Information on EC 1.14.13.39 - nitric-oxide synthase (NADPH dependent)

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

EC NUMBER
COMMENTARY
1.14.13.39
-
RECOMMENDED NAME
GeneOntology No.
nitric-oxide synthase (NADPH dependent)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 L-arginine + 2 NADPH + 2 H+ + 2 O2 = 2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O
show the reaction diagram
(1a)
-
-
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
possible mechanism
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
cytochrome P-450 enzyme
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
alignment of heme-binding domain amino acid sequences of NOS
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
dimerization is required, activation of NO-synthesis by enabling electron transfer between the reductase and the oxygenase domains, isolated monomers are inactive
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
relation between structure, function and binding of prosthetic groups during dissociation, unfolding and renaturation
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
isoform I and II are regulated by Ca2+/calmodulin, isoform II is Ca2+-independent, but requires calmodulin, inducible by cytokines
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
structure-function study of macrophage enzyme
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
subunits align in head-to-head manner with oxygenase domains interacting to form a dimer and reductase domains existing as independent extensions
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
reaction and kinetic mechanism
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
analysis of catalytic site by Fourier transform infrared spectroscopy, extent of modulation of vibrational modes upon photolysis of CO compound
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
analysis of transition states via stopped-flow spectroscopy
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
analysis of transition states via stopped-flow spectroscopy
P29477
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
overall reaction
-
-
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
interaction and electrontransfer between enzyme domains and bound cofactors calmodulin, FMN, FAD, tetrahydrobiopterin, heme, and NADPH, overview
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
interaction and electrontransfer between enzyme domains and bound cofactors calmodulin, FMN, FAD, tetrahydrobiopterin, heme, and NADPH, overview
P29474
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
interaction and electrontransfer between enzyme domains and bound cofactors calmodulin, FMN, FAD, tetrahydrobiopterin, heme, and NADPH, overview
P29476
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
reaction mechanism, NO release and transport, overview, NO formation through sequential electron transfer and the oxidation of L-arginine, in the catalytic process, FMN, FAD, and tetrahydrobiopterin are required as coenzymes, and the presence of Ca2+/calmodulin can aid the electron transfer, isozymes NOS1 and NOS3 perform a similar reaction mechanism
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
reaction mechanism, the reaction of the enzyme with oxygen is fast and takes place within several steps, separated by ephemeral intermediates, two short-lived oxy-compounds OxyI and OxyII
-
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
the key structural features that are involved in the substrate and active site interaction are highly conserved, e.g. residues Pro214, Glu235, Trp234, Tyr237, Asn246, and Gln129, substrate binding structure and mechanism, overview
-
2 Nomega-hydroxy-L-arginine + NADPH + H+ + 2 O2 = 2 L-citrulline + 2 nitric oxide + NADP+ + 2 H2O
show the reaction diagram
(1b)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
L-citrulline-nitric oxide cycle
-
-
Metabolic pathways
-
-
nitric oxide biosynthesis (plants)
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arginine,NADPH:oxygen oxidoreductase (nitric-oxide-forming)
Binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin. This eukaryotic enzyme, which is found in plants [4] and animals [1-3], consists of oxygenase and reductase domains that are linked via a regulatory calmodulin-binding domain. Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. May produce superoxide under certain conditions [3]. cf. EC 1.14.13.165, nitric-oxide synthase [NAD(P)H dependent].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
bacterial nitric oxide synthase
-
-
bacterial nitric-oxide synthase
-
-
bacterial nitric-oxide synthase
-
-
cb-NOS
-
isoform I, constitutive, from brain
cytokine inducible NOS
-
-
e-NOS
-
endothelial isoform III
e-NOS
-
endothelial isoform III
EC-NOS
-
isoform III, in endothelial cells
endothelial nitric oxide synthase
P29473
-
endothelial nitric oxide synthase
-
-
endothelial nitric oxide synthase
P29474
-
endothelial nitric oxide synthase
Q62600
-
endothelial nitric oxide synthase
P70313
-
endothelial nitric oxide synthase
-
-
endothelial nitric oxide synthase
Q62600
isoform
endothelial nitric-oxide synthase
-
-
endothelial nitric-oxide synthase
P29473
-
endothelial nitric-oxide synthase
-
-
endothelial nitric-oxide synthase
-
-
endothelial NO synthase
-
-
endothelial NOS
-
-
endothelial NOS
-
-
endothelial NOS
P29474
isoform
endothelial NOS
-
-
endothelial NOS
-
-
endothelium-derived relaxation factor-forming enzyme
-
-
-
-
endothelium-derived relaxing factor synthase
-
-
-
-
eNOS
-
-
eNOS
P29473
-
eNOS
Q62600
-
eNOS
-
-
eNOS
P70313
-
eNOS
Q62600
isoform
i-NOS
-
isoform II, inducible
i-NOS
-
isoform II, inducible
i-NOS
-
isoform II, inducible
i-NOS
Q06518
isoform
i-NOS
Rattus norvegicus Sprague-Dawley
-
isoform II, inducible
-
inducible nitric oxide synthase
Q9BDQ7
-
inducible nitric oxide synthase
-
-
inducible nitric oxide synthase
P35228
-
inducible nitric oxide synthase
-
-
inducible nitric oxide synthase
-
-
inducible nitric oxide synthase
Q06518
-
inducible nitric oxide synthase
Q06518
isoform
inducible nitric-oxide synthase
-
-
inducible nitric-oxide synthase
P29477
-
inducible NO synthase
P35228
-
inducible NO synthase
-
-
inducible NO synthase
Q06518
-
inducible NOS
-
isoform
inducible NOS
-
-
inducible NOS
Q06518
isoform
iNOS
Q9BDQ7
-
iNOS
P35228
-
iNOS
P35228
isoform
iNOS
P29477
-
iNOS
Q06518
isoform
mitochondrial NO synthase
-
-
mitochondrial-specific nitric oxide synthase
-
-
mtNOS
-
-
mtNOS
-
-
n-NOS
-
isoform I, neuronal enzyme
n-NOS
P29476
isoform
n-NOS
Rattus norvegicus Sprague-Dawley
-
isoform I, neuronal enzyme
-
n-NOS
-
isoform I, neuronal enzyme
NADPH-diaphorase
-
-
-
-
neuronal nitric oxide synthase
-
-
neuronal nitric oxide synthase
-
-
neuronal nitric oxide synthase
P29475
-
neuronal nitric oxide synthase
-
-
neuronal nitric oxide synthase
-
-
neuronal nitric oxide synthase
P29475
-
neuronal nitric oxide synthase
P29476
-
neuronal nitric oxide synthase
Rattus norvegicus Wistar
-
-
-
neuronal nitric-oxide synthase
-
-
neuronal nitric-oxide synthase
-
-
neuronal nitric-oxide synthase
P29476
-
neuronal NO synthase
-
-
neuronal NO synthase
P29475
-
neuronal NO synthase
P29476
-
neuronal NOS
-
-
neuronal NOS
-
-
neuronal NOS
P29475
isoform
neuronal NOS
-
-
neuronal NOS
P29476
-
neuronal NOS
P29476
isoform
nitric oxid synthase
-
-
nitric oxide synthase
-
-
-
-
nitric oxide synthase
-
-
nitric oxide synthase
-
-
nitric oxide synthase
-
-
nitric oxide synthase
-
-
nitric oxide synthase
P29474, P29475, P35228
-
nitric oxide synthase
-
-
nitric oxide synthase
-
-
nitric oxide synthase
-
-
nitric oxide synthase
-
-
nitric oxide synthase-like protein
-
-
nitric oxide synthetase
-
-
-
-
nitric-oxide synthase
-
-
nitric-oxide synthase
-
-
nNOS
-
-
nNOS
P29475
isoform
nNOS
P29475
-
nNOS
Rattus norvegicus Wistar
-
-
-
NO synthase
-
-
-
-
NO synthase
-
-
NO synthase
Rattus norvegicus Wistar
-
-
-
NO synthase type I
P29475
nNOS
NO synthase type II
P35228
iNOS
NO synthase type III
P29474
eNOS
NOS-2
P35228
-
NOS1
-
-
NOS1
-
isoform1
NOS1
P29476
isozyme
NOS2
P35228
-
NOS2
-
isoform2
NOS2
-
-
NOS2
P29477
-
NOS3
-
isoform3
NOS3
Q62600
isozyme
synthetase, nitric oxide
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
125978-95-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
pathogenic bacterium responsible for causing anthrax
-
-
Manually annotated by BRENDA team
3 isoforms exist in bovine aortic endothelial cells differentiated by substrate specificity and Ca2+-dependence
-
-
Manually annotated by BRENDA team
endothelial isoform
-
-
Manually annotated by BRENDA team
fragment of iNOS
UniProt
Manually annotated by BRENDA team
isozymes eNOS and nNOS
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
mongrel cat
-
-
Manually annotated by BRENDA team
shelf fungus, collected from forest in Darjeeling, East Sikkim, India
-
-
Manually annotated by BRENDA team
expression in Pichia pastoris
-
-
Manually annotated by BRENDA team
inducible
-
-
Manually annotated by BRENDA team
isoform Nos2, inducible nitric oxide synthase
UniProt
Manually annotated by BRENDA team
isozyme eNOS
UniProt
Manually annotated by BRENDA team
isozymes NOS1 and NOS3
-
-
Manually annotated by BRENDA team
neuronal enzyme, full-length enzyme, FAD-FMN-domain, FAD-NADPH-domain
-
-
Manually annotated by BRENDA team
constitutive enzyme
-
-
Manually annotated by BRENDA team
3 isoforms exist in mouse macrophages differentiated by substrate specificity and Ca2+-dependence
-
-
Manually annotated by BRENDA team
C57/BL 6J mice
-
-
Manually annotated by BRENDA team
C57BL/6 wild-type mice
-
-
Manually annotated by BRENDA team
cytokine-inducible in macrophage
-
-
Manually annotated by BRENDA team
cytokine-inducible in macrophage
UniProt
Manually annotated by BRENDA team
different splice isoforms of nNOS, e.g. splicing variant nNOSalpha
-
-
Manually annotated by BRENDA team
inducible enzyme
UniProt
Manually annotated by BRENDA team
inducible oxygenase domain
UniProt
Manually annotated by BRENDA team
isozyme iNOS
-
-
Manually annotated by BRENDA team
isozyme NOS1
-
-
Manually annotated by BRENDA team
male and female C57BL/6J mice
-
-
Manually annotated by BRENDA team
strain C57BL/6
-
-
Manually annotated by BRENDA team
tight-skin 1 mouse strain
UniProt
Manually annotated by BRENDA team
Mus musculus C57BL/6
strain C57BL/6
-
-
Manually annotated by BRENDA team
hybrid tilapia, three isozymes eNOS, iNOS and nNOS
-
-
Manually annotated by BRENDA team
2 isoforms; Sprague-Dawley
-
-
Manually annotated by BRENDA team
2 isoforms; Wistar strain
-
-
Manually annotated by BRENDA team
brain isoform
UniProt
Manually annotated by BRENDA team
different splice isoforms of nNOS, e.g. splicing variant nNOSalpha
-
-
Manually annotated by BRENDA team
inducible enzyme
-
-
Manually annotated by BRENDA team
isozyme nNOS
UniProt
Manually annotated by BRENDA team
male Sprague-Dawley rats, isozyme iNOS
UniProt
Manually annotated by BRENDA team
male Sprague-Dawley rats, isozymes nNOS and iNOS
-
-
Manually annotated by BRENDA team
neuronal enzyme
UniProt
Manually annotated by BRENDA team
Wistar and Wistar-Kyoto rats, and 1 month-old, prehypertensive/spontaneously hypertensive rats
-
-
Manually annotated by BRENDA team
Wistar rats
-
-
Manually annotated by BRENDA team
Wistar strain
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
male
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
Wistar strain
-
-
Manually annotated by BRENDA team
induced by methanol
-
-
Manually annotated by BRENDA team
neuronal isoform
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
P70313
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
-
the brain neuronal NOS and inducible NOS are respectively involved in the bombesin-induced secretion of noradrenaline and adrenaline from the adrenal medulla
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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 + ?
show the reaction diagram
-
-
-
-
ir
1-butyl-2-hydroxyguanidine + NADPH + O2
? + NO + NADP+
show the reaction diagram
P29476
-
-
-
?
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 + ?
show the reaction diagram
-
-
-
-
ir
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
P29477
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
P29477
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
P29474
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
P29476
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
P29476
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
Q06518
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
probably via Nomega-hydroxy-L-arginine
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
P29477
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
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
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
Mus musculus C57BL/6
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
?
2,6-dichlorophenolindophenol + NADPH + O2
? + NO + NADP+
show the reaction diagram
-
-
-
-
-
2,6-dichlorophenolindophenol + NADPH + O2
? + NO + NADP+
show the reaction diagram
-
-
-
-
-
2,6-dichlorophenolindophenol + NADPH + O2
? + NO + NADP+
show the reaction diagram
-
best substrate, about 10-fold increase in activity in presence of calmodulin
-
-
?
2-hydroxy-1-(4-hydroxyphenyl)guanidine + NADPH + O2
? + NO + NADP+
show the reaction diagram
P29476
-
-
-
?
2-hydroxy-1-isopropylguanidine + NADPH + O2
? + NO + NADP+
show the reaction diagram
P29476
-
-
-
?
adriamycin + NADPH + O2
? + NO + NADP+
show the reaction diagram
-
-
-
-
?
ferricyanide + NADPH + O2
ferrocyanide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
ferricyanide + NADPH + O2
ferrocyanide + NO + NADP+
show the reaction diagram
-
-
-
-
?
ferricytochrome c + NADPH + O2
ferrocytochrome c + NO + NADP+
show the reaction diagram
-
-
-
-
?
L-Ala-L-Arg + NADPH + O2
?
show the reaction diagram
-
endothelial microsomes, macrophage
-
-
?
L-Arg-L-Arg + NADPH + O2
?
show the reaction diagram
-
endothelial, microsomes, macrophage
-
-
?
L-Arg-L-Arg-L-Arg + NADPH + O2
?
show the reaction diagram
-
endothelial microsomes
-
-
?
L-Arg-L-Phe + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
L-arginine + H2O2 + tetrahydrobiopterin
? + NO + NADP+
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
Q9BDQ7
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
P29475
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
P70313
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
overall reaction
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
NO from acetylsalicylic acid-activated enzyme is involved in thrombolysis, overview
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
Q9BDQ7
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
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
overall reaction, overview
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
regulatory mechanism, overview
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
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
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
complete reaction, oxygen stoichiometry, effects of substrate/cofactor binding on the endothelial NOS isoform, eNOS, overview
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
conserved residue Arg1329 of nNOS enables bound NADPH to stabilize the FMN-shielded conformation, overview
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
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
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
overall reaction, the interactions between heme-bound NO and the substrates are finely tuned by the geometry of the Fe-ligand structure, overview
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
overall reaction, two-step oxidation of L-arginine using an O2-dependent mechanism, detailed overview
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
substrate and product binding analysis
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
the electron transfer between cofactors FMN and FAD is reversible
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
conversion of L-arginine to citrulline and nitric oxide takes place in two steps with N(G)-hydroxy-L-arginine as an intermediate product
-
-
?
L-arginine + NADPH + H+ + O2
Nomega-hydroxy-L-arginine + NADP+ + H2O
show the reaction diagram
-
first half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
?
L-arginine + NADPH + H+ + O2
Nomega-hydroxy-L-arginine + NADP+ + H2O
show the reaction diagram
-
first half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
?
L-arginine + NADPH + H+ + O2
Nomega-hydroxy-L-arginine + NADP+ + H2O
show the reaction diagram
-
first half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
?
L-arginine + NADPH + H+ + O2
Nomega-hydroxy-L-arginine + NADP+ + H2O
show the reaction diagram
-
first half reaction via intermediate Nomega-hydroxy-L-arginine with consecutive appearance of heme-dioxy, ferric heme-NO, and ferric heme species, overview
-
-
?
L-arginine + NADPH + H+ + O2
Nomega-hydroxy-L-arginine + NADP+ + H2O
show the reaction diagram
-
first half reaction
-
-
ir
L-arginine + NADPH + O2 + tetrahydrobiopterin
citrulline + NO + NADP+ + ?
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + O2 + tetrahydrobiopterin
citrulline + NO + NADP+ + ?
show the reaction diagram
P29477
-
-
-
?
L-arginine + NADPH + O2 + tetrahydrobiopterin
citrulline + NO + NADP+ + ?
show the reaction diagram
-
-
-
-
-
L-arginine + NADPH + O2 + tetrahydrobiopterin
citrulline + NO + NADP+ + ?
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + O2 + tetrahydrobiopterin
citrulline + NO + NADP+ + ?
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
-
L-homoarginine + NADPH + O2
?
show the reaction diagram
-
poor substrate
-
-
?
L-homoarginine + NADPH + O2
?
show the reaction diagram
-
constitutive endothelial membrane-bound and inducible soluble macrophage enzyme
-
-
?
L-homoarginine + NADPH + O2
?
show the reaction diagram
Rattus norvegicus Wistar
-
poor substrate
-
-
?
menadione + NADPH + O2
? + NO + NADP+
show the reaction diagram
-
-
-
-
?
N-hydroxy-L-arginine + H2O2 + tetrahydrobiopterin
? + NADP+
show the reaction diagram
-
-
-
-
?
N-hydroxy-L-arginine + NADPH + O2
? + NO + NADP+
show the reaction diagram
-
-
-
-
?
N-hydroxy-L-arginine + NADPH + O2
? + NO + NADP+
show the reaction diagram
P29477
-
-
-
?
N-hydroxy-L-arginine + NADPH + O2
? + NO + NADP+
show the reaction diagram
-
-
-
-
?
N-hydroxy-L-arginine + NADPH + O2
? + NO + NADP+
show the reaction diagram
P29476
-
-
-
?
Ngamma-hydroxy-L-arginine + H2O2
citrulline + Ndelta-cyanoornithine + NO2- + NO3-
show the reaction diagram
-
tetrahydrobiopterin-free
NO2-/NO3- as aerobic decomposition products from NO-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
show the reaction diagram
-
-
-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
show the reaction diagram
-
-
-
-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
show the reaction diagram
-
-
-
-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
show the reaction diagram
-
best substrate
-
-
?
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
show the reaction diagram
-
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
show the reaction diagram
-
substrate is intermediate between reaction 1 and 2 to form citrulline and NO from L-arginine
-
-
ir
Ngamma-hydroxy-L-arginine + NADPH + O2
citrulline + NADP+ + NO
show the reaction diagram
-
reaction is possible without tetrahydrobiopterin, can also use H2O2 instead of NADPH and O2
-
?
nitroblue tetrazolium + NADPH
nitroblue tetrazolium-flavazone + NADP+
show the reaction diagram
-
-
-
-
-
nitroblue tetrazolium + NADPH
nitroblue tetrazolium-flavazone + NADP+
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
-
NADPH-diaphorase reaction
-
?
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
second half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
-
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
second half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
-
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
second half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
-
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
second half reaction via intermediate Nomega-hydroxy-L-arginine
-
-
-
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
second half reaction via intermediate Nomega-hydroxy-L-arginine, FeII and FeII-NO complexes bind Nomega-hydroxy-L-arginine, overview
-
-
-
Nomega-hydroxy-L-arginine + NADPH + H+ + O2
L-citrulline + NADP+ + NO + H2O
show the reaction diagram
-
second half reaction
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
show the reaction diagram
P29477
-
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
show the reaction diagram
-
wild-type and mutants
-
-
?
oxidized cytochrome c + NADPH + O2
reduced cytochrome c + NADP+ + H2O
show the reaction diagram
-
reaction is enhanced by addition of calmodulin at 0.0002 mM
-
-
?
peroxynitrite + 4-hydroxyphenylacetic acid + NADPH + H+
4-hydroxyl-3-nitro-phenylacetic acid + NADP+ + H2O
show the reaction diagram
-
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
-
-
mitomycin c + NADPH + O2
? + NO + NADP+
show the reaction diagram
-
-
-
-
?
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
?
-
-
enzyme shows also superoxide formation activity, uneffected by L-arginine, inhibited by tetrahydrobiopterin and diphenyleneiodonium
-
-
-
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
?
-
-
the enzyme exhibits NADPH-diaphorase activity, uncoupled from nitric oxide synthase activity
-
-
-
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
?
-
-
dimeric enzyme and subunits are equivalent in catalyzing electron transfer from NADPH to cytochrome c, dichlorophenolindiphenol, and ferricyanide, D-arginine is no substrate
-
-
-
additional information
?
-
-
D-arginine is no substrate
-
-
-
additional information
?
-
-
enzyme shows also superoxide formation activity
-
-
-
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
-
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
-
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
?
-
P29474
calmodulin-controlled isoforms are signal generators, overview
-
-
-
additional information
?
-
P29476
calmodulin-controlled isoforms are signal generators, overview
-
-
-
additional information
?
-
-
caveolin-1 is a prominent NOS-interacting protein in rat polymorphonuclear neutrophils
-
-
-
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
?
-
-
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
?
-
-
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
?
-
Q06518
NO is implicated in the pathogenesis of liver cirrhosis, overview
-
-
-
additional information
?
-
-
postsynaptic density 95 proteins mediate the complex formation of neuronal nitric oxide synthase and N-methyl-D-aspartate receptors
-
-
-
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 enzyme might be involved in the infectivity and/or escaping mechanism of the parasite
-
-
-
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
?
-
P29474
both oxyFMN and oxygenase domain activity are measured by following H2O2-supported oxidation of Nomega-hydroxy-L-Arg, L-NOHA, overview
-
-
-
additional information
?
-
P29476
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
?
-
-
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
?
-
-
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
?
-
-
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 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 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
?
-
-
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
?
-
-
a oxygenase domain of dNOS complex with ferrous heme-NO is relatively unreactive toward O2
-
-
-
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
?
-
-
interaction between peroxynitrite and the oxygenase domain of inducible NOS
-
-
-
additional information
?
-
-
mechanisms of oxygen activation by NOSs, 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 bacterial NOS enzymes have no attached flavoprotein domain to reduce their heme and so must rely on unknown bacterial proteins for electrons
-
-
-
additional information
?
-
-
the reduced recombinant trunaction mutant nNOSr performs autooxidation in presence of NADPH, interactions, overview
-
-
-
additional information
?
-
P70313
eNOS is an important negative regulator of AMP-activated protein kinase phosphorylation and intracellular H2O2 generation in endothelial cells
-
-
-
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
?
-
Rattus norvegicus Sprague-Dawley
-
the enzyme exhibits NADPH-diaphorase activity, uncoupled from nitric oxide synthase activity, NO represents the endogenous activator of soluble guanylyl cyclase
-
-
-
additional information
?
-
Rattus norvegicus Wistar
-
D-arginine is no substrate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
P29477
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
P29477
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
P29474
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
P29476
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
Q06518
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Mus musculus C57BL/6
-
-
-
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
NO from acetylsalicylic acid-activated enzyme is involved in thrombolysis, overview
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
Q9BDQ7
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
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
overall reaction, overview
-
-
?
L-arginine + NADPH + H+ + O2
citrulline + nitric oxide + NADP+ + H2O
show the reaction diagram
-
regulatory mechanism, overview
-
-
?
additional information
?
-
-
enzyme shows also superoxide formation activity
-
-
-
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
-
additional information
?
-
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
-
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
?
-
P29474
calmodulin-controlled isoforms are signal generators, overview
-
-
-
additional information
?
-
P29476
calmodulin-controlled isoforms are signal generators, overview
-
-
-
additional information
?
-
-
caveolin-1 is a prominent NOS-interacting protein in rat polymorphonuclear neutrophils
-
-
-
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
?
-
-
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
?
-
-
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
?
-
Q06518
NO is implicated in the pathogenesis of liver cirrhosis, overview
-
-
-
additional information
?
-
-
postsynaptic density 95 proteins mediate the complex formation of neuronal nitric oxide synthase and N-methyl-D-aspartate receptors
-
-
-
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 enzyme might be involved in the infectivity and/or escaping mechanism of the parasite
-
-
-
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
?
-
-
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
?
-
-
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 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 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
?
-
-
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
?
-
P70313
eNOS is an important negative regulator of AMP-activated protein kinase phosphorylation and intracellular H2O2 generation in endothelial cells
-
-
-
additional information
?
-
Rattus norvegicus Sprague-Dawley
-
NO represents the endogenous activator of soluble guanylyl cyclase
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(6R)-5,6,7,8-tetrahydro-L-biopterin
-
-
(6R)-tetrahydrobiopterin
-
-
(6R)-tetrahydrobiopterin
-
enzyme-bound
(6R)-tetrahydrobiopterin
-
required
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
-
enhances initial rate of NO-formation
5,6,7,8-tetrahydro-L-biopterin
-
stimulates 4fold at 0.001 mM
5,6,7,8-tetrahydro-L-biopterin
-
activity is correlated directly to bound biopterin concentration; 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
-
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
-
presumably tightly enzyme-bound
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
stimulates 9fold
5,6,7,8-tetrahydro-L-biopterin
-
required
5,6,7,8-tetrahydro-L-biopterin
-
absolute requirement, recombinant from Pichia pastoris
5,6,7,8-tetrahydro-L-biopterin
-
required
5,6,7,8-tetrahydro-L-biopterin
-
required
5,6,7,8-tetrahydro-L-biopterin
-
required; required for the first partial reaction, formation of NG-hydroxy-L-arginine
5,6,7,8-tetrahydro-L-biopterin
-
0.19 mol bound per mol of dimer; required
5,6,7,8-tetrahydro-L-biopterin
-
required
5,6,7,8-tetrahydro-L-biopterin
-
not required for activity
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
only wild-type
5,6,7,8-tetrahydro-L-biopterin
-
stimulates
5,6,7,8-tetrahydro-L-biopterin
-
0.04 mol per mol of subunit
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
-
0.003 mM; 0.003 mM
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
-
5,6,7,8-tetrahydro-L-biopterin
-
-
Calmodulin
-
activation, potent stimulator of purified, not crude, enzyme preparation
Calmodulin
-
NADPH-diaphorase activity of the 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
-
murine macrophage enzyme is Ca2+/calmodulin independent
Calmodulin
-
-
Calmodulin
-
rat neutrophil enzyme is calmodulin independent
Calmodulin
-
Ca2+/calmodulin stimulates cytochrome c reductase activity
Calmodulin
-
dependent on, endothelial enzyme
Calmodulin
-
Ca2+/calmodulin is required for superoxide formation in absence of tetrahydropterin
Calmodulin
-
required
Calmodulin
-
required
Calmodulin
-
required
Calmodulin
-
required
Calmodulin
-
required
Calmodulin
-
15fold stimulation of cytochrome c reduction of wild-type and mutants C415A and C415H; Ca2+/calmodulin stimulates cytochrome c reductase activity
Calmodulin
-
dependent on, endothelial enzyme
Calmodulin
-
no stimulation with exogenous calmodulin, inducible isoform from liver
Calmodulin
-
enzyme-bound is required, supplemented stimulates
Calmodulin
-
enzyme-bound, the binding sequence links the two enzyme domains
Calmodulin
-
dependent on
Calmodulin
-
dependent on
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
Calmodulin
-
30 nM; 30 nM
Calmodulin
-
in the absence of calmodulin, the wild type enzyme activity is less than 15% of the maximum calmodulin-dependent values
cytochrome c
-
activation
cytochrome c
-
-
cytochrome c
-
-
cytochrome c
-
-
FAD
-
FAD containing flavoprotein
FAD
-
no activation by the addition of exogenous FAD; tightly enzyme-bound
FAD
-
FAD containing flavoprotein; tightly enzyme-bound
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
-
2.2 mol FAD per mol of enzyme dimer; non-covalently bound FAD
FAD
-
absolute requirement for FAD
FAD
-
1 mol per mol of enzyme subunit; FAD containing flavoprotein; slight activation by exogeneous FAD
FAD
-
required
FAD
-
0.56 mol per mol of recombinant enzyme
FAD
-
required
FAD
-
0.49 mol per mol of dimer
FAD
-
required
FAD
-
major source of superoxide production in absence of tetrahydrobiopterin
FAD
-
wild-type and mutant C415H contain1 mol per mol of subunit
FAD
-
no flavin
FAD
-
enzyme-bound
FAD
-
required
FAD
P29474
-
FAD
-
required for catalysis
FAD
Q9BDQ7
binding site sequence, overview
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
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
Q9BDQ7
binding site sequence, overview
-
FMN
-
FMN containing flavoprotein
FMN
-
no activation by the addition of exogenous FMN; tightly enzyme-bound
FMN
-
FMN containing flavoprotein; tightly enzyme-bound
FMN
-
1 mol FMN per mol enzyme dimer
FMN
-
the enzyme bears Ca2+/calmodulin dependent FAD and FMN containing reductase domain which transfers electrons from NADPH to a variety of acceptors
FMN
-
1.1 mol FMN per mol enzyme dimer
FMN
-
1 mol per mol of enzyme subunit; FMN containing flavoprotein
FMN
-
0.79 mol per mol of recombinant enzyme
FMN
-
required
FMN
-
0.71 mol per mol of dimer; required
FMN
-
required
FMN
-
wild-type and mutant C415H contain 0.8 and 0.9 mol per mol of subunit, respectively
FMN
-
no flavin
FMN
-
enzyme-bound
FMN
-
required
FMN
P29474
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
P29476
FMN/heme electron transfer, FMN is capable of serving as a one electron heme reductant
FMN
-
regulation of the FMN module conformational equilibrium, overview
FMN
-
an inverse correlation exists between FMN shielding and the cytochrome c reductase activity
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
heme
-
-
heme
-
an inverse correlation exists between FMN shielding and the cytochrome c reductase activity
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
-
frequencies of electron transfer, overview
heme b
-
bound, quantitative determination
NADP+
-
binding mechanism
NADPH
-
requirement, specific for, NADPH-diaphorase activity requires higher NADPH concentrations than nitric oxide formation
NADPH
-
NADPH-dependent dioxygenase
NADPH
-
dependent on
NADPH
-
crude preparation requires only NADPH as cofactor; dependent on
NADPH
-
dependent on
NADPH
-
at high concentration inhibits dimer reconstitution from subunits; dependent on
NADPH
-
dependent on
NADPH
-
-
NADPH
-
-
NADPH
-
required
NADPH
-
dependent on
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
-
binding mechanism
NADPH
Q9BDQ7
binding site sequence, overview
NADPH
-
1 mM; 1 mM
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
nitroblue tetrazolium
-
activation
tetrahydrobiopterin
-
oxidation product of BH4 is a protonated BH3 radical, key role of BH4 in protonation of Fe(II)-O2-, overview
tetrahydrobiopterin
-
-
tetrahydrobiopterin
-
required
tetrahydrobiopterin
-
the cofactor tetrahydrobiopterin binds along the side of the heme
tetrahydrobiopterin
-
binding analysis
tetrahydrobiopterin
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
requirement, brain, not liver or lung
Ca2+
-
the enzyme bears Ca2+/calmodulin dependent cytochrome P-450 reductase activity which catalyzes cytochrome c reduction
Ca2+
-
slight activation
Ca2+
-
cerebellum enzyme is Ca2+-dependent
Ca2+
-
-
Ca2+
-
constitutive endothelial and inducible membrane bound macrophage enzyme are strictly Ca2+-dependent; insoluble enzyme; macrophage enzyme
Ca2+
-
required, calmodulin independent
Ca2+
-
activation only in the presence of calmodulin
Ca2+
-
activation only in the presence of calmodulin
Ca2+
-
absolutely dependent on
Ca2+
-
Ca2+/calmodulin is required for citrulline/NO formation and for superoxide formation in absence of tetrahydropterin
Ca2+
-
required, calmodulin independent
Ca2+
-
absolutely dependent on
Ca2+
-
required
Ca2+
-
required
Ca2+
-
cerebellum enzyme is Ca2+-dependent; retina enzyme is dependent on Ca2+
Ca2+
-
no stimulation with exogenous Ca2+, inducible isoform from liver
Ca2+
-
required
Ca2+
-
required
Ca2+
-
required
Ca2+
-
activates
Ca2+
-
dependent on
Ca2+
-
required for catalysis
Ca2+
-
required by eNOS, activates
Ca2+
-
dependent on
Ca2+
-
required for calmodulin to bind and activate the enzyme, maximum calmodulin-dependent activity is measured at 1.5 mM CaCl2
Ca2+
-
low levels of Ca2+ stimulate nNOS activity
Ca2+
-
stimulation of mtNOS can be achieved by elevating mitochondrial Ca2+ (0.01-0.1 mM)
Ca2+
-
the raise of intracellular calcium levels increases nNOS dephosphorylation and enzymatic activity
Ca2+
-
dependent, NOS1 and NOS3
Ca2+/calmodulin
-
activate the electron transfer
Ca2+/calmodulin
P29474
calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electrontransfer between NADPH and heme
Ca2+/calmodulin
-
calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electrontransfer between NADPH and heme
Ca2+/calmodulin
P29476
calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electron transfer between NADPH and heme
Fe2+
-
a heme enzyme, spectral comparison of the FeIII-NO and FeII-NO complexes of the bacterial NOSs, FeIII-NO complexes lack change in Fe-N-O frequencies upon (6R) 5,6,7,8-tetrahydro-L-biopterin binding to bacterial NOSs, overview. In the FeIII-NO complexes, both L-arginine and NOHA induced the Fe-N-O bending mode at nearly the same frequency as a result of a steric interaction between the substrates and the heme-bound NO, while in FeII-NO complexes the the Fe-N-O bending mode is no observed
Fe2+
-
a heme enzyme
Fe2+
-
in the heme cofactor
Fe2+
-
in the heme cofactor, substrate-ligand interaction in the Fe2+-O2 complex, overview
Fe2+
-
a heme enzyme, frequencies of electron transfer, overview
Fe2+
-
a heme enzyme
Fe2+
-
a cytochrome P450 enzyme
Fe2+
-
a heme enzyme
Iron
-
2 mol iron-protoporphyrin IX per mol enzyme dimer, the heme-iron is ferric, EPR-and light absorbance spectroscopy
Iron
-
mouse macrophage enzyme: cytochrome P-450 type hemoprotein; protoporphyrin IX heme
Iron
-
protoporphyrin IX heme
Iron
-
0.8 mol per mol of subunit; heme-iron
Iron
-
naturally occuring neuronal mutant with a 105-amino acid deletion in the heme-binding domain as a result of in-frame mutation by specific alternative splicing, contains heme, but shows no L-arginine and NADPH-dependent citrulline-forming activity in presence of Ca2+-promoted calmodulin, the heme coordination geometry is highly abnormal
Iron
-
-
Iron
-
heme-iron
Iron
-
0.9-1.2 mol heme per mol of dimer; heme-iron; protoporphyrin IX heme; required
Iron
-
protoporphyrin IX heme
Iron
-
0.88 mol per mol of recombinant enzyme monomer
Iron
-
heme ligand is bound via C415
Iron
-
0.83 mol per mol of subunit; protoporphyrin IX heme
Iron
-
heme-iron
Iron
-
low-spin heme iron, L-arginine aud tetrahydrobiopterin bind and stabilize heme iron in five-coordinate high-spin state
Iron
-
low-spin heme iron, L-arginine and tetrahydrobiopterin bind and stabilize heme iron in five-coordinate high-spin state
Iron
-
ferric heme
Iron
-
as heme iron in protoporphyrin IX /heme, hemesubstrate interactions and heme-transitions, overview
Iron
-
heme iron
Iron
P29474
heme iron, FMN/heme electron transfer
Iron
-
heme iron, FMN/heme electron transfer
Iron
P29476
heme iron, FMN/heme electron transfer
O2
-
oxygen tension influences the activity
Zinc
-
0.43 mol per mol of subunit
Zn2+
-
bound by Cys104, Cys109, and Cys194 of isozyme iNOS oxygenase domain
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
P29477
highly selective inhibitors
-
3,4-dihydro-1-isoquinolinamines
P29477
-
-
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
-
IC50: 0.0076 mM
4-(3-amino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
P29477
IC50: 0.0119 mM
4-(3-amino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.0091 mM
4-(3-amino-propoxy)-6-chloro-1H-quinolin-2-one trifluoroacetic acid salt
P29477
IC50: 410 nM, pharmacokinetic profile
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
P29477
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
P29477
IC50: 0.0104 mM
4-(3-dimethylamino-propoxy)-1H-quinolin-2-one
-
IC50: 0.010 mM
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-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
P29477
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
P29477
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
P29477
IC50: 0.00025mM
6-chloro-4-(3-methylamino-propoxy)-1-benzopyran-2-one trifluoroacetic acid salt
-
IC50: 0.00053mM
6-n-propyl-2-thyouracil
P29475
0.1 mg 6-n-propyl-2-thyouracil decreases nNOS activity to 45% compared to control
7-nitroindazole
-
weak inhibition
7-nitroindazole
-
reversible inhibition of endothelial enzyme, competitive versus tetrahydrobiopterin, no inhibition of cytochrome c reduction
7-nitroindazole
-
-
7-nitroindazole
-
-
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
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
Aminoguanidine
-
-
Aminoguanidine
-
0.01 mM, about 40% residual activity
AR-C102222
P29477
1,2-dihydro-4-quinazolinamine derivative
AR-C102222
-
1,2-dihydro-4-quinazolinamine derivative
AR-C85016
P29477
1,2-dihydro-4-quinazolinamine derivative
AR-C85016
-
1,2-dihydro-4-quinazolinamine derivative
Ca2+
-
preincubation at 37C leads to time-dependent inhibition of the enzyme
Ca2+
-
high levels of Ca2+ inhibit nNOS activity
Calcineurin
-
-
-
Calmidazolium
-
calmodulin antagonist
Calmidazolium
-
-
Calmidazolium
-
in absence of calmodulin
Calmidazolium
-
calmodulin antagonist; complete inhibition
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
-
partially purified rat cerebellum enzyme
CO/O2
-
80%:20%, mixture
-
cyanide
-
heme-blocker inhibits superoxide formation after pretreatment of the enzyme
cyanide
-
pretreatment
Di-2-thienyliodonium
-
competitive, irreversible, complete, time and temperature dependent inhibition
dimethylarginine
-
-
diphenylene iodonium
-
competitive, irreversible, complete, time and temperature dependent inhibition
diphenylene iodonium
-
inhibition of superoxide production of recombinant isoform III
EDTA
-
brain enzyme
EDTA
-
no inhibition
EDTA
-
brain enzyme
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
-
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
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
imidazole
-
heme-blocker inhibits superoxide formation after pretreatment of the enzyme
imidazole
-
inhibition of the endothelial enzyme, competitive versus L-arginine, no inhibition of cytochrome c reduction
imidazole
-
the enzyme forms a sixcoordinate low-spin complex with inhibitor imidazole, interaction analysis
Iodoniumdiphenyl
-
competitive, irreversible, complete, time and temperature dependent inhibition
L-arginine
-
inhibits peroxynitrite activation
L-arginine
-
L-arginine strongly stimulates oxygen consumption of eNOS and inhibits that of nNOS
L-arginine methyl ester
P70313
-
L-Asn-methyl-L-arginine
-
inhibition of the isozymes in absence or presence of L-arginine
L-canavanine
-
liver enzyme, slight inhibition of brain enzyme
L-canavanine
-
not inhibitory
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-nitro-arginine-methylester
-
-
-
L-Nomega-nitroarginine-(4R)-amino-L-proline amide
-
;
L-Nomega-nitroarginine-2,4-L-diaminobutyramide
-
;
L-omega-monomethyl L-arginine
Q62600
potent competitive eNOS inhibitor, complete inhibition at 10 mM
L-thiocitrulline
-
5 mM, above 95% inhibition
L-thiocitrulline
P29477
no isozyme specificity
N(G),N(G)-dimethyl-L-arginine
-
asymmetric dimethyl arginine
N(G)-nitroarginine methyl ester
P70313
-
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
P29477
no isozyme specificity
N-iminoethyl-L-ornithine
P29477
no isozyme specificity
N-monomethyl-L-arginine
-
0.01 mM, about 55% residual activity
N-nitro-L-arginine methyl ester
-
1 mM, about 50% residual activity
N-nitro-L-arginine methyl ester
-
0.01 mM, about 40% residual activity
N-nitro-L-arginine methyl ester
-
0.5 mM, 65% inhibition
N-nitro-L-arginine methyl ester
-
competitive NOS inhibitor
N-[(1,3-benzodioxol-5-yl)methyl]-1-[2-(1H-imidazol-1-yl)pyrimidin-4-yl]-4-(methoxycarbonyl)-piperazine-2-acetamide
P29477
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
-
;
NG-methyl arginine
-
specific inhibition
NG-methyl-L-arginine
P29477
no isozyme specificity
Ng-monomethy-L-arginine
-
-
NG-Nitro-L-arginine
P29477
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-amino-L-arginine
-
-
Ngamma-hydroxy-Ngamma-methyl-L-arginine
-
preincubation at 37C leads to irreversible inactivation, substrates protect
Ngamma-iminoethyl-L-ornithine
-
competitive inhibitor
Ngamma-monomethyl-L-arginine
-
-
Ngamma-monomethyl-L-arginine
-
-
Ngamma-monomethyl-L-arginine
-
not D-isomer, strong, competitive
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
-
slightly
Ngamma-monomethyl-L-arginine
-
slightly
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
-
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
-
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
-
-
Ngamma-nitro-L-arginine
-
-
Ngamma-nitro-L-arginine
-
competitive inhibitor
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
-
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
-
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
-
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
-
very slightly, only L-isomer and in presence of tetrahydrobiopterin and NADPH
Ngamma-nitro-L-arginine methyl ester
-
-
Ngamma-nitro-L-arginine methyl ester
-
complete inhibition
Ngamma-nitro-L-arginine methyl ester
-
-
Ngamma-nitro-L-arginine methyl ester
-
nearly complete inhibition at 0.5 mM
nitroblue tetrazolium
-
potent non-competitive inhibitor, partially reversible by tetrahydrobiopterin
nitroblue tetrazolium
-
-
nitroblue tetrazolium
-
-
NO
-
feedback inhibition
Nomega-nitro-L-arginine methyl ester
-
nonselective NOS inhibitor
Nomega-nitro-L-arginine methyl ester
-
-
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
-
S-ethylisothiourea
-
5 mM, 85% inhibition
S-ethylisothiourea
-
inducible NOS inhibitor
tetrahydrobiopterin
-
inhibits peroxynitrite activation
thiocoumarin
-
IC50: 0.018 mM
thiocoumarin
P29477
weak inhibitor
Trifluoperazine
-
no inhibitor of macrophage enzyme
Trifluoperazine
-
inhibition in the presence of Ca2+, reversible by calmodulin
Trifluoperazine
-
no inhibitor of macrophage enzyme
Trifluoperazine
-
inhibits cytochrome c reductase activity
Trifluoperazine
-
-
Trifluoperazine
-
in absence of calmodulin
W7 hydrochloride
-
5 mM, 50% inhibition
methylisothiourea
-
0.01 mM, about 80% residual activity
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
-
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
-
Ngamma,Ngamma'-dimethyl-L-arginine has no inhibitory effect
-
additional information
-
not inhibitory: N-nitro-L-arginine methyl ester, or specific inhibitor of inducible NOS, 1400W
-
additional information
-
not inhibitory: N-nitro-D-arginine methyl ester at 0.5 mM
-
additional information
-
no inhibition by 4-(3-amino-propoxy)-6-chloro-1H-quinolin-2-one trifluoroacetic acid salt
-
additional information
P29477
inhibitory activity for coumarin derivatives, inhibitor screening, overview
-
additional information
-
no inhibition by 4-(3-amino-propoxy)-6-chloro-1H-quinolin-2-one trifluoroacetic acid salt and thiocoumarin
-
additional information
-
fibroblast growth factor-2 treatment up-regulates the enzyme in tectume, but down-regulates it in the optic nerve, overview
-
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
-
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
-
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
-
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
P70313
there is decreased eNOS activity in tight-skin 1-mouse skin tissue
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(6R,S)-Methyl-tetrahydropterin
-
activation in the absence of biopterin, not as effective as tetrahydrobiopterin
A-23187
-
low levels of A-23187 stimulate nNOS activity
Acetylsalicylic acid
-
maximal activation at 0.004 mM
Ca2+/calmodulin
-
activate the electron transfer
-
Ca2+/calmodulin
P29474
calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electrontransfer between NADPH and heme
-
Ca2+/calmodulin
-
calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electrontransfer between NADPH and heme
-
Ca2+/calmodulin
P29476
calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electron transfer between NADPH and heme
-
Calmodulin
-
substrate 2,6-dichlorophenolindophenol, about 10fold increase in activity in presence of calmodulin
Calmodulin
-
required
Calmodulin
-
required
Calmodulin
-
-
Calmodulin
-
-
Calmodulin
-
activates the neuronal NOS by binding and inhibiting the suppression through the C-terminal tail of the enzyme, overview
Calmodulin
-
required for catalysis
Calmodulin
-
activates O2 consumption of eNOS
dithiothreitol
-
requirement
dithiothreitol
-
-
dithiothreitol
-
-
interferon gamma
-
activates
-
L-arginine
-
L-arginine strongly stimulates oxygen consumption of eNOS and inhibits that of nNOS, nonhydrolyzable L-arginine analogues are not stimulatory
tetrahydrobiopterin
-
-
thyroxin
P29475
0.001 mg thyroxin significantly increases nNOS activity and nNOS protein level to 153% compared to control
-
lipopolysaccharide
-
from Escherichia coli, activates
additional information
-
neopterin derivatives are completely inactive and do not bind to the enzyme
-
additional information
-
fibroblast growth factor-2 teratment up-regulates the enzyme in tectume, but down-regultes it in the optic nerve, overview
-
additional information
Q06518
hepatic isozyme iNOS expression is induced in chronic liver cirrhosis early stages
-
additional information
Q9BDQ7
iNOS is induced by pathogens and their components, e.g. induction in alveolar macropages by infection with the intracellular pathogen Mycobacterium bovis
-
additional information
-
short-term (20-30 min) treatment of endothelial cells with the synthetic NO donor (Z)-1-[2-(2-aminoethyl)-N-(2-aminoethyl)amino](diazen-1-ium-1,2-diolate) increases the Ser1177 phosphorylation of the constitutively expressed endothelial NOS and the production of endogenous NO generated by eNOS from L-arginine, the phosphorylation of eNOS is Akt-dependent and completely reverted by the phosphatidylinositol-3 kinase inhibitor LY-294002
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0008
2',3'-dialdehyde NADPH
-
-
0.012
adriamycin
-
FAD-FMN domain, absence of calmodulin
0.021
adriamycin
-
full-length enzyme, absence of calmodulin
0.043
adriamycin
-
full-length enzyme, presence of calmodulin
0.05
adriamycin
-
FAD-NADPH domain
0.078
adriamycin
-
FAD-FMN domain, presence of calmodulin
0.000004
Calmodulin
-
-
0.008 - 0.0084
dichlorophenolindophenol
-
-
0.008 - 0.0084
dichlorophenolindophenol
-
with L-arginine
0.0019
L-arginine
-
mutant nNOS D597N/M336V
0.002 - 0.0028
L-arginine
-
NADPH
0.002 - 0.0028
L-arginine
-
-
0.002 - 0.0028
L-arginine
-
-
0.002 - 0.0028
L-arginine
-
-
0.0021
L-arginine
-
-
0.0022
L-arginine
-
22C, wild type
0.0023
L-arginine
-
-
0.0023
L-arginine
-
22C, wild type
0.0024
L-arginine
-
22C, mutant W678F
0.0025
L-arginine
-
22C, mutant W678A
0.0028
L-arginine
-
-
0.0029
L-arginine
-
isoform III
0.0033 - 0.0043
L-arginine
-
NADPH, bovine
0.0033 - 0.0043
L-arginine
-
-
0.0039
L-arginine
-
recombinant from Pichia pastoris
0.0044
L-arginine
-
wild-type
0.0052
L-arginine
-
mutant E298D
0.00746
L-arginine
-
pH 7.0, 37C
0.0084
L-arginine
-
-
0.0091
L-arginine
-
detrusor
0.0099
L-arginine
-
urethra
0.011
L-arginine
-
with FAD and tetrahydropterin
0.0134
L-arginine
-
pH 6.5, 47.5C
0.014 - 0.018
L-arginine
-
-
0.014 - 0.018
L-arginine
-
-
0.014 - 0.018
L-arginine
-
-
0.022
L-arginine
-
-
0.022
L-arginine
-
in presence of tetrahydrobiopterin and L-arginine
0.0275
L-arginine
-
22C, mutant W457A
0.0323 - 0.035
L-arginine
-
NADPH, diaphorase activity
0.0323 - 0.035
L-arginine
-
cytochrome c reduction
0.0323 - 0.035
L-arginine
-
-
0.041
L-arginine
-
without tetrahydropterin and FAD
0.097
L-arginine
-
with Ca2+, 0.01 mM
0.11
L-arginine
-
without Ca2+
4.8
L-arginine
-
pH 7.6, 10C, wild type
5.32
L-arginine
-
pH 7.4, 30C
5.4
L-arginine
-
pH 7.6, 10C, mutant DELTA296nNOS
68.5
L-arginine
-
pH 7.6, 10C, mutant DELTA349nNOS
0.01
menadione
-
FAD-FMN domain, absence of calmodulin; FAD-FMN domain, presence of calmodulin
0.011
menadione
-
full-length enzyme, presence of calmodulin
0.014
menadione
-
full-length enzyme, absence of calmodulin
0.041
menadione
-
FAD-NADPH domain
0.0073
mitomycin C
-
full-length enzyme, absence of calmodulin
0.013
mitomycin C
-
full-length enzyme, presence of calmodulin
0.015
mitomycin C
-
FAD-FMN domain, absence of calmodulin
0.028
mitomycin C
-
FAD-NADPH domain
0.0003
NADPH
-
-
0.000383
NADPH
-
pH 7.0, 37C
0.0004
NADPH
-
-
0.001
NADPH
-
mutant D1393E
0.0013
NADPH
-
mutant D1393N
0.0025
NADPH
-
wild-type
0.0029
NADPH
-
mutant D1393V
0.0032
NADPH
-
CaM-bound recombinant eNOS
0.0041
NADPH
-
CaM-free recombinant eNOS
0.019
Ngamma-hydroxy-L-arginine
-
-
0.028
Ngamma-hydroxy-L-arginine
-
nonlinear regression analysis
0.0314
Ngamma-hydroxy-L-arginine
-
Eadie-Hofstee graph
0.036
Ngamma-hydroxy-L-arginine
-
25C, with tetrahydrobiopterin
0.129
Ngamma-hydroxy-L-arginine
-
25C, tetrahydrobiopterin-free
0.016
nitroblue tetrazolium
-
-
0.00002
tetrahydrobiopterin
-
-
0.0002
tetrahydrobiopterin
-
22C, wild type
0.0016
tetrahydrobiopterin
-
22C, wild type
0.025
tetrahydrobiopterin
-
22C, mutant W678A
0.1
tetrahydrobiopterin
-
22C, mutant W457A
0.114
tetrahydrobiopterin
-
22C, mutant W678A
0.055
mitomycin C
-
FAD-FMN domain, presence of calmodulin
additional information
additional information
-
rapid kinetic analysis, stopped-flow measurements under high pressure
-
additional information
additional information
-
biochemical pathway model, kinetic modeling, isozymes NOS1 and NOS3
-
additional information
additional information
-
kinetics of NO and substrate binding, recombinant enzyme
-
additional information
additional information
-
kinetics modeling and single-turnover reactions, kinetics of heme transitions during Arg oxidation, product stoichiometry analysis, detailed overview
-
additional information
additional information
-
kinetics of flavin reduction of the recombinant enzyme, overview
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetic analysis of the interaction between peroxynitrite and the oxygenase domain of inducible NOS at three different pH values, overview
-
additional information
additional information
-
kinetics and kinetic modelling, stopped-flow measurements
-
additional information
additional information
-
kinetics of heme-NO complex formation in the stopped-flow reaction
-
additional information
additional information
-
kinetics, rapid-freeze method, overview
-
additional information
additional information
-
kinetics of cytcochrome c reduction and of reaction with FMN and cytochrome c, overview, eNOS and nNOS differ slightly in their NADP(H) interaction and flavin thermodynamics, and show distinct electron transfer activities, two-state conformational equilibrium of the FMN subdomain, overview
-
additional information
additional information
-
Km-value for arginine about 0.003-0.02 mM
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.8
adriamycin
-
FAD-FMN domain, absence of calmodulin
4.9
adriamycin
-
FAD-NADPH domain
5.3
adriamycin
-
full-length enzyme, absence of calmodulin
94
adriamycin
-
FAD-FMN domain, presence of calmodulin
95
adriamycin
-
full-length enzyme, presence of calmodulin
1.08
L-arginine
-
-
6.6
menadione
-
full-length enzyme, absence of calmodulin
8
menadione
-
FAD-NADPH domain
9.5
menadione
-
FAD-FMN domain, absence of calmodulin
88
menadione
-
FAD-FMN domain, presence of calmodulin
96
menadione
-
full-length enzyme, presence of calmodulin
0.62
mitomycin C
-
full-length enzyme, absence of calmodulin
0.8
mitomycin C
-
FAD-NADPH domain
2.2
mitomycin C
-
FAD-FMN domain, absence of calmodulin
15.8
mitomycin C
-
full-length enzyme, presence of calmodulin
26
mitomycin C
-
FAD-FMN domain, presence of calmodulin
0.28
NADPH
-
DELTAG810 mutant enzyme, in the presence of 10 units/ml catalase and superoxide dismutase, in 25 mM potassium phosphate, pH 7.5, with 100 mM KCl, at 25C
0.32
NADPH
-
DELTAG810 mutant enzyme, in 25 mM potassium phosphate, pH 7.5, with 100 mM KCl, at 25C
2.33
NADPH
-
wild type enzyme, in the presence of 10 units/ml catalase and superoxide dismutase, in 25 mM potassium phosphate, pH 7.5, with 100 mM KCl, at 25C
2.57
NADPH
-
wild type enzyme, in 25 mM potassium phosphate, pH 7.5, with 100 mM KCl, at 25C
0.033
nitric oxide
-
DELTAG810 mutant enzyme, in 25 mM potassium phosphate, pH 7.5, with 100 mM KCl, at 25C
0.055
nitric oxide
-
DELTAG810 mutant enzyme, in the presence of 10 units/ml catalase and superoxide dismutase, in 25 mM potassium phosphate, pH 7.5, with 100 mM KCl, at 25C
0.92
nitric oxide
-
wild type enzyme, in 25 mM potassium phosphate, pH 7.5, with 100 mM KCl, at 25C
1.23
nitric oxide
-
wild type enzyme, in the presence of 10 units/ml catalase and superoxide dismutase, in 25 mM potassium phosphate, pH 7.5, with 100 mM KCl, at 25C
0.65
nitroblue tetrazolium
-
NADPH-diaphorase activity
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00015
(4S)-N-(4-amino-5-[aminoethyl]aminopentyl)-N''-nitroguanidine
-
wild type nNOS
0.08
(4S)-N-(4-amino-5-[aminoethyl]aminopentyl)-N''-nitroguanidine
-
wild type eNOS
0.05
1-phenylimidazole
-
-
0.0094
3-[cis-4'-[(6''-aminopyridin-2''-yl)methyl]pyrrolidin-3'-ylamino]propan-1-ol
-
wild type nNOS
0.0492
3-[cis-4'-[(6''-aminopyridin-2''-yl)methyl]pyrrolidin-3'-ylamino]propan-1-ol
-
mutant nNOS D597N/M336V
0.3666
3-[cis-4'-[(6''-aminopyridin-2''-yl)methyl]pyrrolidin-3'-ylamino]propan-1-ol
-
wild type eNOS
0.0008
7-nitroindazole
-
-
0.66
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
0.05
imidazole
-
-
0.0001
L-Nomega-nitroarginine-(4R)-amino-L-proline amide
-
wild type nNOS
0.11
L-Nomega-nitroarginine-(4R)-amino-L-proline amide
-
wild type eNOS
0.0003
L-Nomega-nitroarginine-2,4-L-diaminobutyramide
-
wild type nNOS
0.107
L-Nomega-nitroarginine-2,4-L-diaminobutyramide
-
wild type eNOS
0.0000022
N-[(1,3-benzodioxol-5-yl)methyl]-1-[2-(1H-imidazol-1-yl)pyrimidin-4-yl]-4-(methoxycarbonyl)-piperazine-2-acetamide
P29477
-
-
0.000085
N1-[cis-4'-[(6''-amino-4''-methylpyridin-2''-yl)methyl]pyrrolidin-3'-yl]-N2-(4'-chlorobenzyl)ethane-1,2-diamine
-
wild type nNOS
0.0012
N1-[cis-4'-[(6''-amino-4''-methylpyridin-2''-yl)methyl]pyrrolidin-3'-yl]-N2-(4'-chlorobenzyl)ethane-1,2-diamine
-
mutant nNOS D597N/M336V
0.0852
N1-[cis-4'-[(6''-amino-4''-methylpyridin-2''-yl)methyl]pyrrolidin-3'-yl]-N2-(4'-chlorobenzyl)ethane-1,2-diamine
-
wild type eNOS
0.000388
N1-[cis-4'-[(6''-aminopyridin-2''-yl)methyl]pyrrolidin-3'-yl]ethane-1,2-diamine
-
wild type nNOS
0.0367
N1-[cis-4'-[(6''-aminopyridin-2''-yl)methyl]pyrrolidin-3'-yl]ethane-1,2-diamine
-
mutant nNOS D597N/M336V
0.4167
N1-[cis-4'-[(6''-aminopyridin-2''-yl)methyl]pyrrolidin-3'-yl]ethane-1,2-diamine
-
wild type eNOS
0.00025
N1-[trans-4'-[(6''-amino-4''-methylpyridin-2''-yl)methyl]pyrrolidin-3'-yl]-N2-(3'-chlorobenzyl)ethane-1,2-diamine
-
wild type nNOS
0.0061
N1-[trans-4'-[(6''-amino-4''-methylpyridin-2''-yl)methyl]pyrrolidin-3'-yl]-N2-(3'-chlorobenzyl)ethane-1,2-diamine
-
mutant nNOS D597N/M336V
0.0034
Ngamma,Ngamma-dimethyl-L-arginine
-
-
0.00667
Ngamma,Ngamma-dimethyl-L-arginine
-
pH 7.0, 37C
0.0265
Ngamma-hydroxy-Ngamma-methyl-L-arginine
-
-
0.0012
Ngamma-iminoethyl-L-ornithine
-
-
0.00031
Ngamma-monomethyl-L-arginine
-
-
0.0007
Ngamma-monomethyl-L-arginine
-
endothelial isoform
0.0007
Ngamma-monomethyl-L-arginine
-
-
0.0018
Ngamma-monomethyl-L-arginine
-
-
0.002
Ngamma-monomethyl-L-arginine
-
neuronal isoform in presence of 0.004 mM tetrahydrobiopterin
0.0025
Ngamma-monomethyl-L-arginine
-
-
0.0026
Ngamma-monomethyl-L-arginine
-
inducible isoform from macrophage after preincubation
0.0039
Ngamma-monomethyl-L-arginine
-
inducible isoform from macrophage without preincubation
0.0054
Ngamma-monomethyl-L-arginine
-
-
0.0065
Ngamma-monomethyl-L-arginine
-
neuronal isoform
0.00002
Ngamma-nitro-L-arginine
-
irreversible inactivation of endothelial isoform after preincubation
0.000041
Ngamma-nitro-L-arginine
-
-
0.00009
Ngamma-nitro-L-arginine
-
irreversible inactivation of neuronal isoform after preincubation
0.0002
Ngamma-nitro-L-arginine
-
-
0.0004
Ngamma-nitro-L-arginine
-
-
0.0015
Ngamma-nitro-L-arginine
-
-
0.0081
Ngamma-nitro-L-arginine
-
reversible inhibition of inducible macrophage isoform
0.0155
Ngamma-nitro-L-arginine methyl ester
-
-
0.007
nitroblue tetrazolium
-
-
0.0952
N1-[trans-4'-[(6''-amino-4''-methylpyridin-2''-yl)methyl]pyrrolidin-3'-yl]-N2-(3'-chlorobenzyl)ethane-1,2-diamine
-
wild type eNOS
additional information
Ng,Ng-dimethylarginine
-
value about 0.001-0.0016
additional information
Ng-monomethy-L-arginine
-
value about 0.001-0.0016
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0076
4-(3-amino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.0076 mM
0.0091
4-(3-amino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.0091 mM
0.0119
4-(3-amino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
P29477
IC50: 0.0119 mM
0.00041
4-(3-amino-propoxy)-6-chloro-1H-quinolin-2-one trifluoroacetic acid salt
P29477
IC50: 410 nM, pharmacokinetic profile
0.004
4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.004 mM
0.01
4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
P29477
IC50: 0.01 mM
0.01
4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.01 mM
0.0026
4-(3-dimethylamino-propoxy)-1H-quinolin-2-one
-
IC50: 0.0026 mM
0.01
4-(3-dimethylamino-propoxy)-1H-quinolin-2-one
-
IC50: 0.010 mM
0.0104
4-(3-dimethylamino-propoxy)-1H-quinolin-2-one
P29477
IC50: 0.0104 mM
0.00006
6-chloro-4-(3-aminopropoxy)-1-benzopyran-2-one trifluoroacetic acid salt
P29477
IC50: 60 nM, pharmacokinetic profile
0.00009
6-chloro-4-(3-aminopropoxy)-1-benzopyran-2-one trifluoroacetic acid salt
-
IC50: 90 nM, pharmacokinetic profile
0.00056
6-chloro-4-(3-aminopropoxy)-1-benzopyran-2-one trifluoroacetic acid salt
-
IC50: 0.00056 mM, pharmacokinetic profile
0.0012
6-chloro-4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
P29477
IC50: 0.0012 mM
0.0041
6-chloro-4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.0041 mM
0.008
6-chloro-4-(3-dimethylamino-propoxy)-1-benzopyran-2-one hydrochloric acid salt
-
IC50: 0.008 mM
0.00011
6-chloro-4-(3-methylamino-propoxy)-1-benzopyran-2-one trifluoroacetic acid salt
-
IC50: 0.00011mM
0.00025
6-chloro-4-(3-methylamino-propoxy)-1-benzopyran-2-one trifluoroacetic acid salt
P29477
IC50: 0.00025mM
0.00053
6-chloro-4-(3-methylamino-propoxy)-1-benzopyran-2-one trifluoroacetic acid salt
-
IC50: 0.00053mM
0.018
thiocoumarin
-
IC50: 0.018 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000000335
-
crude extract
0.000000305
-
crude extract
0.000009
-
liver mitochondria
0.000017
-
liver
0.000033
-
brain mitochondria
0.000043
-
crude extract
0.000073
-
purified enzyme, without tetrahydropterin
0.00035
-
purified enzyme, with tetrahydropterin
0.00054
-
brain
0.00074
-
crude extract
0.0075
-
brain homogenates
0.0098
-
purified enzyme
0.01
-
reductase activity
0.031
-
purified recombinant enzyme, NADPH/O2-supported reduction of Ngamma-hydroxy-L-arginine, tetrahydrobiopterin-free, 25C
0.031
-
purified pancreatic enzyme
0.0353
-
pH 6.5, 47.5C
0.074
-
purified enzyme
0.12
-
NADPH-diaphorase activity
0.12
-
purified enzyme
0.12
-
purified recombinant enzyme, H2O2-supported reduction of Ngamma-hydroxy-L-arginine, tetrahydrobiopterin-free, 25C
0.142
-
wild-type
0.143
-
purified recombinant enzyme
0.159
-
mutant E298D
0.17
-
purified recombinant enzyme, NADPH/O2-supported reduction of Ngamma-hydroxy-L-arginine, with tetrahydrobiopterin, 25C
0.181
-
partially purified enzyme
0.19
-
purified recombinant enzyme
0.34 - 0.35
-
-
0.34 - 0.35
-
purified enzyme, recombinant, determined as NADPH-oxidase activity
0.41
-
substrate Ngamma-hydroxy-L-arginine, purified enzyme
0.6
-
pH 7.4, 30C
0.73
-
purified enzyme
0.815
-
purified recombinant enzyme, H2O2-supported reduction of Ngamma-hydroxy-L-arginine, with tetrahydrobiopterin, 25C
0.94 - 0.96
-
-
0.94 - 0.96
-
purified enzyme
1
-
purified enzyme
1.06
-
purified enzyme
1.1
-
purified enzyme
1.62
-
purified enzyme
1.9
-
purified enzyme
38
-
purified enzyme, inducible isoform, cytochrome c reductase activity
983.7
-
pH 7.0, 37C
additional information
-
activity in lung and liver only after induction by endotoxin
additional information
-
-
additional information
-
-
additional information
-
activity in urinary tract tissues
additional information
-
assay method
additional information
-
wild-type and mutants
additional information
-
activity in hypertensive and healthy rats, overview
additional information
-
iNOS activities in wild-type and chimeric mice, both with induced colitis, overview
additional information
-
steady-state catalytic activities of dNOSr
additional information
-
enzyme activities with different flavodoxins, overview
additional information
-
-
additional information
-
low eNOS activity might involve an altered interaction with NADP(H)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
assay at
7
-
assay at
7.4
-
-
7.4
-
assay at
7.4
-
assay at
7.4
-
assay at
7.4
-
assay at
7.4
-
ligand interaction assay at
7.4
-
-
7.5 - 7.6
-
assay at
7.5
-
assay at
7.5
-
assay at
7.6
P29474
assay at
7.6
-
assay at
7.6
-
assay at
7.6
-
assay at
7.8
-
assay at
8
-
assay at
additional information
-
pI: 5.6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6 - 8
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 25
-
assay at
10
-
anaerobic pre-steady-state cytochrome c reduction assay at
22
-
assay at room temperature
22
-
assay at room temperature
23
-
about, assay at
24
-
assay at
25
-
assay at
25
-
assay at
30
-
assay at
32
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
P29474
assay at
37
-
assay at
37
P29476
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Pseudomonas aeruginosa stimulates expression of inducible nitric oxide synthase by A-549 cells
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
axenic, high enzyme expression level
Manually annotated by BRENDA team
-
thoracic, muscle
Manually annotated by BRENDA team
-
isozyme NOS3
Manually annotated by BRENDA team
-
Ca2+-dependent isoform
Manually annotated by BRENDA team
-
Ca2+-dependent isoform
Manually annotated by BRENDA team
-
nNOS is the predominant isozyme in brain
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley, Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
Ca2+-dependent isoform, 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
-
Manually annotated by BRENDA team
-
cerebrum shows higher activity than cerebellum
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
cerebrum shows higher activity than cerebellum
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
cell line ME-180, constitutive expression
Manually annotated by BRENDA team
-
iNOS is more frequently expressed in osteoarthritic than in normal chondrocytes, iNOS expression and activity in osteoarthritic chondrocytes is sub-maximal, nNOS is more frequently expressed in normal than in osteoarthritic chondrocytes
Manually annotated by BRENDA team
-
bone marrow-derived
Manually annotated by BRENDA team
-
mainly in the lateral soma rind, surrounding the sensory glomeruli, partially in association with the antennal mechanosensory and motor neuropil
Manually annotated by BRENDA team
-
umbilical vein cells
Manually annotated by BRENDA team
-
constitutive, from pulmonary artery
Manually annotated by BRENDA team
-
aorta, cell culture
Manually annotated by BRENDA team
-
liver, lung, adrenal glandcolon, isoform II
Manually annotated by BRENDA team
-
comparison of endothelial and neuronal isoform
Manually annotated by BRENDA team
-
specific isozyme eNOS
Manually annotated by BRENDA team
-
vascular, constitutive expression of the endothelial isozyme in endothelial cells
Manually annotated by BRENDA team
-
eNOS, endothelial cells of blood vessels
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
synaptosomal fraction
Manually annotated by BRENDA team
-
subesophageal and prothoracic
Manually annotated by BRENDA team
-
cell line A-172, american type
Manually annotated by BRENDA team
-
macula densa cells, isoform I
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
renal cortex
-
Manually annotated by BRENDA team
-
leaf extract
Manually annotated by BRENDA team
-
inducible isoform
Manually annotated by BRENDA team
Q06518
temporal expression of hepatic iNOS in liver cirrhosis, induced in rats by chronic bile duct ligation, overview
Manually annotated by BRENDA team
Mus musculus C57BL/6, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Q9BDQ7
alveolar
Manually annotated by BRENDA team
-
in liver, lung, kidney, isoform II
Manually annotated by BRENDA team
-
Ca2+-independent form
Manually annotated by BRENDA team
-
cytokine-activated
Manually annotated by BRENDA team
-
bone marrow-derived
Manually annotated by BRENDA team
-
iNOS is the predominant isozyme in macrophages
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
isozyme NOS1
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
isozyme NOS1
Manually annotated by BRENDA team
E1XU24
high expression
Manually annotated by BRENDA team
E1XU24
constitutive expression of Ca22+/calmodulin-dependent neuronal nitric oxide synthase in the central and peripheral nervous system
Manually annotated by BRENDA team
-
peripheral nitrergic nerves, isoform I
Manually annotated by BRENDA team
-
central nervous system, natural variant with 105-amino acid deletion in the heme-binding domain
Manually annotated by BRENDA team
-
comparison of endothelial and neuronal isoform
Manually annotated by BRENDA team
-
isozyme NOS1
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
polymorphonuclear, peritoneal polymorphonuclear
Manually annotated by BRENDA team
-
polymorphonuclear neutrophils, PMN
Manually annotated by BRENDA team
E1XU24
high expression
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
constitutive, soluble form
Manually annotated by BRENDA team
-
distribution, overview, in retinorecipient tectal layer, before and after axotomy and fibroblast growth factor-2 application
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
constitutive, soluble form
-
Manually annotated by BRENDA team
P70313
n the skin, eNOS is present in the epidermal layer, hair follicles and also in the endothelial cells lining the blood vessels
Manually annotated by BRENDA team
-
nNOS, nerve cell bodies and neuronal fibers
Manually annotated by BRENDA team
-
red pulp, eosinophils and neutrophils, isoform II
Manually annotated by BRENDA team
-
distribution, overview, before and after axotomy and fibroblast growth factor-2 application
Manually annotated by BRENDA team
E1XU24
high expression in cephalic tentacle
Manually annotated by BRENDA team
-
eNOS immunoreactivity is detected in germ cells, Sertoli cells, Leydig cells and vascular endothelial cells of the testis, iNOS positive cells are detected in seminiferous epithelial cells, especially in germ cells of the testis
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
additional information
-
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, activity of constitutive enzymes is regulated by binding of calmodulin and Ca2+, the inducible enzyme is regulated by binding of calmodulin, not by Ca2+
Manually annotated by BRENDA team
additional information
Q06518
expression analysis in isolated hepatocytes, healthy liver, and cirrhotic liver, overview
Manually annotated by BRENDA team
additional information
-
immunohistochemic analysis of enzyme distribution, overview
Manually annotated by BRENDA team
additional information
-
nNOS splicing variants tissue distribution, immunohistochemic analysis, overview
Manually annotated by BRENDA team
additional information
-
no activity in gill, intestine, and liver
Manually annotated by BRENDA team
additional information
E1XU24
no expression in salivary glands and the gland of Leiblein
Manually annotated by BRENDA team
additional information
Rattus norvegicus Wistar
-
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
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Rattus norvegicus Sprague-Dawley, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
constitutive endothelial enzyme: predominantly membrane-bound, inducible macrophage enzyme: equally distributed between cytosol and membrane, small constitutive membrane-bound portion in murine macrophages
Manually annotated by BRENDA team
-
total NOS activity is enriched in the intracellular membrane fraction at normal salt diet
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
distinct enzyme not identical to other known isoforms
Manually annotated by BRENDA team
-
isozyme NOS1 contains a mitochondrial targeting signal
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
additional information
-
3 distinct isoforms: 1. a membrane-associated, constitutive enzyme from the vascular endothelium, 2. a soluble, constitutive enzyme from neuronal cells, 3. an endotoxin- and cytokine-inducible enzyme exemplified by that from murine macrophages
-
Manually annotated by BRENDA team
additional information
-
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
-
Manually annotated by BRENDA team
additional information
-
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
-
Manually annotated by BRENDA team
additional information
-
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
-
Manually annotated by BRENDA team
additional information
-
activity of constitutive enzymes is regulated by binding of calmodulin and Ca2+, the inducible enzyme is regulated by binding of calmodulin, not by Ca2+
-
Manually annotated by BRENDA team
additional information
-
subcellular distribution of NOS and caveolin-1, nNOS and iNOS are co-localized with caveolin-1, overview
-
Manually annotated by BRENDA team
additional information
-
subcellular distribution of NOS1
-
Manually annotated by BRENDA team
additional information
Rattus norvegicus Wistar
-
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
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Geobacillus kaustophilus (strain HTA426)