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Information on EC 4.6.1.2 - guanylate cyclase and Organism(s) Sus scrofa and UniProt Accession P55204
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4.6.1.2 guanylate cyclaseIUBMB Comments
Also acts on ITP and dGTP.
Specify your search results
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: Sus scrofa
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
-
-
-
-
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
guanylyl cyclase-C is a peptide hormone receptor
-
-
?
GTP
3',5'-cyclic GMP + diphosphate
guanylin-GC-C interaction, overview
-
-
?
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
-
-
?
additional information
?
-
-
sGC mediates the NO-induced aqueous humor secretion and increased outflow facility from the eye
-
-
?
additional information
?
-
-
sGC role in vascular system diseases and failures, 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
guanylyl cyclase-C is a peptide hormone receptor
-
-
?
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
-
-
?
additional information
?
-
-
sGC mediates the NO-induced aqueous humor secretion and increased outflow facility from the eye
-
-
?
additional information
?
-
-
sGC role in vascular system diseases and failures, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1H-[1,2,4]oxadiazolo[4,3a]quinoxalin-1-one
-
acute addition to pulmonary artery does not affect phenylephrine responsiveness, but restores the responsiveness in pulmonary artery treated with an NO-donor, overview
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
additional information
-
effects of activators and inhibitors on enzyme regulation, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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, 70fold activation as sole stimulator, 160fold in presence of YC-1 and 230fold in presence of sodium nitroprusside
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
BAY 58-2667
-
activates the heme-free sGC 200fold, the activation is increased by inhibitor 1H-[1,2,4]oxidazolol[4,3a]quinoxalin-1-one
cinaciguat
-
cinaciguat activates the heme-free enzyme in a concentration-dependent manner with an EC50 value of about 0.2 microM and maximal cGMP formation at 10 microM. The compound causes time- and concentration-dependent relaxation of precontracted vessels with a maximal effect observed at 90 minutes. The dilatory response is not affected by extensive washout of the drug. Cinaciguat-induced vasodilation is associated with a time- and concentration-dependent increase of cGMP levels. The effect of cinaciguat on 1H-[1,2,4]oxadiazolo-[4,3-a]quinoxalin-1-one-oxidized (ferric) soluble guanylate cyclase is moderate, reaching about 10%-15% of maximal activity
sodium nitroprusside
-
synergistic to YC-1 and A-350619 for the binding site, 230fold activation in presence of A-350619
YC-1
-
synergistic with NO, blocked by 1H-[1,2,4]oxidazolol[4,3a]quinoxalin-1-one, from rats, synergistic to A-350619 and sodium nitroprusside for the binding site, 160fold activation in presence of A-350619
NO
-
activates the soluble guanylate cyclase, the activation is abolished by 1H-[1,2,4]oxadiazolo[4.3a]quinoxalin-1-one
additional information
-
effects of activators and inhibitors on enzyme regulation, overview
-
additional information
-
NO treatment elevates the enzyme activity shortly after application, but does not significantly affect the steady-state levels of cGMP
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
activation of sGC is involved in the nitric oxide-induced increases in outflow facility of the eye
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). GUC2C_PIG
1073
2
123220
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
the enzyme is active as a heterodimer of alpha and beta subunits, but probably requires additional components for activity
additional information
homology structure modeling of the extracellular domain of GC-C, GC-C structure analysis by NMR and fluorescence emission spectroscopy, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
recombinant miniGC-C, comprising the exracellular enzyme domain, binds the heat-stable enterotoxin STp-(5-17) with high affinity, ligand binding and structure analysis, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant Trx-tagged miniGC-C, comprising the extracellular domain, from Escherichia coli strain AD494(DE3) by Co2+ affinity chromatography, dialysis and ultrafiltration, cleavage of the thioredoxin tag
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of a Trx-tagged miniGC-C, comprising the extracellular domain, in Escherichia coli strain AD494(DE3) using expression vector pET-32a
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hasegawa, M.; Kawano, Y.; Matsumoto, Y.; Hidaka, Y.; Fujii, J.i.; Taniguchi, N.; Wada, A.; Hirayama, T.; Shimonishi, Y.
Expression and characterization of the extracellular domain of guanylyl cyclase C from a baculovirus and Sf21 insect cells
Protein Expr. Purif.
15
271-281
1999
Sus scrofa
Perkins, W.J.; Kost, S.L.; Danielson, M.A.
Prolonged NO treatment decreases alpha adrenoreceptor agonist responsiveness in porcine pulmonary artery due to persistent soluble guanylyl cyclase activation
Am. J. Physiol. Lung Cell Mol. Physiol.
296
666-673
2009
Sus scrofa
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)
Ellis, D.Z.; Dismuke, W.M.; Chokshi, B.M.
Characterization of soluble guanylate cyclase in NO-induced increases in aqueous humor outflow facility and in the trabecular meshwork
Invest. Ophthalmol. Vis. Sci.
50
1808-1813
2008
Homo sapiens, Sus scrofa
Lauber, T.; Tidten, N.; Matecko, I.; Zeeb, M.; Roesch, P.; Marx, U.C.
Design and characterization of a soluble fragment of the extracellular ligand-binding domain of the peptide hormone receptor guanylyl cyclase-C
Protein Eng. Des. Sel.
22
1-7
2009
Sus scrofa (P55204)
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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