Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.6.1.2 - guanylate cyclase and Organism(s) Rattus norvegicus and UniProt Accession P16067

for references in articles please use BRENDA:EC4.6.1.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Also acts on ITP and dGTP.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: P16067
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
guanylate cyclase, soluble guanylate cyclase, guanylyl cyclase, soluble guanylyl cyclase, npr-a, npr-b, particulate guanylate cyclase, h-nox, no receptor, guanylyl cyclase c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
natriuretic peptide-activated guanylate cyclase
-
ANPRA
-
-
-
-
ANPRB
-
-
-
-
Atrial natriuretic peptide A-type receptor
-
-
-
-
Atrial natriuretic peptide B-type receptor
-
-
-
-
GC-B
-
isoform
GTP-pyrophosphate lyase
-
-
guanyl cyclase
-
-
-
-
Guanylate cyclase
-
-
-
-
Guanylate cyclase 2D, retinal
-
-
-
-
Guanylate cyclase 2E
-
-
-
-
Guanylate cyclase 2F, retinal
-
-
-
-
guanylate cyclase A
-
-
guanylate cyclase B
-
-
Guanylate cyclase, olfactory
-
-
-
-
guanylyl cyclase
-
-
-
-
guanylyl cyclase C
-
-
hSTAR
-
-
-
-
Intestinal guanylate cyclase
-
-
-
-
KSGC
-
-
-
-
membrane-bound GC
-
-
membrane-bound guanylate cyclase
-
-
natriuretic peptide-activated guanylate cyclase
-
nitric oxide sensitive guanylyl cyclase
-
-
nitric oxide sensitive-guanylyl cyclase
-
-
NO receptor
-
alpha1*beta1 isoform of soluble guanylyl cyclase
NO sensitive guanylyl cyclase
-
-
ONE-GC membrane guanylate cyclase
-
-
Rod outer segment membrane guanylate cyclase
-
-
-
-
ROS-GC
-
-
-
-
ROS-GC2
-
-
-
-
sGC alpha2 inhibitory isoform
-
-
sGC alpha2 isoform
-
-
sGCbeta1
soluble guanylate cyclase
soluble guanylyl cyclase
STA receptor
-
-
-
-
additional information
-
the enzyme is a member of the family of nucleotide cyclizing enzymes
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP = 3',5'-cyclic GMP + diphosphate
show the reaction diagram
reaction mechanism, structure-function relationship
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P-O bond cleavage
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
GTP diphosphate-lyase (cyclizing; 3',5'-cyclic-GMP-forming)
Also acts on ITP and dGTP.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-75-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP
3',5'-cyclic GMP + diphosphate
show the reaction diagram
-
-
-
?
ATP
3',5'-cyclic AMP + diphosphate
show the reaction diagram
-
-
-
-
?
GTP
3',5'-cyclic GMP + diphosphate
show the reaction diagram
GTP
3',5'-cyclic-GMP + diphosphate
show the reaction diagram
guanosine-5'-[alpha,beta-methylene]triphosphate
?
show the reaction diagram
-
-
-
-
?
guanyl-(beta,gamma-methylene)-diphosphate
?
show the reaction diagram
-
-
-
?
guanyl-imidodiphosphate
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP
3',5'-cyclic GMP + diphosphate
show the reaction diagram
-
-
-
?
GTP
3',5'-cyclic GMP + diphosphate
show the reaction diagram
GTP
3',5'-cyclic-GMP + diphosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaN3
-
activation
NaNO3
-
activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17beta-estradiol
-
decreases enzyme activity in immature rats, while the amount of sGC alpha subuit increases, estrogen receptor-dependent effects, overview
1H-(1,2,4)oxadiazole(4,3-a)quinoxalin-1-one
-
-
1H-[1,2,4]-oxadiazole[4,3-a]quinoxalin-1-one
i.e. ODQ, a highly selective sGC inhibitor
1H-[1,2,4]oxadiazolo [4,3,-a]quinoxalin-1-one
i.e. ODQ, in vivo treatment with the sGC inhibitors ODQ does not decrease plasmatic and jejunal cGMP levels, nor does it influence the change in electrical field-induced relaxation
1H-[1,2,4]oxadiazolo[4,3-a]-quinoxalin-1-one
-
specific sGC inhibitor, significantly blocks the capsaicin-induced reduction of mechanical threshold to noxious stimulation of the masseter
1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one
-
-
1H-[1,2,4]oxadiazolo[4,3-a]quinoxaline-1-one
-
-
4H-8-bromo-1,2,4-oxadiazolo(3,4-d)benz(b)(1,4)oxazin-1-one
-
i.e. NS-2028, acts via the heme domain
6-(ethoxymethyl)-1-methyl-1,4,5,6-tetrahydropyrrolo[2,3-g]indazole
-
-
6-(ethoxymethyl)-1-phenyl-1,4,5,6-tetrahydropyrrolo[2,3-g]indazole
-
-
6-(ethoxymethyl)-5,6-dihydro-4H-[1,2]oxazolo[5,4-e]indole
-
-
6-(ethoxymethyl)-6H-[1,2]oxazolo[5,4-e]indole
-
-
6-anilino-5,8-quinolinedione
-
-
6H-[1,2,4]oxadiazolo[4,3-d]pyrido[3,2-b][1,4]oxazin-9-one
-
-
8-(4-methoxyphenyl)-4H-[1,2,4]oxadiazolo[3,4-c][1,4]-benzoxazin-1-one
-
-
8-bromo-4H-[1,2,4]oxadiazolo[3,4-c]benzoxazin-1-one
-
NS 2028
8-oxoguanosine triphosphate
-
i.e. oxo8GTP, a potent competitive inhibitor of nitric oxide-stimulated soluble guanylyl cyclase
8-[3-(trifluoromethyl)phenyl]-4H-[1,2,4]oxadiazolo[3,4-c]-benzoxazin-1-one
-
-
9-chloro-12-oxo-6,12-dihydroquinazolino[2,3-c][1,4]-benzoxazine
-
-
adenosine-5'-tetraphosphate
-
basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity
ADPbetaS
-
basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity
Ca2+
-
1-2 mM
diphosphate
-
-
GDPbetaS
-
basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity
guanosine-5'-tetraphosphate
-
basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity
LY 83583
-
-
LY-83583
-
inhibits the enzyme and completely blocks at 5 mM high frequency stimuli at 20 Hz/20 s-induced gLTP in superior cervical ganglia isolated from control rats
LY83583
-
a selective sGC inhibitor
methylene blue
Mg2+ATPgammaS
-
inhibits cyclase activity through a mixed, non-competitive mechanism, only observable under NO stimulation and not under basal conditions
Mg2+GTPgammaS
-
inhibits cyclase activity through a mixed, non-competitive mechanism, only observable under NO stimulation and not under basal conditions
nitric oxide
-
-
ONE-GC 880MGTTVEPEYFDQVTIYFSDIVG901
-
causes ca. 90% inhibition
ONE-GC 900VGFTTISALSEPIEVVGFLNDL921
-
most effective inhibitor, causes ca. 95% inhibition
oxaloacetate
-
-
phosphoenolpyruvate
-
-
superoxide
-
-
XDP
-
basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity
XTP
-
basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity
[1,2,4]-oxadiazolo[4,3-a]quinoxalin-1-one
-
-
[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-3',5-dihydroxy-4',7-dimethoxyspiro(2H-1-benzopyran-3(4H)-7'-bicyclo[4.2.0]-octa[1,3,5]-trien)4-one
-
activates the soluble guanylate cyclase exhibiting a vasorelaxing effect on the aortic ring, the compound is isolated from bulbs of South African Hyacinthaceae, i.e. Drimiopsis maculata, Eucomis schiffii, Urginea epigea, Drimia altissima, mass spectrometric identification. The compound counteracts vasocontractory agents, overview
(Z)-1-(N,N-diethylamino)diazen-1-ium-1,2-diolate
-
sGC ferrous-nitrosyl complex adopts two 5-coordinate conformations, a lower activity closed form, which releases NO slowly, and a higher activity open form, which releases NO rapidly
1-benzyl-3-(hydroxymethyl-2-furyl)indazole
-
trivial name YC-1, allosteric activator, synergistically increases the catalytic activity in the presence of NO
2-(N,N-diethylamino)-diazenolate-2-oxide
-
stimulates 4.3fold
2-(N,N-diethylamino)diazenolate-2-oxide
-
the wild type enzyme shows 59fold stimulation of activity at 0.001 mM 2-(N,N-diethylamino)diazenolate-2-oxide
3-(5'-hydroxymethyl-2'-furylf)-1-benzylimdazole
-
activation
3-(5'-hydroxymethyl-3'-furyl)-1-benzylindazole
-
-
4-((4-carboxybutyl){2-[(4-phenethyl-benzyl)oxy]-phenethyl}amino)methyl[benzoic]acid
-
NO- and heme-independent sGC activator, stimulates 15fold, stimulation increases up to 30fold in the presence of 1H-(1,2,4)-oxadiazole-(4,3-a)-quinoxalin-1-one
5-cyclopropyl-2-[1-(2-fluoro-benzyl)-1H-pyrazolo[3,4-b]pyridin-3-yl]-pyrimidin-4-ylamine
-
NO-independent but heme-dependent sGC stimulator, stimulates the enzyme in a concentration-dependent manner
5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
-
the wild type enzyme shows 6fold stimulation of activity at 0.1 mM
A-350619
-
a heme-dependent stimulator of sGC, structurally not related to YC-1, but synergistic to YC-1 and sodium nitroprusside for the binding site
A-778935
-
i.e. cis-3-[2-(2,2-dimethyl-propylsulfanyl)pyridin-3-yl]-N-(3-hydroxycyclohexyl-)acrylamide, derived from the YC-1 structure, activates the enzyme is a synergistic fashion with the NO donor sodium nitroprusside
Activator protein
-
from rat lung
-
adenylylimidophosphate
-
activation
ataciguat
-
HMR 1766
ATP
-
induces a concentration-dependent increase in basal and atrial natriuretic peptide 1-28-stimulated GC activity of glomerular and papillary membranes that is significantly higher in spontaneously hypertensive rats than in age-matched Wistar Kyoto rats
ATP(gamma)S
-
activation
ATPgammaS
-
is more effective than ATP on glomerular and papillary membranes, has little effect on GC activity in solubilized membranes
atrial natriuretic peptide
-
atrial natriuretic peptide 1-28
-
increases GC enzymatic activity of glomerular and papillary membranes in a concentration-dependent manner
-
BAY 41-2272
BAY 41-8543
-
lowers blood pressure in normotensive rats
BAY 58-2667
-
long term treatment causes a slight decrease in systolic blood pressure
BAY 60-2770
-
i.e. 4-([(4-carboxybutyl)[2-(5-fluoro-2-([4'-(trifluoromethyl)biphenyl-4-yl]methoxy)phenyl)ethyl]amino]methyl)benzoic acid, NO-independent activation, the compound attenuates pig serum-induced liver fibrosis in vivo but does not affect blodd pressure in spontaneously hypertensive rats, overview
BaY 63-2521
-
i.e. methyl-4,6-diamino-2-(1-(2-fluorobenzyl)-1H-pyrazolo[3,4-b]pyridin-3-yl)pyrimindin-5-ylmethylcarbamate, stimulates sGC directly and sensitizes it to NO, causes enzyme upregulation in pulmonary arterial hypertension lungs
brain natriuretic peptide
-
activation of isoforms GC-A and GC-B
-
C-type natriuretic peptide
-
cGMP
-
activation
cinaciguat
-
BAY 58-2667
G protein alpha subunit
-
-
-
heat-stable enterotoxin
-
-
-
HMR-1766
-
chronic treatment causes reduced ex-vivo platelet adhesion and in vivo vasodilator-stimulated phosphoprotein phosphorylation
Lubrol Px
-
activation
N-(beta-D-glucopyranosyl-N2-acetyl-S-nitroso-D,L-penicillaminamide)
-
NO donor
natriuretic peptide
-
-
-
neurocalcin
-
in the presence of the semimicromolar range of free Ca2+, neurocalcin binds to the catalytic module and stimulates ONE-GC, M880-L921 region of ONE-GC is the Ca2+-dependent neurocalcin binding and the transduction site of ONE-GC
-
neurocalcin sigma
-
dose-dependent stimulation in presence of the 0.01 mM Ca2+, 8fold over the basal value at ca. 0.002 mM
-
nitric oxide
nitrosobutane
-
6fold activation in absence of 3-(5'-hydroxymethyl-3'-furyl)-1-benzylimidazole, 47fold activation in presence of 0.15 mM 3-(5'-hydroxymethyl-3'-furyl)-1-benzylimidazole
nitrosohexane
-
2fold activation in absence of 3-(5'-hydroxymethyl-3'-furyl)-1-benzylimidazole, 33fold activation in presence of 0.15 mM 3-(5'-hydroxymethyl-3'-furyl)-1-benzylimidazole
nitrosooctane
-
2fold activation in absence of 3-(5'-hydroxymethyl-3'-furyl)-1-benzylimidazole, 11fold activation in presence of 0.15 mM 3-(5'-hydroxymethyl-3'-furyl)-1-benzylimidazole
nitrosopentane
-
2fold activation in absence of 3-(5'-hydroxymethyl-3'-furyl)-1-benzylimidazole, 39fold activation in presence of 0.15 mM 3-(5'-hydroxymethyl-3'-furyl)-1-benzylimidazole
nitrosopropane
-
2fold activation in absence of 3-(5'-hydroxymethyl-3'-furyl)-1-benzylimidazole, 45fold activation in presence of 0.15 mM 3-(5'-hydroxymethyl-3'-furyl)-1-benzylimidazole
phenylhydrazine
-
acivation
prostaglandin endoepoxide analogs
-
activation
-
protoporphyrin-IX
-
the wild type enzyme shows 1.9fold stimulation of activity at 0.1 mM and 12fold stimulation at 0.01 mM
S-nitroso-N-acetylpenicillamine
-
the wild type enzyme shows 14.5fold stimulation of activity at 0.1 mM
sodium nitroprusside
Triton X-100
-
activation
unsaturated fatty acids
-
activation
-
uroguanylin
-
stimulates ONE-GC through its external domain in a dose-dependent fashion
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.8234
GTP
0.37
guanyl-(beta,gamma-methylene)-diphosphonate
-
-
0.07
guanyl-imidodiphosphate
-
-
2.7
Mn2+
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.251
Mg2+GTPgammaS
-
pH 8.0, 30°C, wild-type enzyme
additional information
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.288 - 1.8
8-oxoguanosine triphosphate
0.06
900VGFTTISALSEPIEVVGFLNDL921
Rattus norvegicus
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.047
-
mutant enzyme D102N, at pH 8.5 and 33°C, in the absence of any stimulator
0.073
-
mutant enzyme D102E, at pH 8.5 and 33°C, in the absence of any stimulator
0.087
-
mutant enzyme D102N, at pH 8.5 and 33°C, in the presence of 0.1 mM protoporphyrin-IX
0.108
-
mutant enzyme F120A, at pH 8.5 and 33°C, in the presence of 0.1 mM protoporphyrin-IX
0.12
-
basal activity
0.128
-
mutant enzyme D102E, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
0.152
-
mutant enzyme D102E, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
0.16
-
mutant enzyme D102A, at pH 8.5 and 33°C, in the presence of 0.1 mM protoporphyrin-IX
0.161
-
mutant enzyme D102A, at pH 8.5 and 33°C, in the absence of any stimulator
0.168
-
mutant enzyme D102E, at pH 8.5 and 33°C, in the presence of 0.1 mM protoporphyrin-IX
0.169
-
mutant enzyme F120A, at pH 8.5 and 33°C, in the absence of any stimulator
0.172
-
mutant enzyme F120A, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
0.202
-
mutant enzyme D102N, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
0.229
0.231
-
mutant enzyme F120A, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol and 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
0.276
-
with Mn2+
0.278
-
mutant enzyme F120A, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
0.292
-
mutant enzyme D102E, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol and 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
0.354
-
mutant enzyme D102A, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
0.431
-
wild type enzyme, at pH 8.5 and 33°C, in the presence of 0.1 mM protoporphyrin-IX
0.662
-
mutant enzyme D102A, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol and 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
1.063
-
mutant enzyme D102N, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol and 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
1.232
-
mutant enzyme D102A, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
1.43
-
wild type enzyme, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
12.1
-
in the presence of 0.1 mM N-(beta-D-glucopyranosyl-N2-acetyl-S-nitroso-D,L-penicillaminamide) and YC-1
3.328
-
wild type enzyme, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
3.402
-
wild type enzyme, at pH 8.5 and 33°C, in the presence of 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol and 0.1 mM 5-[1-(phenylmethyl)-1H-indazol-3-yl]-2-furanmethanol
9.1
-
in the presence of 0.1 mM N-(beta-D-glucopyranosyl-N2-acetyl-S-nitroso-D,L-penicillaminamide)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.5
-
presence of activators
7.4 - 8
-
-
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 37
-
inclusion of 3-(5'-hydroxymethyl-3'-furyl)-1-benzylindazole moderately accelerates NO dissociation from sGC and beta2(1-217) at 37°C and dramatically accelerates NO dissociation from sGC at 10°C. Presence of guanosine-5'-[alpha,beta-methylene]triphosphate also dramatically accelerates NO dissociation from sGC at 10 °C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NPR-B; adult male Wistar rats
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
natriuretic peptide-activated guanylate cyclase NPR-B is expressed in several layers of the retina including amacrine cells and the ganglion cell layer
Manually annotated by BRENDA team
-
brain natriuretic peptide stimulated membrane-bound GC
Manually annotated by BRENDA team
-
2-4 months old
Manually annotated by BRENDA team
-
prominent for beta1 and to a lesser extent for the other subunits
Manually annotated by BRENDA team
-
high expression of beta1 and moderate to low expression of both alpha subunits
Manually annotated by BRENDA team
-
coronary
Manually annotated by BRENDA team
-
highest levels of mRNA for beta1, alpha1 and alpha2 subunits
Manually annotated by BRENDA team
-
beta1 subunit mRNA widely distributed through all cortical areas and cell layers with higher intensity in layer V, alpha2 mRNA homogeneously distributed through all cortical layers and alpha1 expression higher in layers II–III and V
Manually annotated by BRENDA team
-
moderate expression of alpha1 and alpha2 mRNAs in many white matter tracts, beta1 mRNA expression is very low
Manually annotated by BRENDA team
-
atrial- and C-type natriuretic peptide stimulated membrane-bound GC
Manually annotated by BRENDA team
-
expression of the beta1 subunit moderate in the ventromedial, dorsomedial, arcuate, and geniculate nuclei. In these hypothalamic nuclei levels for the alpha subunits are low, all three subunits show moderate levels in the interpeduncular nucleus
Manually annotated by BRENDA team
-
sGC alpha2 and beta1 subunits expressed strongly by dentate gyrus granule cells and CA1-CA3 pyramidal neurons, expression of alpha1 mRNA is high in CA2 pyramidal cells but low in the other CA subfields
Manually annotated by BRENDA team
-
alveolar
Manually annotated by BRENDA team
-
high levels of beta1 but low levels of alpha subunits in superior colliculus, locus coeruleus presents high levels of beta1 and alpha1 subunits, ventral tegmental nucleus wiht moderate levels of expression for the three sGC subunits
Manually annotated by BRENDA team
-
brain- and atrial natriuretic peptide stimulated membrane-bound GC
Manually annotated by BRENDA team
-
high expression of beta1 and moderate to low expression of both alpha subunits
Manually annotated by BRENDA team
-
adrenal medulla derived cell line
Manually annotated by BRENDA team
-
shows high levels of expression for beta1 mRNA and moderate for alpha1 and alpha2 mRNAs
Manually annotated by BRENDA team
-
anterior, sGC alpha2 inhibitory isoform and sGC alpha2 isoform are expressed
Manually annotated by BRENDA team
-
upper villous and crypt cells
Manually annotated by BRENDA team
-
shows high expression of beta1, moderate of alpha2, and low of alpha1
Manually annotated by BRENDA team
-
moderate expression of beta1, alpha subunits expression is very low
Manually annotated by BRENDA team
-
high levels of mRNA for the three subunits in the medial habenula, in other thalamic nuclei mainly beta1 mRNA
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
nuclear localization of the soluble guanylate cyclase in alveolar macrophages in nucleoplasm
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
nitric oxide sensitive guanylyl cyclase is the major physiological receptor for nitric oxide throughout the cardiovascular and central nervous system
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ANPRB_RAT
1047
2
117127
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
135000 - 160000
150000
-
gel filtration
19500
1 * 38500 + 1 * 19500, gel filtration, homodimers of sGC have also been observed but are not functionally active
200000
-
gel filtatrion
300000
-
particulate form, sucrose density gradient centrifugation
38500
1 * 38500 + 1 * 19500, gel filtration, homodimers of sGC have also been observed but are not functionally active
450000
-
soluble form, gel filtration
70000
700000 - 900000
-
particulate form, gel filtration
70400
-
1 * 78600 + 1 * 70400, calculated from amino acid sequence
72000
-
1 * 80000 + 1 * 72000, SDS-PAGE
74000
-
1 * 79400 + 1 * 74000
77000
-
beta1 subunit of sGC, Western blot analysis
78600
-
1 * 78600 + 1 * 70400, calculated from amino acid sequence
79400
-
1 * 79400 + 1 * 74000
80000
-
1 * 80000 + 1 * 72000, SDS-PAGE
82000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
heterodimer
homodimer
-
-
additional information
-
each of the catalytic domains alphacat and betacat (expressed in Escherichia coli), form homodimers. Heterodimers are formed when alphacat and betacat are combined
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
sGC is phosphorylated at Ser64 of the alpha1 subunit by the cGMP-dependent protein kinase, which leads to sGC inhibition, no phosphorylation of the enzyme mutant S64A alpha1/beta1 sGC, mutational determination of the phosphorylation site, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M Bis-Tris pH 7.0, and 0.7 M ammonium sulfate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C238S
-
no change in cGMP production
C243S
-
no change in cGMP production
C594D
-
no 1-benzyl-3-(hydroxymethyl-2-furyl)indazole activation, no synergy with NO
C594D/E525K
-
loss of activity
C594Y
-
reduced level of NO and 1-benzyl-3-(hydroxymethyl-2-furyl)indazole activation
D102A
-
the mutant shows 70% of wild type activity
D102E
-
the mutant shows 32% of wild type activity
D102N
-
the mutant shows 20.5% of wild type activity
D477A
E138A
the mutant is less responsive to nitric oxide in comparison to the wild type enzyme
E525K/C594D
-
mutation in alpha subunit, mutant does not show a non-competitive mechanism with Mg2+GTPgammaS and Mg2+ATPgammaS that is observed with wild-type enzyme
F120A
-
the mutant shows 73% of wild type activity
G114A
the mutant has characteristics similar to the wild type enzyme
I111A
the mutant has a decreased basal activity and is less responsive to activators in comparison to the wild type enzyme
I41A
the mutant is strongly activated by YC-1, nitric oxide and to a lesser extent by protoporphyrin IX
M537N
-
high level of 1-benzyl-3-(hydroxymethyl-2-furyl)indazole activation
R40A
the mutation results in a drastic decrease not only in basal activity but also in stimulated activity in response to protoporphyrin IX, YC-1, nitric oxide
S64A
-
an alpha1/beta1 sGC mutant, shows resistance to phosphorylation by the cGMP-dependent protein kinase
S64D
-
an alpha1/beta1 sGC mutant, is less activated by NO in comparison to the wild-type enzyme
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis inactivates
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-60°C, N2 atmosphere, 25 mM triethanolamine, pH 7.8, 5 mM dithiothreitol, 1 M NaCl, 30% glycerol, several months
-
-70°C, 10 mM dithiothreitol, 25% sucrose, several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cobalt affinity column chromatography and Mono Q anion exchange column chromatography
-
Ni-NTA column chromatography, Q-Sepharose column chromatography, and Superdex 75 gel filtration
on Ni-NTA affinity column
-
on Ni2+ column and anion-exchange column
-
recombinant His-tagged enzyme
-
recombinant sGC
-
Strep-Tactin1 Superflow column chromatography, Mono Q column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
beta1 (residues 1-194) and beta2 (residues 1-217) homodimers expressed in Escherichia coli
-
catalytic domains (alphacat and betacat) of alpha1beta1 soluble guanylate cyclase are expressed in Escherichia coli
-
construction of a fluorescent alpha1/beta1-sGC heterodimer by fusion of the N-terminal YFP fragment and the C-terminal fragment to the N terminus and the C terminus of the alpha1- and beta1-subunit, respectively. Generated fusion proteins, wild-type and deletion mutants transiently expressed in a cGMP reporter cell line based on a Chinese hamster ovary cell line stably transfected with the cyclic nucleotide gated olfactory CNG2A-channel and cytosolic aequorin
-
COS-7 cells transfected with the wild-type ONE-GC cDNA or its deletion mutants, ONE-GC mutants into pET30aLIC vector, expressed in Escherichia coli BL21-Codon-Plus-RIL
-
expressed in Sf21 insect cells
-
expressed in Sf9 insect cells
-
expression analysis of enzyme subunits during the estrous cycle overview
-
expression analysis of sGC subunits in pulmonary artery tissue from healthy and hypertensive lungs
-
expression in CHO cells in a reporter-coupled system, overview
-
expression of alpha1 and beta1 subunits and mutant enzyme in COSm6 and A7r5 smooth muscle cells
-
expression of sGC in Sf9 insect cells and COS-7 cells
-
expression of wild-type alpha1beta2 sGC enzyme in Spodoptera frugiperda Sf9 cells, and of heme domain mutants in Escherichia coli
-
MDCK cell lines expressing HA-tagged GCC or HA-tagged GCC lacking the amino acids from the conserved 63 amino acid span
-
N-terminal heme-binding regions of subunit beta1 from soluble guanylate cyclase are generated by subcloning specific constructs into the Escherichia coli expression vector pET-20b. The shortest region that is subcloned, has heme-bound, and is expressed well is beta1(1-194)
-
sGC beta1 cDNA inserted between the NotI and XbaI sites of the plasmid pFastBac1, H6sGC alpha1 gene inserted between the NotI and XbaI sites of pFastBac1, expression in Sf9 cells
-
the beta1 subunit of soluble guanylyl cyclase is expressed in Escherichia coli BL21 (DE3) pLysS cells
wild-type and mutant enzymes expressed in Sf21/baculovirus system
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ohlstein, E.H.; Wood, K.S.; Ignarro, L.J.
Purification and properties of heme-deficient hepatic soluble guanylate cyclase: effects of heme and other factors on enzyme activation by NO, NO-heme, and protoporphyrin IX
Arch. Biochem. Biophys.
218
187-198
1982
Rattus norvegicus
Manually annotated by BRENDA team
Zwiller, J.; Basset, P.; Mandel, P.
Rat brain guanylate cyclase. Purification, amphiphilic properties and immunological characterization
Biochim. Biophys. Acta
658
64-75
1981
Rattus norvegicus
Manually annotated by BRENDA team
Spruill, W.A.; Steiner, A.L.; Earp, H.S.
Characterization of rat testicular guanylate cyclase during development
Biochim. Biophys. Acta
587
484-494
1979
Rattus norvegicus
Manually annotated by BRENDA team
Braughler, J.M.; Mittal, C.K.; Murad, F.
Purification of soluble guanylate cyclase from rat liver
Proc. Natl. Acad. Sci. USA
76
219-222
1979
Rattus norvegicus
Manually annotated by BRENDA team
Garbers, D.L.
Purification of soluble guanylate cyclase from rat lung
J. Biol. Chem.
254
240-243
1979
Rattus norvegicus
Manually annotated by BRENDA team
Tsai, S.C.; Manganiello, V.C.; Vaughan, M.
Purification of guanylate cyclase from rat liver supernatant
J. Biol. Chem.
253
8452-8457
1978
Rattus norvegicus
-
Manually annotated by BRENDA team
Nakane, M.; Deguchi, T.
Purification and properties of guanylate cyclase from the synaptosomal soluble fraction of rat brain
Biochim. Biophys. Acta
525
275-285
1978
Rattus norvegicus
Manually annotated by BRENDA team
Craven, P.A.; DeRubertis, F.R.
Properties and subcellular distribution of guanylate cyclase activity in rat renal medulla: correlation with tissue content of guanosine 3 ,5 -monophosphate
Biochemistry
15
5131-5137
1976
Rattus norvegicus
Manually annotated by BRENDA team
Neer, E.J.; Sukiennnik, E.A.
Guanylate cyclase from the rat renal medulla. Physical properties and comparison with adenylate cyclase
J. Biol. Chem.
250
7905-7909
1975
Rattus norvegicus
Manually annotated by BRENDA team
De Jonge, H.R.
Properties of guanylate cyclase and levels of cyclic GMP in rat small intestinal villous and crypt cells
FEBS Lett.
55
143-152
1975
Rattus norvegicus
Manually annotated by BRENDA team
Chrisman, T.D.; Garbers, D.L.; Parks, M.A.; Hardman, J.G.
Characterization of particulate and soluble guanylate cyclases from rat lung
J. Biol. Chem.
250
374-381
1975
Rattus norvegicus
Manually annotated by BRENDA team
Hardman, J.C.; Sutherland, E.W.
Guanyl cyclase, an enzyme catalyzing the formation of guanosine 3 ,5 -monophosphate from guanosine trihosphate
J. Biol. Chem.
244
6363-6370
1969
Rattus norvegicus
Manually annotated by BRENDA team
Hoenicka, M.; Becker, E.M.; Apeler, H.; Sirichoke, T.; Schroeder, H.; Gerzer, R.; Stasch, J.P.
Purified soluble guanylyl cyclase expressed in a baculovirus/Sf9 system: stimulation by YC-1, nitric oxide, and carbon monoxide
J. Mol. Med.
77
14-23
1999
Rattus norvegicus
Manually annotated by BRENDA team
Hakki, S.; Crane, M.; Hugues, M.; O'Hanley, P.; Waldman, S.A.
Solubilization and characterization of functionally coupled Escherichia coli heat-stable toxin receptors and particulate guanylate cyclase associated with the cytoskeleton compartment of intestinal membranes
Int. J. Biochem.
25
557-566
1993
Rattus norvegicus
Manually annotated by BRENDA team
Grabow, M.; Chakraborty, G.; Ledeen, R.W.
Characterization of guanylyl cyclase in purified myelin
Neurochem. Res.
21
457-462
1996
Rattus norvegicus
Manually annotated by BRENDA team
Chang, C.H.; Kohse, K.P.; Chang, B.; Hirata, M.; Jiang, B.; Douglas, J.E.; Murad, F.
Characterization of ATP-stimulated guanylate cyclase activation in rat lung membranes
Biochim. Biophys. Acta
1052
159-165
1990
Rattus norvegicus
Manually annotated by BRENDA team
Waldman, S.A.; Leitman, D.C.; Murad, F.
Immunoaffinity purification of soluble guanylyl cyclase
Methods Enzymol.
195
391-396
1991
Rattus norvegicus
Manually annotated by BRENDA team
Lamothe, M.; Chang, F.J.; Balashova, N.; Shirokov, R.; Beuve, A.
Functional Characterization of Nitric Oxide and YC-1 Activation of Soluble Guanylyl Cyclase: Structural Implication for the YC-1 Binding Site?
Biochemistry
43
3039-3048
2004
Rattus norvegicus
Manually annotated by BRENDA team
Rambotti, M.G.; Spreca, A.; Giambanco, I.; Sorci, G.; Donato, R.
Ultracytochemistry as a tool for the study of the cellular and subcellular localization of membrane-bound guanylate cyclase (GC) activity. Applicability to both receptor-activated and receptor-independent GC activity
Mol. Cell. Biochem.
230
85-96
2002
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Derbyshire, E.R.; Tran, R.; Mathies, R.A.; Marletta, M.A.
Characterization of nitrosoalkane binding and activation of soluble guanylate cyclase
Biochemistry
44
16257-16265
2005
Rattus norvegicus
Manually annotated by BRENDA team
Karow, D.S.; Pan, D.; Davis, J.H.; Behrends, S.; Mathies, R.A.; Marletta, M.A.
Characterization of functional heme domains from soluble guanylate cyclase
Biochemistry
44
16266-16274
2005
Rattus norvegicus
Manually annotated by BRENDA team
Winger, J.A.; Marletta, M.A.
Expression and characterization of the catalytic domains of soluble guanylate cyclase: interaction with the heme domain
Biochemistry
44
4083-4090
2005
Rattus norvegicus
Manually annotated by BRENDA team
Chang, F.J.; Lemme, S.; Sun, Q.; Sunahara, R.K.; Beuve, A.
Nitric oxide-dependent allosteric inhibitory role of a second nucleotide binding site in soluble guanylyl cyclase
J. Biol. Chem.
280
11513-11519
2005
Rattus norvegicus
Manually annotated by BRENDA team
Cary, S.P.; Winger, J.A.; Marletta, M.A.
Tonic and acute nitric oxide signaling through soluble guanylate cyclase is mediated by nonheme nitric oxide, ATP, and GTP
Proc. Natl. Acad. Sci. USA
102
13064-13069
2005
Rattus norvegicus
Manually annotated by BRENDA team
Woodard, G.E.; Zhao, J.; Rosado, J.A.
Different effect of ATP on ANP receptor guanylyl cyclase in spontaneously hypertensive and normotensive rats
Acta Physiol. (Oxf.)
188
195-206
2006
Rattus norvegicus
Manually annotated by BRENDA team
Belik, J.; Hehne, N.; Pan, J.; Behrends, S.
Soluble guanylate cyclase-dependent relaxation is reduced in the adult rat bronchial smooth muscle
Am. J. Physiol. Lung Cell Mol. Physiol.
292
L699-L703
2007
Rattus norvegicus
Manually annotated by BRENDA team
Duda, T.; Sharma, R.K.
ONE-GC membrane guanylate cyclase, a trimodal odorant signal transducer
Biochem. Biophys. Res. Commun.
367
440-445
2008
Rattus norvegicus
Manually annotated by BRENDA team
Ro, J.Y.; Lee, J.; Capra, N.F.; Zhang, Y.
Role of soluble guanylate cyclase in the trigeminal subnucleus caudalis in capsaicin-induced muscle hypersensitivity
Brain Res.
1184
141-148
2007
Rattus norvegicus
Manually annotated by BRENDA team
Poulos, T.L.
Soluble guanylate cyclase
Curr. Opin. Struct. Biol.
16
736-743
2006
Bos taurus, Clostridium botulinum, Homo sapiens, Rattus norvegicus, Caldanaerobacter subterraneus subsp. tengcongensis, Vibrio cholerae serotype O1
Manually annotated by BRENDA team
Mueller, D.; Cortes-Dericks, L.; Budnik, L.T.; Brunswig-Spickenheier, B.; Pancratius, M.; Speth, R.C.; Mukhopadhyay, A.K.; Middendorff, R.
Homologous and lysophosphatidic acid-induced desensitization of the atrial natriuretic peptide receptor, guanylyl cyclase-A, in MA-10 leydig cells
Endocrinology
147
2974-2985
2006
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Winger, J.A.; Derbyshire, E.R.; Marletta, M.A.
Dissociation of nitric oxide from soluble guanylate cyclase and heme-nitric oxide/oxygen binding domain constructs
J. Biol. Chem.
282
897-907
2007
Rattus norvegicus
Manually annotated by BRENDA team
Ding, J.D.; Weinberg, R.J.
Localization of soluble guanylyl cyclase in the superficial dorsal horn
J. Comp. Neurol.
495
668-678
2006
Rattus norvegicus
Manually annotated by BRENDA team
Pifarre, P.; Garcia, A.; Mengod, G.
Species differences in the localization of soluble guanylyl cyclase subunits in monkey and rat brain
J. Comp. Neurol.
500
942-957
2007
Macaca fascicularis, Rattus norvegicus
Manually annotated by BRENDA team
Ding, J.D.; Weinberg, R.J.
Distribution of soluble guanylyl cyclase in rat retina
J. Comp. Neurol.
502
734-745
2007
Rattus norvegicus
Manually annotated by BRENDA team
Rothkegel, C.; Schmidt, P.M.; Atkins, D.J.; Hoffmann, L.S.; Schmidt, H.H.; Schroeder, H.; Stasch, J.P.
Dimerization region of soluble guanylate cyclase characterized by bimolecular fluorescence complementation in vivo
Mol. Pharmacol.
72
1181-1190
2007
Rattus norvegicus
Manually annotated by BRENDA team
Hodson, C.A.; Ambrogi, I.G.; Scott, R.O.; Mohler, P.J.; Milgram, S.L.
Polarized apical sorting of guanylyl cyclase C is specified by a cytosolic signal
Traffic
7
456-464
2006
Rattus norvegicus
Manually annotated by BRENDA team
Cabilla, J.P.; Ronchetti, S.A.; Nudler, S.I.; Miler, E.A.; Quinteros, F.A.; Duvilanski, B.H.
Nitric oxide sensitive-guanylyl cyclase subunits expression changes during estrous cycle in anterior pituitary glands
Am. J. Physiol. Endocrinol. Metab.
296
731-737
2009
Rattus norvegicus
Manually annotated by BRENDA team
Jebelovszki, E.; Kiraly, C.; Erdei, N.; Feher, A.; Pasztor, E.T.; Rutkai, I.; Forster, T.; Edes, I.; Koller, A.; Bagi, Z.
High-fat diet-induced obesity leads to increased NO sensitivity of rat coronary arterioles: role of soluble guanylate cyclase activation
Am. J. Physiol. Heart Circ. Physiol.
294
H2558-H2564
2008
Rattus norvegicus
Manually annotated by BRENDA team
Zhou, Z.; Sayed, N.; Pyriochou, A.; Roussos, C.; Fulton, D.; Beuve, A.; Papapetropoulos, A.
Protein kinase G phosphorylates soluble guanylyl cyclase on serine 64 and inhibits its activity
Arterioscler. Thromb. Vasc. Biol.
28
1803-1810
2008
Rattus norvegicus
Manually annotated by BRENDA team
Knorr, A.; Hirth-Dietrich, C.; Alonso-Alija, C.; Haerter, M.; Hahn, M.; Keim, Y.; Wunder, F.; Stasch, J.P.
Nitric oxide-independent activation of soluble guanylate cyclase by BAY 60-2770 in experimental liver fibrosis
Arzneimittelforschung
58
71-80
2008
Rattus norvegicus
Manually annotated by BRENDA team
Derbyshire, E.R.; Gunn, A.; Ibrahim, M.; Spiro, T.G.; Britt, R.D.; Marletta, M.A.
Characterization of two different five-coordinate soluble guanylate cyclase ferrous-nitrosyl complexes
Biochemistry
47
3892-3899
2008
Rattus norvegicus
Manually annotated by BRENDA team
Coffey, M.J.; Phare, S.M.; Luo, M.; Peters-Golden, M.
Guanylyl cyclase and protein kinase G mediate nitric oxide suppression of 5-lipoxygenase metabolism in rat alveolar macrophages
Biochim. Biophys. Acta
1781
299-305
2008
Rattus norvegicus
Manually annotated by BRENDA team
El-Awady, M.S.; Smirnov, S.V.; Watson, M.L.
Desensitization of the soluble guanylyl cyclase/cGMP pathway by lipopolysaccharide in rat isolated pulmonary artery but not aorta
Br. J. Pharmacol.
155
1164-1173
2008
Rattus norvegicus
Manually annotated by BRENDA team
Hoenicka, M.; Schmid, C.
Cardiovascular effects of modulators of soluble guanylyl cyclase activity
Cardiovasc. Hematol. Agents Med. Chem.
6
287-301
2008
Bos taurus, Canis lupus familiaris, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa, Ovis aries (Q8SPV3)
Manually annotated by BRENDA team
Ruiz-Torres, M.P.; Griera, M.; Chamorro, A.; Diez-Marques, M.L.; Rodriguez-Puyol, D.; Rodriguez-Puyol, M.
Tirofiban increases soluble guanylate cyclase in rat vascular walls: pharmacological and pathophysiological consequences
Cardiovasc. Res.
82
125-132
2009
Rattus norvegicus
Manually annotated by BRENDA team
Schermuly, R.T.; Stasch, J.P.; Pullamsetti, S.S.; Middendorff, R.; Mueller, D.; Schlueter, K.D.; Dingendorf, A.; Hackemack, S.; Kolosionek, E.; Kaulen, C.; Dumitrascu, R.; Weissmann, N.; Mittendorf, J.; Klepetko, W.; Seeger, W.; Ghofrani, H.A.; Grimminger, F.
Expression and function of soluble guanylate cyclase in pulmonary arterial hypertension
Eur. Respir. J.
32
881-891
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Bolin, C.; Cardozo-Pelaez, F.
Characterization of oxidized guanosine 5-triphosphate as a viable inhibitor of soluble guanylyl cyclase
Free Radic. Biol. Med.
46
828-835
2009
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Powers-Martin, K.; Barron, A.M.; Auckland, C.H.; McCooke, J.K.; McKitrick, D.J.; Arnolda, L.F.; Phillips, J.K.
Immunohistochemical assessment of cyclic guanosine monophosphate (cGMP) and soluble guanylate cyclase (sGC) within the rostral ventrolateral medulla
J. Biomed. Sci.
15
801-812
2008
Rattus norvegicus
Manually annotated by BRENDA team
Fusi, F.; Ferrara, A.; Koorbanally, C.; Crouch, N.R.; Mulholland, D.A.; Sgaragli, G.
Vascular myorelaxing activity of isolates from South African Hyacinthaceae partly mediated by activation of soluble guanylyl cyclase in rat aortic ring preparations
J. Pharm. Pharmacol.
60
489-497
2008
Rattus norvegicus
Manually annotated by BRENDA team
Fernandes, D.; de Sordi, R.; Pacheco, L.K.; Nardi, G.M.; Heckert, B.T.; Villela, C.G.; Lobo, A.R.; Barja-Fidalgo, C.; Assreuy, J.
Late but not early inhibition of soluble guanylate cyclase decreases mortality in a rat sepsis model
J. Pharmacol. Exp. Ther.
328
991-999
2008
Rattus norvegicus (P19686), Rattus norvegicus (Q80WY4)
Manually annotated by BRENDA team
Alzoubi, K.H.; Alkadhi, K.A.
Calmodulin and guanylyl cyclase inhibitors block the in vivo expression of gLTP in sympathetic ganglia from chronically stressed rats
Neurosci. Res.
63
95-99
2009
Rattus norvegicus
Manually annotated by BRENDA team
Abdelalim, E.M.; Masuda, C.; Tooyama, I.
Expression of natriuretic peptide-activated guanylate cyclases by cholinergic and dopaminergic amacrine cells of the rat retina
Peptides
29
622-628
2008
Rattus norvegicus (P16067), Rattus norvegicus (P18910)
Manually annotated by BRENDA team
Vanneste, G.; Van Nassauw, L.; Kalfin, R.; Van Colen, I.; Elinck, E.; Van Crombruggen, K.; Timmermans, J.P.; Lefebvre, R.A.
Jejunal cholinergic, nitrergic, and soluble guanylate cyclase activity in postoperative ileus
Surgery
144
410-426
2008
Rattus norvegicus (Q02108), Rattus norvegicus (Q02153)
Manually annotated by BRENDA team
Murphy, B.A.; Fakira, K.A.; Song, Z.; Beuve, A.; Routh, V.H.
AMP-activated protein kinase and nitric oxide regulate the glucose sensitivity of ventromedial hypothalamic glucose-inhibited neurons
Am. J. Physiol. Cell Physiol.
297
C750-C758
2009
Rattus norvegicus
Manually annotated by BRENDA team
Spyridonidou, K.; Fousteris, M.; Antonia, M.; Chatzianastasiou, A.; Papapetropoulos, A.; Nikolaropoulos, S.
Tricyclic indole and dihydroindole derivatives as new inhibitors of soluble guanylate cyclase
Bioorg. Med. Chem. Lett.
19
4810-4813
2009
Rattus norvegicus
Manually annotated by BRENDA team
von Wantoch Rekowski, M.; Pyriochou, A.; Papapetropoulos, N.; Stoessel, A.; Papapetropoulos, A.; Giannis, A.
Synthesis and biological evaluation of oxadiazole derivatives as inhibitors of soluble guanylyl cyclase
Bioorg. Med. Chem.
18
1288-1296
2010
Rattus norvegicus
Manually annotated by BRENDA team
Ma, X.; Beuve, A.; van den Akker, F.
Crystal structure of the signaling helix coiled-coil domain of the beta1 subunit of the soluble guanylyl cyclase
BMC Struct. Biol.
10
2-2
2010
Rattus norvegicus (P20595)
Manually annotated by BRENDA team
Haase, N.; Haase, T.; Kraehling, J.R.; Behrends, S.
Direct fusion of subunits of heterodimeric nitric oxide sensitive guanylyl cyclase leads to functional enzymes with preserved biochemical properties: evidence for isoform specific activation by ciguates
Biochem. Pharmacol.
80
1676-1683
2010
Rattus norvegicus
Manually annotated by BRENDA team
Baskaran, P.; Heckler, E.J.; van den Akker, F.; Beuve, A.
Aspartate 102 in the heme domain of soluble guanylyl cyclase has a key role in NO activation
Biochemistry
50
4291-4297
2011
Rattus norvegicus
Manually annotated by BRENDA team
Shpakov, A.; Derkach, K.; Chistyakova, O.; Pertseva, M.
Changes in the functional activity of membrane-bound guanylate cyclase forms in tissues of diabetic rats
Dokl. Biochem. Biophys.
433
219-222
2010
Rattus norvegicus
Manually annotated by BRENDA team
Baskaran, P.; Heckler, E.J.; van den Akker, F.; Beuve, A.
Identification of residues in the heme domain of soluble guanylyl cyclase that are important for basal and stimulated catalytic activity
PLoS ONE
6
e26976
2011
Rattus norvegicus (P20595)
Manually annotated by BRENDA team
Ghosh, A.; Stuehr, D.J.
Soluble guanylyl cyclase requires heat shock protein 90 for heme insertion during maturation of the NO-active enzyme
Proc. Natl. Acad. Sci. USA
109
12998-13003
2012
Rattus norvegicus
Manually annotated by BRENDA team