotic liver, overview
brenda
additional information
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nNOS splicing variants tissue distribution, immunohistochemic analysis, overview
brenda
additional information
determination of NADPH diaphorase staining in preganglionic terminals, staining generally ascribed to NADH diaphorase activity in aldehyde-treated tissues
brenda
additional information
distribution of NADPH-d-positive neurons and fibers in the paraventricular nucleus (PVN) after saline and leptin treatment, in situ overview
brenda
additional information
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distribution of NADPH-d-positive neurons and fibers in the paraventricular nucleus (PVN) after saline and leptin treatment, in situ overview
brenda
additional information
immunohistochemic enzyme and NADPH histochemic analysis, distributions of nNOS neurons and their terminals throughout the rat stomach, overview. NADPH diaphorase is the colour reaction that reveals the presence of NADPH oxidases, and because nNOS is a NADPH oxidase, it is revealed by NADPHd histochemistry
brenda
additional information
NO synthase (NOS) immunohistochemic analysis and nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) staining in vivo in rat odontoblasts. The expression of neuronal NOS and endothelial NOS is upregulated during the odontoblastic differentiation of DPCs
brenda
additional information
pattern of NADPH-d neuropil staining and pattern of astrocyte reactivity, qualitative and quantitative analysis, overview. MeHg-intoxicated animals display a significant decrease of NADPH-d neuropil reactivity across the visual cortex when compared to controls
brenda
additional information
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NO synthase (NOS) immunohistochemic analysis and nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) staining in vivo in rat odontoblasts. The expression of neuronal NOS and endothelial NOS is upregulated during the odontoblastic differentiation of DPCs
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brenda
additional information
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immunohistochemic enzyme and NADPH histochemic analysis, distributions of nNOS neurons and their terminals throughout the rat stomach, overview. NADPH diaphorase is the colour reaction that reveals the presence of NADPH oxidases, and because nNOS is a NADPH oxidase, it is revealed by NADPHd histochemistry
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brenda
additional information
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determination of NADPH diaphorase staining in preganglionic terminals, staining generally ascribed to NADH diaphorase activity in aldehyde-treated tissues
-
brenda
additional information
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3 isoforms: 1. neuronal, soluble isoform I is constitutively expressed in brain and other tissues and Ca2+-regulated, 2. soluble isoform II is usually not constitutively expressed, but inducible in macrophages and other cells, 3. isoform III is membrane-bound and expressed in endothelial cells
-
brenda
additional information
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distribution of NADPH-d-positive neurons and fibers in the paraventricular nucleus (PVN) after saline and leptin treatment, in situ overview
-
brenda
additional information
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pattern of NADPH-d neuropil staining and pattern of astrocyte reactivity, qualitative and quantitative analysis, overview. MeHg-intoxicated animals display a significant decrease of NADPH-d neuropil reactivity across the visual cortex when compared to controls
-
brenda
additional information
no expression in salivary glands and the gland of Leiblein
brenda
additional information
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no expression in salivary glands and the gland of Leiblein
brenda
additional information
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3 isoforms: 1. neuronal, soluble isoform I is constitutively expressed in brain and other tissues and Ca2+-regulated, 2. soluble isoform II is usually not constitutively expressed, but inducible in macrophages and other cells, 3. isoform III is membrane-bound and expressed in endothelial cells
brenda
additional information
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immunohistochemic analysis of enzyme distribution, overview
brenda
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malfunction
attachment of N-glycan to the Asn695 residue inhibits activity by disturbing electron transfer. N-glycosylated iNOS consumes NADPH more slowly than the unliganded enzyme. Mutating Asn695 to Gln695 yields an iNOS that exhibits greater enzyme activity compared to wild-type. NO produced by N695Q iNOS-transformed HEK293 cells is 1.32fold greater than that of N-glycosylated iNOS, the increased enzyme activity of N695Q iNOS in HEK293 cells was caused by loss of N-glycan
malfunction
inhibition of NOS function by NOS inhibitor L-NG-monomethyl arginine (L-NMMA) results in reduced formation of mineralized nodules and expression of dentin sialophosphoprotein (DSPP) and dentin matrix protein (DMP1) during dental papilla cell (DPC) differentiation
malfunction
role of oxidative stress in the dysfunction of the placental endothelial nitric oxide synthase in preeclampsia (PE), multifactorial pregnancy disease, characterized by new-onset gestational hypertension with (or without) proteinuria or end-organ failure, exclusively observed in humans. PE pathophysiology can result from abnormal placentation due to a defective trophoblastic invasion and an impaired remodeling of uterine spiral arteries, leading to a poor adaptation of utero-placental circulation. This would be associated with hypoxia/ reoxygenation phenomena, oxygen gradient fluctuations, altered antioxidant capacity, oxidative stress, and reduced nitric oxide (NO) bioavailability. This results in part from the reaction of NO with the radical anion superoxide, which produces peroxynitrite ONOO-, a powerful pro-oxidant and inflammatory agent. Another mechanism is the progressive inhibition of the placental endothelial nitric oxide synthase (eNOS) by oxidative stress, which results in eNOS uncoupling via several events such as a depletion of the eNOS substrate L-arginine due to increased arginase activity, an oxidation of the eNOS cofactor tetrahydrobiopterin (BH4), or eNOS posttranslational modifications (for instance by S-glutathionylation). The uncoupling of eNOS triggers a switch of its activity from a NO-producing enzyme to a NADPH oxidase-like system generating superoxide, thereby potentiating ROS production and oxidative stress. Moreover, in PE placentas, eNOS can be posttranslationally modified by lipid peroxidation-derived aldehydes such as 4-oxononenal (ONE) a highly bioreactive agent, able to inhibit eNOS activity and NO production. Analysis of the dysfunction of placental eNOS evoked by oxidative stress and lipid peroxidation products, and the potential consequences on PE pathogenesis, detailed overview. Oxidative stress is thought to play a pivotal role in the decreased NO bioavailability in PE pathophysiology, via several mechanisms including an inhibition of eNOS (eNOS uncoupling) and subsequent defect of NO biosynthesis, or through the formation of peroxynitrite, via the reaction of NO with the radical anion superoxide. eNOS inhibition is associated with a decrease in endothelial-dependent relaxation in vitro and in vivo. Therapeutic perspectives targeting oxidative stress and NO/eNOS dysfunction
malfunction
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attachment of N-glycan to the Asn695 residue inhibits activity by disturbing electron transfer. N-glycosylated iNOS consumes NADPH more slowly than the unliganded enzyme. Mutating Asn695 to Gln695 yields an iNOS that exhibits greater enzyme activity compared to wild-type. NO produced by N695Q iNOS-transformed HEK293 cells is 1.32fold greater than that of N-glycosylated iNOS, the increased enzyme activity of N695Q iNOS in HEK293 cells was caused by loss of N-glycan
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malfunction
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inhibition of NOS function by NOS inhibitor L-NG-monomethyl arginine (L-NMMA) results in reduced formation of mineralized nodules and expression of dentin sialophosphoprotein (DSPP) and dentin matrix protein (DMP1) during dental papilla cell (DPC) differentiation
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metabolism
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activation of G protein-coupled estrogen receptor in the supraoptic and paraventricular nuclei of the hypothalamus inhibits the phosphorylation of ERK 1/2, which induces a decrease in NADPH-diaphorase expression
metabolism
synthesis of the signaling molecule nitric oxide
metabolism
the enzyme plays an important role in host defense system by catalyzing the production of nitric oxide
physiological function
eNOS selectively activates N-Ras but not K-Ras on the Golgi complex of T cells engaged with antigen-presenting cells by S-nitrosylation at Cys118
physiological function
si-RNA mediated knockdown of eNOS leads to a striking increase in AMP-activated protein kinase phosphorylation, homozygot eNOS knockout mice show a marked increase in AMP-activated protein kinase phosphorylation in liver and lung compared to wild type mice
physiological function
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the brain neuronal NOS and inducible NOS are respectively involved in the bombesin-induced secretion of noradrenaline and adrenaline from the adrenal medulla
physiological function
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developmental but not adult exposure to polychlorinated biphenyls significantly reduces NO synthase responses to hyperosmolality in neuroendocrine cells. Reduced NADPH diaphorase activity produced by in utero exposure persists in stimulated late adult rats concomitant with reduced osmoregulatory capacity
physiological function
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during muscle pain development, a significant contralateral increase in the number of NADPH-diaphorase reactive cells is accompanied by anipsilateral increase in c-Fos expression in lamina VII. NADPH-diaphorase reactive neurons of the contralateral ventral horn may be involved through commissural connections in the maintenance of the neuronal activity associated with acute muscle inflammation. During acute myositis, plastic changes in the ventral horn may activate the processes of disinhibition due to an increase in the number of NADPH-diaphorase reactive neurons in the spinal gray matter
physiological function
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estradiol regulates the nitrergic system in the supraoptic and paraventricular hypothalamic nuclei under acute osmotic stress conditions, but the effects specifically depend on the anatomical subregions and different estrogen receptors. The inhibition of estrogen receptor alpha enhances the effect of 1.5 M NaCl injection, inducing a further decrease in the number of NADPH-diaphorase-positive cells. The estrogen receptor beta agonist enhances and the estrogen receptor beta antagonist blocks the effect of NaCl injection on the number of NADPH-diaphorase-positive neurons in the supraoptic hypothalamic nuclei and in the medial magnocellular subdivision of the paraventricular hypothalamic nuclei
physiological function
endothelial nitric oxide synthase (eNOS) is responsible for maintaining systemic blood pressure, vascular remodeling and angiogenesis
physiological function
NADPH oxidases (NOX2/NOX4) and inducible nitric oxide synthase (iNOS) derived oxidative stress play a key role in psoriasis induced kidney dysfunction. NADPH oxidase (NOX2 and NOX4) isoforms, and inducible nitric oxidase synthase (iNOS) are elevated in the renal tissue under inflammatory conditions such as acute kidney injury and chronic kidney disease. These enzymes are capable of producing reactive oxygen species (ROS) in large quantities under inflammatory conditions, which may cause oxidative damage to biological macromolecules such as lipids, proteins and nucleic acids leading to malfunction of cellular structures through dysregulation of ion pumps, and enzymatic activity
physiological function
nitric-oxide synthase (NOS) is required in mammals to generate nitric-oxide for regulating blood pressure, synaptic response, and immune defense
physiological function
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the product nitric oxide may function as a co-transmitter in the central nervous system of Helix pomatia
physiological function
the product nitric oxide may function as a co-transmitter in the central nervous system of Helix pomatia
physiological function
in endothelium and placenta, NO is biosynthesized by the endothelial nitric oxide synthase (eNOS), and confers to endothelium its vasorelaxing and anti-aggregant properties. NO participates to placentation and the synthesis of the vascular endothelial growth factor (VEGF). NO plays an essential role in vascular homeostasis due to its vasodilatory effect. NO is synthesized by nitric oxide synthases (NOS), from L-arginine and molecular oxygen (O2). In short, the reaction allowing NO synthesis can be compared to two monooxygenation reactions. The first reaction consists of the oxidation of L-arginine. This reaction produces an intermediate, -OH-L-arginine, which is rapidly oxidized into L-citrulline. These two oxygenation reactions occur in parallel with a concomitant conversion of NADPH to NADP+. The electrons are supplied by NADPH, transferred to flavins (FAD and FMN) and calmodulin, then presented to heme, the catalytic center. Three NOS isoforms have been characterized, the neuronal NOS (nNOS or NOS1), the inducible NOS (iNOS or NOS2) and the endothelial NOS (eNOS or NOS3). NO released by endothelial cells in vivo causes a permanent vasodilation of the arterial tone that helps to regulate arterial pressure. During pregnancy, NO has a primary role in vasodilation and blood pressure regulation, placentation and VEGF synthesis. Oxidative stress impact on NO bioavailability, detailed overview. S-Glutathionylation can be promoted by NO, via mechanisms implicating S-nitrosoglutathione (GSNO) and thiyl radicals. S-glutathionylated proteins reversibly accumulate under oxidative stress conditions and can be rapidly reduced by reducing agents and glutaredoxins. S-glutathionylation alters the structure, folding and function of proteins, and can be considered as an adaptative and protective mechanism against the irreversible oxidation of cysteine residues during oxidative stress
physiological function
inducible nitric oxide synthase (iNOS) is a key inflammatory factor. It functions in both acute and chronic inflammation. Nitric oxide (NO) is a signaling mediator with many diverse and often contradictory biological activities. In mammals, NO is produced by a family of nitric oxide synthase (NOS). The NOS family includes neuronal nitric oxide synthase (nNOS, type I), inducible nitric oxide synthase (iNOS, type II), and endothelial nitric oxide synthase (eNOS, type III). All these three NOS isoforms catalyze a similar reaction. Consuming NADPH and O2, NOS oxidizes L-arginine into L-citrulline and releases NO. The reaction is an oxidation-reduction reaction, and electron transfer plays a vital role. Inducible nitric oxide synthase (iNOS) plays critical roles in the inflammatory response and host defense. The essence of nitric oxide synthase catalytic reaction is an electron transfer process, which involves a series of conformational changes, and the linker between the flavin mononucleotide-binding domain and the flavin adenine dinucleotide-binding domain plays vital roles in the conformational changes. Residue Asn695 is part of the linker. Enzyme iNOS is N-glycosylated at its Asn695 residue and N-glycosylation of Asn695 might suppress iNOS activity by disturbing electron transfer
physiological function
leptin-induced NO production in tanycytes may affect the neurogenesis occurs in the hypothalamus. The increased NADPH-d staining in both the arcuate nucleus (ARC) and paraventricular nucleus (PVN) of the leptin-treated rats suggests that both the PVN and ARC may be important centers in the hypothalamus for the leptin action, mediated at least in part by increased NO synthesis. The present observations also suggest that leptin may activate NOS thereby resulting in increased production of NO in hypothalamic tanycytes, possibly affecting the release of neurohormones and hypothalamic neurogenesis
physiological function
nitrergic neurons in the rat stomach supply the longitudinal, circular and oblique layers of the external muscle, the muscularis mucosae and arteries within the astric wall. A small number of fibres are in the mucosa. All the neurons appear to have a single axon and in most cases a type I morphology. Type I is the typical morphology of enteric motor neurons that supply the muscle of the gastrointestinal tract. Neuronal nitric oxide synthase (nNOS) neurons do not supply terminals around myenteric nerve cells, whether NADPHd histochemistry or nNOS immunohistochemistry is used to locate the terminals of nNOS neurons. Thus, nNOS appears to be exclusively in motor neurons supplying the muscle of the rat stomach. This may be different from other species. nNOS immunoreactivity identifies 4 classes of motor neurons that supply the muscle of the rat stomach, an analysis of cell body sizes does not identify separate grouping of neurons. The rat stomach harbours large numbers of nNOS neurons, all or almost all of which are motor neurons supplying the external muscle, the muscularis mucosae and intramural arteries
physiological function
nitric oxide (NO) is a key cellular signaling mediator involved in the overall regulation of physiological homeostasis and in numerous pathological processes related to cardiovascular, nervous and immune systems. NO is formed together with L-citruline by nitric-oxide synthases (NOS) that catalyze the oxidation of L-arginine using nicotinamide adenine dinucleotide phosphate (NADPH), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), tetrahydrobiopterin (BH4) and O2 as cofactors. The overall catalytic process is driven by reducing equivalents supplied by NADPH. NOS are composed of a reductase domain which binds NADPH and the two flavins and an oxygenase domain which binds the heme, L-arginine, BH4 and O2. These two domains are connected by the calmodulin-binding domain. The electron flow leading to the formation of NO is initiated by the binding of NADPH to the reductase domain and requires the binding of calmodulin for efficient FMN to heme electron transfer. NO is produced by three NOS isoforms, the two first are constitutive, neuronal (nNOS) and endothelial (eNOS) whereas the third one is inducible (iNOS). Efficient photoactivatable NADPH analogues targeting NOS can have important implications for generating apoptosis in tumor cells or modulating NO-dependent physiological processes
physiological function
nitric oxide (NO) is a ubiquitous gaseous cellular messenger with multiple physiological roles in the brain, such as synaptic plasticity, neurotransmission, neuronal communication, neurogenesis, learning, and memory. NO can be generated by three different isoforms of the enzyme nitric oxide synthase (NOS): neuronal NOS (nNOS), endothelial NOS (eNOS), and inducible NOS (iNOS), from L-arginine as the substrate and molecular oxygen and NADPH as cosubstrates
physiological function
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nitric oxide (NO) is synthesized from L-arginine by the NADPH-dependent enzyme nitric oxide synthase (NOS), and is involved in many essential biological functions including immune defense, vascular regulation, muscle relaxation, and neuromodulation, and neurotransmission
physiological function
nitric oxide (NO) regulates the functions of multiple cells and organ tissues, including stem cell differentiation and bone formation, role of nitric oxide in odontoblastic differentiation of rat dental papilla cells, overview. NO regulates the odontoblastic differentiation of dental papilla cells (DPCs), thereby influencing dentin formation and tooth development. The NO donor S-nitroso-N-acetylpenicillamine (SNAP) promotes the viability of DPCs. Extracellular matrix mineralization and odontogenic markers expression are elevated by SNAP at low concentrations and suppressed at high concentration. Blocking the generation of cyclic guanosine monophosphate (cGMP) with 1H-(1,2,4)oxadiazolo-(4,3-a)quinoxalin-1-one (ODQ) abolishes the positive influence of SNAP on the odontoblastic differentiation of DPCs
physiological function
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nitrergic neurons in the rat stomach supply the longitudinal, circular and oblique layers of the external muscle, the muscularis mucosae and arteries within the astric wall. A small number of fibres are in the mucosa. All the neurons appear to have a single axon and in most cases a type I morphology. Type I is the typical morphology of enteric motor neurons that supply the muscle of the gastrointestinal tract. Neuronal nitric oxide synthase (nNOS) neurons do not supply terminals around myenteric nerve cells, whether NADPHd histochemistry or nNOS immunohistochemistry is used to locate the terminals of nNOS neurons. Thus, nNOS appears to be exclusively in motor neurons supplying the muscle of the rat stomach. This may be different from other species. nNOS immunoreactivity identifies 4 classes of motor neurons that supply the muscle of the rat stomach, an analysis of cell body sizes does not identify separate grouping of neurons. The rat stomach harbours large numbers of nNOS neurons, all or almost all of which are motor neurons supplying the external muscle, the muscularis mucosae and intramural arteries
-
physiological function
-
inducible nitric oxide synthase (iNOS) is a key inflammatory factor. It functions in both acute and chronic inflammation. Nitric oxide (NO) is a signaling mediator with many diverse and often contradictory biological activities. In mammals, NO is produced by a family of nitric oxide synthase (NOS). The NOS family includes neuronal nitric oxide synthase (nNOS, type I), inducible nitric oxide synthase (iNOS, type II), and endothelial nitric oxide synthase (eNOS, type III). All these three NOS isoforms catalyze a similar reaction. Consuming NADPH and O2, NOS oxidizes L-arginine into L-citrulline and releases NO. The reaction is an oxidation-reduction reaction, and electron transfer plays a vital role. Inducible nitric oxide synthase (iNOS) plays critical roles in the inflammatory response and host defense. The essence of nitric oxide synthase catalytic reaction is an electron transfer process, which involves a series of conformational changes, and the linker between the flavin mononucleotide-binding domain and the flavin adenine dinucleotide-binding domain plays vital roles in the conformational changes. Residue Asn695 is part of the linker. Enzyme iNOS is N-glycosylated at its Asn695 residue and N-glycosylation of Asn695 might suppress iNOS activity by disturbing electron transfer
-
physiological function
-
leptin-induced NO production in tanycytes may affect the neurogenesis occurs in the hypothalamus. The increased NADPH-d staining in both the arcuate nucleus (ARC) and paraventricular nucleus (PVN) of the leptin-treated rats suggests that both the PVN and ARC may be important centers in the hypothalamus for the leptin action, mediated at least in part by increased NO synthesis. The present observations also suggest that leptin may activate NOS thereby resulting in increased production of NO in hypothalamic tanycytes, possibly affecting the release of neurohormones and hypothalamic neurogenesis
-
physiological function
-
nitric oxide (NO) is a ubiquitous gaseous cellular messenger with multiple physiological roles in the brain, such as synaptic plasticity, neurotransmission, neuronal communication, neurogenesis, learning, and memory. NO can be generated by three different isoforms of the enzyme nitric oxide synthase (NOS): neuronal NOS (nNOS), endothelial NOS (eNOS), and inducible NOS (iNOS), from L-arginine as the substrate and molecular oxygen and NADPH as cosubstrates
-
physiological function
-
nitric oxide (NO) regulates the functions of multiple cells and organ tissues, including stem cell differentiation and bone formation, role of nitric oxide in odontoblastic differentiation of rat dental papilla cells, overview. NO regulates the odontoblastic differentiation of dental papilla cells (DPCs), thereby influencing dentin formation and tooth development. The NO donor S-nitroso-N-acetylpenicillamine (SNAP) promotes the viability of DPCs. Extracellular matrix mineralization and odontogenic markers expression are elevated by SNAP at low concentrations and suppressed at high concentration. Blocking the generation of cyclic guanosine monophosphate (cGMP) with 1H-(1,2,4)oxadiazolo-(4,3-a)quinoxalin-1-one (ODQ) abolishes the positive influence of SNAP on the odontoblastic differentiation of DPCs
-
additional information
residue Asn695 of the mouse iNOS locates at the hinge segment which connects the FMN-binding domain to the FAD-binding domain. The electrostatic and flexibility properties of hinge segment are critical for electron transfer from CPR to its redox partners. For mouse iNOS, N-glycosylation of Asn695 might disturb electron transfer by influencing the electrostatic and flexibility properties of the hinge segment
additional information
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residue Asn695 of the mouse iNOS locates at the hinge segment which connects the FMN-binding domain to the FAD-binding domain. The electrostatic and flexibility properties of hinge segment are critical for electron transfer from CPR to its redox partners. For mouse iNOS, N-glycosylation of Asn695 might disturb electron transfer by influencing the electrostatic and flexibility properties of the hinge segment
additional information
the large numbers of nNOS neurons and the density of innervation of the circular muscle and pyloric sphincter suggest that there is a finely graded control of motor function in the stomach by the recruitment of different numbers of inhibitory motor neurons
additional information
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the large numbers of nNOS neurons and the density of innervation of the circular muscle and pyloric sphincter suggest that there is a finely graded control of motor function in the stomach by the recruitment of different numbers of inhibitory motor neurons
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additional information
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residue Asn695 of the mouse iNOS locates at the hinge segment which connects the FMN-binding domain to the FAD-binding domain. The electrostatic and flexibility properties of hinge segment are critical for electron transfer from CPR to its redox partners. For mouse iNOS, N-glycosylation of Asn695 might disturb electron transfer by influencing the electrostatic and flexibility properties of the hinge segment
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