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Information on EC 4.6.1.2 - guanylate cyclase and Organism(s) Bos taurus and UniProt Accession P19687
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4.6.1.2 guanylate cyclaseIUBMB Comments
Also acts on ITP and dGTP.
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Word Map
- 4.6.1.2
- cgmp
- artery
- guanosine
- nitroprusside
- monophosphate
- phosphodiesterase
-
methylene
-
vasodilation
- endothelium
-
cgmp-dependent
-
l-name
- l-arginine
- pkg
-
tone
-
endothelium-dependent
-
blocker
- aorta
- acetylcholine
-
vasorelaxation
-
endothelium-derived
- ng-nitro-l-arginine
- snap
- phenylephrine
- 8-br-cgmp
- ng-monomethyl-l-arginine
-
endothelium-denuded
- nnos
- nomega-nitro-l-arginine
-
apamin
-
no-dependent
- zaprinast
- tetraethylammonium
- 8-bromo-cgmp
- glibenclamide
- sin-1
- s-nitroso-n-acetylpenicillamine
-
no-mediated
- sildenafil
-
no-induced
-
precontracted
- nitroglycerin
- diagnostics
- trinitrate
- molecular biology
- analysis
-
iberiotoxin
- cavernosum
- 7-nitroindazole
-
no-donors
- pharmacology
- medicine
-
phototransduction
-
charybdotoxin
-
endothelium-intact
- drug development
-
nitrergic
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ANPRA
-
-
-
-
ANPRB
-
-
-
-
Atrial natriuretic peptide A-type receptor
-
-
-
-
Atrial natriuretic peptide B-type receptor
-
-
-
-
guanyl cyclase
-
-
-
-
Guanylate cyclase
-
-
-
-
Guanylate cyclase 2D, retinal
-
-
-
-
Guanylate cyclase 2E
-
-
-
-
Guanylate cyclase 2F, retinal
-
-
-
-
Guanylate cyclase, olfactory
-
-
-
-
guanylyl cyclase
-
-
-
-
hSTAR
-
-
-
-
Intestinal guanylate cyclase
-
-
-
-
KSGC
-
-
-
-
Rod outer segment membrane guanylate cyclase
-
-
-
-
ROS-GC
-
-
-
-
ROS-GC2
-
-
-
-
sGC
soluble guanylate cyclase
STA receptor
-
-
-
-
additional information
-
the enzyme is a member of the family of nucleotide cyclizing enzymes
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP = 3',5'-cyclic GMP + diphosphate
reaction mechanism, structure-function relationship
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P-O bond cleavage
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
SYSTEMATIC NAME
IUBMB Comments
GTP diphosphate-lyase (cyclizing; 3',5'-cyclic-GMP-forming)
Also acts on ITP and dGTP.
CAS REGISTRY NUMBER
COMMENTARY
9054-75-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP
3',5'-cyclic GMP + diphosphate
-
cGMP is involved in transmitting the NO activating signals to a variety of downstream effectors such as cyclicnucleotide-gated channels, protein kinases, and phosphodiesterases
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
-
664860, 665511, 666248, 679399, 680671, 681631, 684348, 690841, 691656, 692446, 693082, 693256, 693267, 694270, 694411
-
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
cGMP is involved in transmitting the NO activating signals to a variety of downstream effectors such as cyclicnucleotide-gated channels, protein kinases, and phosphodiesterases
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
the guanylyl cyclase messenger system is potentially responsive to hormones/neurotranmitters that may control the degree of relaxation in this vascular tissue
-
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
sGC activity plays an important role in a variety of aspects of the cardiovascular system, regulatory mechanisms, overview. sGC has an anti-proliferative effect on smooth muscle cells
-
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
sGC produces cGMP, a second messenger required for normal vascular smooth muscle cell, VSMC, relaxation. Activating NADPH oxidase in bovine aortic VSMC increases ROS levels and induces oxidative posttranslational modification of Cys122, a beta1-subunit cysteinyl residue of the guanylate cyclase leading to its inhibition
-
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
the enzyme is involved in regualtion of artery contaction, enzyme activation by NO leads to increased pulmonary artery relaxation
-
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
the retinal isozyme retGC-1 influences transducin movement, not through its cyclase activity, but through direct interaction with Galphat protein, overview
-
-
?
additional information
?
-
-
2'-deoxy-3'-GMP and cGMP exhibit no detectable affinity for the enzyme
-
-
?
additional information
?
-
-
GMPNH-P, GMPCH-P and N-methylanthraniloyl 2'-GTP are poor substrates
-
-
?
additional information
?
-
-
heme oxygenase-1 induction depletes heme and attenuates pulmonary artery relaxation and guanylate cyclase activation by nitric oxide
-
-
?
additional information
?
-
-
sGC role in vascular system diseases and failures, overview
-
-
?
additional information
?
-
-
the enzyme binds the human rod Galphat protein without altering cyclase activity, interactions with ligands, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP
3',5'-cyclic GMP + diphosphate
-
cGMP is involved in transmitting the NO activating signals to a variety of downstream effectors such as cyclicnucleotide-gated channels, protein kinases, and phosphodiesterases
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
cGMP is involved in transmitting the NO activating signals to a variety of downstream effectors such as cyclicnucleotide-gated channels, protein kinases, and phosphodiesterases
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
the guanylyl cyclase messenger system is potentially responsive to hormones/neurotranmitters that may control the degree of relaxation in this vascular tissue
-
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
sGC activity plays an important role in a variety of aspects of the cardiovascular system, regulatory mechanisms, overview. sGC has an anti-proliferative effect on smooth muscle cells
-
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
sGC produces cGMP, a second messenger required for normal vascular smooth muscle cell, VSMC, relaxation. Activating NADPH oxidase in bovine aortic VSMC increases ROS levels and induces oxidative posttranslational modification of Cys122, a beta1-subunit cysteinyl residue of the guanylate cyclase leading to its inhibition
-
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
the enzyme is involved in regualtion of artery contaction, enzyme activation by NO leads to increased pulmonary artery relaxation
-
-
?
GTP
3',5'-cyclic GMP + diphosphate
-
the retinal isozyme retGC-1 influences transducin movement, not through its cyclase activity, but through direct interaction with Galphat protein, overview
-
-
?
additional information
?
-
-
heme oxygenase-1 induction depletes heme and attenuates pulmonary artery relaxation and guanylate cyclase activation by nitric oxide
-
-
?
additional information
?
-
-
sGC role in vascular system diseases and failures, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
the weak Fe2+-proximal His bond is a key determinant for the low O2 affinity of the heme moiety of soluble guanylate cyclase
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe2+
Mg2+
Mn2+
Ca2+
-
Ca2+-dependent negative feedback control mediated by guanylate-activating proteins
Ca2+
-
activates, is required for activation of the retinal enzyme by cone-specific calcium sensor guanylate cyclase activating protein 4
Fe2+
-
ligands of the form XO can bind to the heme Fe in either a linear or bent configuration
Mg2+
-
-
Mg2+
-
one Mg2+ is primarily associated with the enzyme and the second is directly bound to the alpha, beta and gamma phosphates of GTP
Mg2+
-
activates up to 2 mM, in the presence of small amounts of Mn2+ activation increases dramatically
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2'-dADP
-
mixture of competitive and noncompetitive inhibition, binding to the substrate site excludes the substrate GTP, whereas binding to the noncompetitive site has no effect on GTP binding, although the resulting complex is catalytically inactive. It binds to the high and low affinity sites with equivalent affinities. BAY 41-2272, which shares an analogous core structure to YC-1, fully inhibits 2'-dADP binding to the low affinity site, whereas the inhibition by YC-1 is incomplete
2'-deoxy-3'-O-(N-methylanthraniloyl)-guanosine 5'-[beta,gamma-imido]triphosphate
-
-
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
8-oxoguanosine triphosphate
-
i.e. oxo8GTP, a potent inhibitor of nitric oxide-stimulated soluble guanylyl cyclase
adenosine 5'-beta,gamma-imido triphosphate
-
competitive inhibitor, reduces the Bmax for the binding of guanosine 5'-beta,gamma-methylene triphosphate, is tightly and selectively associated with the high affinity site
aldosterone
-
diminishes GC activity by activating NADPH oxidase in bovine aortic VSMC to increase ROS levels and induce oxidative posttranslational modification of Cys122, a beta1-subunit cysteinyl residue
Ca2+ ionophore A23187
-
Ca2+-dependent inhibition of sGC can be achieved with the Ca2+ ionophore A23187 (0.01 mM)
Calmidazolium
-
uncompetitive inhibition, time-dependent inhibition at 0.03 mM, pre-treatment of sGC with calmidazolium, followed by filtration, causes an 80% inhibition of sGC activation by nitric oxide and a 23% inhibition of activation by protoporphyrin IX
DNIC-G
-
a dinitrosyl iron complex, solutions contain 18fold molar excess of free thiosulfate, inhibition of the NO-stimulated enzyme, inhibited by GSH
DNIC-Y
-
a dinitrosyl iron complex, no free thiosulfate in solutions of the binuclear complex DNIC-Y, inhibition of the NO-stimulated enzyme, inhibited by GSH
H2O2
-
diminishes GC activity by activating NADPH oxidase in bovine aortic VSMC to increase ROS levels and induce oxidative posttranslational modification of Cys122, a beta1-subunit cysteinyl residue
ATP
-
mechanism involving ATP pre-binding is physiologically relevant to activation of retinal guanylate cyclase, inhibition at high concentrations
ATP
-
80% inhibition at 0.1 mM, affects C-type NP 1-53 stimulation of the enzyme, in the presence of Mn2+ inhibition of mastoparan-induced activation of the enzyme
Ca2+
-
inhibition of both, the basal and NO-stimulated forms of sGC, competitive vs. Mg2+, noncompetitive vs. MgGTP
additional information
-
desensitization of the enzyme to NO and inactivation of soluble guanylate cyclase by stoichiometric S-nitrosation through dinitrosyl iron complexes, which is slowly reversible by GSH, overview
-
additional information
-
effects of activators and inhibitors on enzyme regulation, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-ethyl-3-(ethylaminoethyl)-1-hydroxy-2-oxo-1-triazene
stimulates via release of NO
2'-deoxy-3'-GMP
-
the addition of the effector to CO-activated enzyme causes the original 6-coordinate CO-heme to convert to an end product that is an equimolar mixture of a 5- and a new 6-coordinate CO-heme
2,2-diethyl-1-nitroso-oxyhydrazine
-
70-80% activation at 0.01 mM in presence of 2 mM GSH
3-ethyl-3-(ethylaminoethyl)-1-hydroxy-2-oxo-1-triazene
stimulates via release of NO
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
ATP
-
mechanism involving ATP pre-binding is physiologically relevant to activation of retinal guanylate cyclase, inhibition at high concentrations
cone-specific calcium sensor guanylate cyclase activating protein 4
-
encoded by gene zGCAP4 from zebrafish, cloning and expression in Escherichia coli, zGCAP4 is a strong activator of membrane-bound guanylate cyclases from bovine retina, mainly present as a monomer and showing half-maximal activation at 520-570 nM free Ca2+ concentration
-
Foscarnet
-
the addition of the effector to CO-activated enzyme causes the original 6-coordinate CO-heme to convert to an end product that is an equimolar mixture of a 5- and a new 6-coordinate CO-heme
guanylate-activating protein
-
proteins GCAP-1 and GCAP-2, Ca2+-dependent negative feedback control
-
protoporphyrin IX
-
0.001 mM activates untreated sGC with around half the effectiveness of nitric oxide
additional information
-
effects of activators and inhibitors on enzyme regulation, overview
-
BAY 41-2272
-
one molecule is required for maximal enzyme activation and is tightly associated with sGC
BAY 41-2272
-
the addition of the effector to CO-activated enzyme causes the original 6-coordinate CO-heme to convert to an end product that is an equimolar mixture of a 5- and a new 6-coordinate CO-heme
CO
-
ferrous soluble guanylate cyclase binds CO as two reversible steps. The primary step leads to the full conversion of the ferrous enzyme to the 6-coordinate CO-heme, followed by the slower second step leading to a partial conversion of the 6-coordinate CO-heme to the 5-coordinate CO-heme. Reaction may folow a multistep mechanism, in which the 5-coordinate CO-heme is led by CO release from a putative bis-carbonyl intermediate that is likely provided by the binding of a second CO to the 6-coordinate CO-heme
hydrogencarbonate
ED50 value of 27 mM. Stimulation is more powerful in the presence of activating protein GCAP1 or GCAP2 at low concentrations of Ca2+
hydrogencarbonate
ED50 value of 39 mM. When applied to retinal photoreceptors, hydrogencarbonate enhances the circulating current, decreases sensitivity to flashes, and accelerates flash response kinetics
NO
-
perfect heme ligand, serves as an effector of enzyme activation via conformational transitions
NO
-
about 5000fold activation over basal level, mechanism for NO receptor activation and its modulation by GTP, ATP, and allosteric agents, model formation comprising a module in which NO, the nucleotides, and allosteric agents bind and the protein undergoes a conformational change, dovetailing with a catalytic module where GTP is converted to cGMP and diphosphate, enzyme-linked receptor mechanism, overview
NO
-
activation of sGC by NO, released from 2,2-diethyl-1-nitroso-oxyhydrazine, is a link to the nitroglycerin biotransformation by mitochondrial aldehyde dehydrogenase, ALDH2
NO
-
binding of NO to a regulatory heme group at the beta-subunit of the protein results in 100fold stimulation of cGMP formation, NO is involved in the vascular NO/cGMP signalling, dysfunction of the signaling is thought to contribute to a wide variety of cardiovascular disorders
NO
-
the enzyme activation by NO leads to increased pulmonary artery relaxation, the activation is inhibited by heme depletion through heme oxygenase-1 induction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
GTP
purified recombinant sGC in presence of 3-ethyl-3-(ethylaminoethyl)-1-hydroxy-2-oxo-1-triazene
0.043
GTP
purified recombinant sGC in presence of 3-ethyl-3-(ethylaminoethyl)-1-hydroxy-2-oxo-1-triazene
additional information
additional information
kinetics, purified recombinant sGC, overview
-
additional information
additional information
kinetics, purified recombinant sGC, overview
-
additional information
additional information
-
kinetics, purified recombinant sGC, overview
-
additional information
additional information
-
activation kinetics and thermodynamics, binding of GTP and NO, overview
-
additional information
additional information
kinetics, purified recombinant sGC, overview
-
additional information
additional information
kinetics, purified recombinant sGC, overview
-
additional information
additional information
-
kinetics, purified recombinant sGC, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.53
2'-deoxy-3'-O-(N-methylanthraniloyl)-guanosine 5'-[beta,gamma-imido]triphosphate
-
pH 7.4, 30°C
0.23
N-methylanthraniloyl-adenosine 5'-[beta,gamma-imido]triphosphate
-
pH 7.4, 30°C
1.5
N-methylanthraniloyl-guanosine 5'-[beta,gamma-imido]triphosphate
-
pH 7.4, 30°C
1.7
N-methylanthraniloyl-xanthosine 5'-[beta,gamma-imido]triphosphate
-
pH 7.4, 30°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.33
purified recombinant sGC in presence of 3-ethyl-3-(ethylaminoethyl)-1-hydroxy-2-oxo-1-triazene
1.33
purified recombinant sGC in presence of 3-ethyl-3-(ethylaminoethyl)-1-hydroxy-2-oxo-1-triazene
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the guanylyl cyclase messenger system is potentially responsive to hormones/neurotranmitters that may control the degree of relaxation in this vascular tissue
-
retina and rod segements, retGC is a transmembrane protein localized in the outer segment
-
GC-B is the predominant functional membrane-bound guanylyl cyclase subtype
-
-
34833, 34850, 34857, 34858, 34866, 34869, 34874, 34879, 34881, 649442, 665511, 666248, 679399, 680671, 684348, 691656, 692446, 693082, 694270, 694411, 707918, 715597, 747134
-
-
-
soluble guanylate cyclase accounts for nearly 10% of the total guanylate cyclase activity of the retina
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
-
-
rod outer segment membrane
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
soluble guanylate cyclase is an NO-sensing hemoprotein that serves as a nitric oxide receptor in nitric oxide-mediated signaling pathways
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GCYA1_BOVIN
691
0
77533
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
74000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C122A
-
site-directed mutagenesis of the aldosterone modification site, the mutant is insensitive to inhibition by aldosterone or H2O2
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native soluble guanylate cyclase from lung to high yield by two different steps of anion chromatography, hydroxyapatite chromatography, a third anion exchange chromatography, GTP affinity chromatography, and gel filtration
-
-
native soluble guanylate cyclase from lung to high yield by two different steps of anion chromatography, hydroxyapatite chromatography, a third anion exchange chromatography, GTP affinity chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
pre-treatment of sGC with Tween-20 (0.5%), followed by filtration to remove the detergent, decreases the effectiveness of nitric oxide for activating cGMP synthesis by 73%
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
purified sGC can act as detector for NO-like bioactivity generated from nitrite and glycerol trinitrate and for NO released by heart and liver mitochondria
additional information
-
two nucleotide-binding sites with high and low affinity for GMP-CPP, one of the two sites constitutes the substrate site responsible for catalysis. The other site is the pseudosymmetric site, which exclusively serves as the binding site for YC-1 or BAY 41-2272
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaever, V.; Szamel, M.; Goppelt, M.; Resch, K.
Characterization and subcellular localization of nucleotide cyclases in calf thymus lymphocytes
Biochim. Biophys. Acta
776
133-143
1984
Bos taurus
Gorczyca, W.A.; VanHooser, J.P.; Palczewski, K.
Nucleotide inhibitors and activators of retinal guanylyl cyclase
Biochemistry
33
3217-3222
1994
Bos taurus
Gerzer, R.; Hofmann, F.; Schultz, G.
Purification of a soluble, sodium-nitroprusside-stimulated guanylate cyclase from bovine lung
Eur. J. Biochem.
116
479-486
1981
Bos taurus
Fleischman, D.; Denisevich, M.
Guanylate cyclase of isolated bovine retinal rod axonemes
Biochemistry
18
5060-5066
1979
Bos taurus
Krishnan, N.; Fletcher, R.T.; Chader, G.J.; Krishna, G.
Characterization of guanylate cyclase of rod outer segments of the bovine retina
Biochim. Biophys. Acta
523
506-515
1978
Bos taurus
White, A.A.; Zenser, T.V.
Preparation and characterization of guanylate cyclase from bovine lung
Methods Enzymol.
38C
192-195
1974
Bos taurus
Hakki, S.; Sitaramayya, A.
Guanylate cyclase from bovine rod outer segments: solubilization, partial purification, and regulation by inorganic pyrophosphate
Biochemistry
29
1088-1094
1990
Bos taurus
Serfass, L.; Burstyn, J.N.
Effect of heme oxygenase inhibitors on soluble guanylyl cyclase activity
Arch. Biochem. Biophys.
359
8-16
1998
Bos taurus
Mayer, B.; Schrammel, A.; Klatt, P.; Koesling, D.; Schmidt, K.
Peroxynitrite-induced accumulation of cyclic GMP in endothelial cells and stimulation of purified soluble guanylyl cyclase
J. Biol. Chem.
29
17355-17360
1995
Bos taurus
Hayashi, F.; Yamazaki, A.
Polymorphism in purified guanylate cyclase from vertebrate rod photoreceptors
Proc. Natl. Acad. Sci. USA
88
4746-4750
1991
Bos taurus, Rhinella marina, Lithobates catesbeianus
Koch, K.W.
Purification and identification of photoreceptor guanylate cyclase
J. Biol. Chem.
266
8634-8637
1991
Bos taurus
Wolbring, G.; Baehr, W.; Palczewski, K.; Schnetkamp, P.P.
Light inhibition of bovine retinal rod guanylyl cyclase mediated by beta gamma-transducin
Biochemistry
38
2611-2616
1999
Bos taurus
Ivanova, K.; Heim, J.M.; Gerzer, R.
Kinetic characterization of atrial natriuretic factor-sensitive particulate guanylate cyclase
Eur. J. Pharmacol.
189
317-326
1990
Bos taurus
Schrammel, D.; Koesling, D.; Gorren, A.C.F.; Chevion, M.; Schmidt, K.; Mayer, B.
Inhibition of purified soluble guanylyl cyclase by copper ions
Biochem. Pharmacol.
52
1041-1045
1996
Bos taurus
Bocanera, L.V.; Martinetto, H.; Flawia, M.M.; Pisarev, M.A.
Partial characterization of guanylyl cyclase activity in calf thyroid
Endocr. Res.
25
215-228
1999
Bos taurus
Stone, J.R.; Marletta, M.A.
Soluble guanylate cyclase from bovine lung: activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states
Biochemistry
33
5636-5640
1994
Bos taurus
Aparicio, J.G.; Applebury, M.L.
The bovine photoreceptor outer segment guanylate cyclase: purification, kinetic properties, and molecular size
Protein Expr. Purif.
6
501-511
1995
Bos taurus
Li, P.L.; Jin, M.W.; Campbell, W.B.
Effect of selective inhibition of soluble guanylyl cyclase on the K(Ca) channel activity in coronary artery smooth muscle
Hypertension
31
303-308
1998
Bos taurus
Tomita, T.; Tsuyama, S.; Imai, Y.; Kitagawa, T.
Purification of bovine soluble guanylate cyclase and ADP-ribosylation on its small subunit by bacterial toxins
J. Biochem.
122
531-536
1997
Bos taurus
Horio, Y.; Murad, F.
Purification of guanylyl cyclase from rod outer segments
Biochim. Biophys. Acta
1133
81-88
1991
Bos taurus
Muelsch, A.; Gerzer, R.
Purification of heme-containing soluble guanylyl cyclase
Methods Enzymol.
195
377-383
1991
Bos taurus
Humbert, P.; Niroomand, F.; Fischer, G.; Mayer, B.; Koesling, D.; Hinsch, K.D.; Schultz, G.; Boehme, E.
Preparation of soluble guanylyl cyclase from bovine lung by immunoaffinity chromatography
Methods Enzymol.
195
384-389
1991
Bos taurus
Borges, A.; de Villarroel, S.S.; Winand, N.J.; de Becemberg, I.L.; Alfonzo, M.J.; de Alfonzo, R.G.
Molecular and biochemical characterization of a CNP-sensitive guanylyl cyclase in bovine tracheal smooth muscle
Am. J. Respir. Cell Mol. Biol.
25
98-103
2001
Bos taurus
Serfass, L.; Carr, H.S.; Aschenbrenner, L.M.; Burstyn, J.N.
Calcium ion downregulates soluble guanylyl cyclase activity: Evidence for a two-metal ion catalytic mechanism
Arch. Biochem. Biophys.
387
47-56
2001
Bos taurus
Hwang, J.Y.; Lange, C.; Helten, A.; Hoeppner-Heitmann, D.; Duda, T.; Sharma, R.K.; Koch, K.W.
Regulatory modes of rod outer segment membrane guanylate cyclase differ in catalytic efficiency and Ca2+-sensitivity
Eur. J. Biochem.
270
3814-3821
2003
Bos taurus
Sitaramayya, A.
Soluble guanylate cyclases in the retina
Mol. Cell. Biochem.
230
177-186
2002
Bos taurus, Mus musculus
Yamazaki, M.; Usukura, J.; Yamazaki, R.K.; Yamazaki, A.
ATP binding is required for physiological activation of retinal guanylate cyclase
Biochem. Biophys. Res. Commun.
338
1291-1298
2005
Bos taurus
Schmidt, K.G.; Geyer, O.; Mittag, T.W.
Adenylyl and guanylyl cyclase activity in the choroid
Exp. Eye Res.
78
901-907
2004
Bos taurus
Gille, A.; Lushington, G.H.; Mou, T.C.; Doughty, M.B.; Johnson, R.A.; Seifert, R.
Differential inhibition of adenylyl cyclase isoforms and soluble guanylyl cyclase by purine and pyrimidine nucleotides
J. Biol. Chem.
279
19955-19969
2004
Bos taurus
Russwurm, M.; Koesling, D.
Purification and characterization of NO-sensitive guanylyl cyclase
Methods Enzymol.
396
492-501
2005
Bos taurus
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
Yazawa, S.; Tsuchiya, H.; Hori, H.; Makino, R.
Functional characterization of two nucleotide-binding sites in soluble guanylate cyclase
J. Biol. Chem.
281
21763-21770
2006
Bos taurus
Alfonzo, M.J.; de Aguilar, E.P.; de Murillo, A.G.; de Villarroel, S.S.; de Alfonzo, R.G.; Borges, A.; de Becemberg, I.L.
Characterization of a G protein-coupled guanylyl cyclase-B receptor from bovine tracheal smooth muscle
J. Recept. Signal Transduct. Res.
26
269-297
2006
Bos taurus
Mingone, C.J.; Ahmad, M.; Gupte, S.A.; Chow, J.L.; Wolin, M.S.
Heme oxygenase-1 induction depletes heme and attenuates pulmonary artery relaxation and guanylate cyclase activation by nitric oxide
Am. J. Physiol. Heart Circ. Physiol.
294
H1244-H1250
2008
Bos taurus
Rosenzweig, D.H.; Nair, K.S.; Levay, K.; Peshenko, I.V.; Crabb, J.W.; Dizhoor, A.M.; Slepak, V.Z.
Interaction of retinal guanylate cyclase with the alpha subunit of transducin: potential role in transducin localization
Biochem. J.
417
803-812
2009
Bos taurus, Mus musculus, Homo sapiens (Q02846)
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)
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
Roy, B.; Halvey, E.J.; Garthwaite, J.
An enzyme-linked receptor mechanism for nitric oxide-activated guanylyl cyclase
J. Biol. Chem.
283
18841-18851
2008
Bos taurus
Maron, B.A.; Zhang, Y.Y.; Handy, D.E.; Beuve, A.; Tang, S.S.; Loscalzo, J.; Leopold, J.A.
Aldosterone increases oxidant stress to impair guanylyl cyclase activity by cysteinyl thiol oxidation in vascular smooth muscle cells
J. Biol. Chem.
284
7665-7672
2009
Bos taurus
Behnen, P.; Scholten, A.; Raetscho, N.; Koch, K.W.
The cone-specific calcium sensor guanylate cyclase activating protein 4 from the zebrafish retina
J. Biol. Inorg. Chem.
14
89-99
2009
Bos taurus, Danio rerio
Mayer, B.; Kleschyov, A.L.; Stessel, H.; Russwurm, M.; Munzel, T.; Koesling, D.; Schmidt, K.
Inactivation of soluble guanylate cyclase by stoichiometric S-nitrosation
Mol. Pharmacol.
75
886-891
2008
Bos taurus
Kollau, A.; Beretta, M.; Russwurm, M.; Koesling, D.; Keung, W.M.; Schmidt, K.; Mayer, B.
Mitochondrial nitrite reduction coupled to soluble guanylate cyclase activation: lack of evidence for a role in the bioactivation of nitroglycerin
Nitric Oxide
20
53-60
2009
Bos taurus
Mathis, K.J.; Emmons, T.L.; Curran, D.F.; Day, J.E.; Tomasselli, A.G.
High yield purification of soluble guanylate cyclase from bovine lung
Protein Expr. Purif.
60
58-63
2008
Bos taurus (P16068), Bos taurus (P19687), Bos taurus
James, L.R.; Griffiths, C.H.; Garthwaite, J.; Bellamy, T.C.
Inhibition of nitric oxide-activated guanylyl cyclase by calmodulin antagonists
Br. J. Pharmacol.
158
1454-1464
2009
Bos taurus
Makino, R.; Park, S.Y.; Obayashi, E.; Iizuka, T.; Hori, H.; Shiro, Y.
Oxygen binding and redox properties of the heme in soluble guanylate cyclase: implications for the mechanism of ligand discrimination
J. Biol. Chem.
286
15678-15687
2011
Bos taurus
Makino, R.; Obata, Y.; Tsubaki, M.; Iizuka, T.; Hamajima, Y.; Kato-Yamada, Y.; Mashima, K.; Shiro, Y.
Mechanistic insights into the activation of soluble guanylate cyclase by carbon monoxide a multistep mechanism proposed for the BAY 41-2272 induced formation of 5-coordinate CO-heme
Biochemistry
57
1620-1631
2018
Bos taurus
EXTERNAL LINKS (specific for EC-Number 4.6.1.2)
Transporter Classification Database (TCDB): 1.A.87.2.9, 8.A.85.1.6, 8.A.85.1.2, 8.A.85.1.1, 8.A.85.1.3
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