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Information on EC 2.7.11.12 - cGMP-dependent protein kinase and Organism(s) Oryctolagus cuniculus and UniProt Accession O77676
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2.7.11.12 cGMP-dependent protein kinaseIUBMB Comments
CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates . The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase .
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Word Map
- 2.7.11.12
- cyclase
-
guanylyl
-
guanylate
-
camp-dependent
- phosphodiesterase
- endothelial
- artery
-
natriuretic
- pka
- cardiac
- nitroprusside
- 8-br-cgmp
-
contractile
- atrial
- phosphoprotein
-
myocytes
-
vasodilation
- 8-bromo-cgmp
-
l-name
-
no-induced
- sildenafil
-
vasorelaxation
-
l-type
-
cgmp-mediated
-
vasodilator-stimulated
-
patch-clamp
-
membrane-permeable
- snap
- vasp
-
cell-attached
- monophosphorothioate
- nonoate
-
cgmp-independent
- zaprinast
-
no-cgmp
-
iberiotoxin
-
atp-sensitive
-
1h-1,2,4oxadiazolo4,3-aquinoxalin-1-one
-
large-conductance
- s-nitroso-n-acetylpenicillamine
-
8-bromo-cyclic
-
cgmp-specific
- cak
- drug development
- 8-bromoguanosine
- rp-camps
-
cgmp-inhibited
-
nitrovasodilators
- medicine
- mypt1
- pharmacology
-
no-sensitive
-
oxide-cyclic
The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
cgmp-dependent protein kinase, protein kinase g, cyclic gmp-dependent protein kinase, cgkii, pkg-i, cgmp kinase, prkg1, pkg ii, cgk ii, cgmp-dependent protein kinase i, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CGK
-
-
-
-
CGK 1 alpha
-
-
-
-
CGK 1 beta
-
-
-
-
CGKI-alpha
-
-
-
-
cGKI-beta
-
-
-
-
cGKII
-
-
-
-
cGMP-dependent protein kinase
-
-
-
-
Foraging protein
-
-
-
-
protein kinase G
-
-
-
-
Type II cGMP-dependent protein kinase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (cGMP-dependent)
CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates [3]. The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase [4].
CAS REGISTRY NUMBER
COMMENTARY
141588-27-4
-
141588-27-4
cGMP-dependent protein kinase
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
ATP + inositol 1,4,5-trisphosphate receptor-I
ADP + phosphorylated inositol 1,4,5-trisphosphate receptor-I
ATP + inositol 1,4,5-trisphosphate receptor-I
ADP + phosphorylated inositol 1,4,5-trisphosphate receptor-I
-
the phosphorylation of the receptor inhibits inositol 1,4,5-trisphosphate-induced Ca2+ release
-
-
?
ATP + inositol 1,4,5-trisphosphate receptor-I
ADP + phosphorylated inositol 1,4,5-trisphosphate receptor-I
-
selective phosphorylation at Ser1755
-
-
?
additional information
?
-
-
PKG-1 is involved in NO-induced cGMP-mediated increase in corpus cavernosum smooth muscle relaxation and penile erection, enzyme disfunction can cause erectile dysfunction, diabetes reduces corpus cavernosum smooth muscle relaxation
-
-
?
additional information
?
-
-
PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins
-
-
?
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
ATP + inositol 1,4,5-trisphosphate receptor-I
ADP + phosphorylated inositol 1,4,5-trisphosphate receptor-I
-
the phosphorylation of the receptor inhibits inositol 1,4,5-trisphosphate-induced Ca2+ release
-
-
?
additional information
?
-
-
PKG-1 is involved in NO-induced cGMP-mediated increase in corpus cavernosum smooth muscle relaxation and penile erection, enzyme disfunction can cause erectile dysfunction, diabetes reduces corpus cavernosum smooth muscle relaxation
-
-
?
additional information
?
-
-
PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KT5823
-
i.e. (8R,9S,11S)-(-)-9-methoxy-carbamyl-8-methyl-2,3,9,10-tetrahydro-8,11-epoxy-1H,8H-2,7b,11a-trizadizobenzo9(a,g)cycloocta(c,d,e)-trinden-1-one, selective PKG inhibitor
additional information
-
enzyme activity is reduced in diabetic rabbits
-
additional information
-
no inhibition by myristoylated PKI14-22 amide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-pCPT-CGMP
-
i.e. 8-(4-chlorophenylthio)guanosine 3',5'-cyclic monophosphate, 358% activation, inhibitor KT5823 abolishes the activating effect
sodium nitroprusside
-
i.e. SNP, selective activator of PKG, 414% activation, inhibitor KT5823 abolishes the activating effect
additional information
-
high glucose levels induce NO-induced stimulation of cGMP production and increase PKG-1 activity
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
corpus cavernosum smooth muscle, high expression of isozymes PKG-1alpha and PKG-1beta, corpus cavernosum smooth muscle of diabetic rabbits show reduced expression of isozyme PKG-1alpha
-
corpus cavernosum smooth muscle, high expression of isozymes PKG-1alpha and PKG-1beta, corpus cavernosum smooth muscle of diabetic rabbits show reduced expression of isozyme PKG-1alpha
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview
physiological function
-
PKG-I is a serine/threonine-specific protein kinase that is activated by the NO/sGC/cGMP system. PKG-I is involved in many cell functions, such as relaxation, platelet aggregation, remodelling, hypertrophy, apoptosis, differentiation, neuronal plasticity, and erectile dysfunction
additional information
-
the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform
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). KGP1_RABIT
671
0
76454
Swiss-Prot
other Location (Reliability: 2)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded
additional information
-
the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kumar, R.; Joyner, R.W.; Komalavilas, P.; Lincoln, T.M.
Analysis of expression of cGMP-dependent protein kinase in rabbit heart cells
J. Pharmacol. Exp. Ther.
291
967-975
1999
Oryctolagus cuniculus (O77676), Oryctolagus cuniculus
Chang, S.; Hypolite, J.A.; Velez, M.; Changolkar, A.; Wein, A.J.; Chacko, S.; DiSanto, M.E.
Downregulation of cGMP-dependent protein kinase-1 activity in the corpus cavernosum smooth muscle of diabetic rabbits
Am. J. Physiol.
287
R950-960
2004
Oryctolagus cuniculus
Murthy, K.S.; Zhou, H.
Selective phosphorylation of the IP3R-I in vivo by cGMP-dependent protein kinase in smooth muscle
Am. J. Physiol. Gastronintest. Liver Physiol.
284
G221-230
2003
Oryctolagus cuniculus
Sellak, H.; Choi, C.S.; Dey, N.B.; Lincoln, T.M.
Transcriptional and post-transcriptional regulation of cGMP-dependent protein kinase (PKG-I): pathophysiological significance
Cardiovasc. Res.
97
200-207
2013
Bos taurus, Oryctolagus cuniculus, Ovis aries, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
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