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Information on EC 2.7.11.11 - cAMP-dependent protein kinase and Organism(s) Bos taurus and UniProt Accession P00517

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IUBMB Comments
This eukaryotic enzyme recognizes the sequence -Arg-Arg-X-Ser*/Thr*-Hpo, where * indicates the phosphorylated residue and Hpo indicates a hydrophobic residue.The inactive holoenzyme is a heterotetramer composed of two regulatory (R) subunits and two catalytic (C) subunits. Each R subunit occludes the active site of a C subunit and contains two binding sites for 3',5'-cyclic-AMP (cAMP). Binding of cAMP activates the enzyme by causing conformational changes that release two free monomeric C subunits from a dimer of the R subunits, i.e. R2C2 + 4 cAMP = R2(cAMP)4 + 2 C. Activity requires phosphorylation of a conserved Thr in the activation loop (T-loop) sequence (Thr198 in human Calpha; Thr224 in budding yeast Tpk2), installed by auto-phosphorylation or by the 3-phosphoinositide-dependent protein kinase-1 (PDPK1). Certain R2C2 combinations can be localized to particular subcellular regions by their association with diverse species of 'A Kinase-Anchoring Proteins' (AKAPs). The enzyme has been characterized from many organisms. Humans have three C units (Calpha, Cbeta, and Cgamma) encoded by the paralogous genes PRKACA, PRKACB and PRKACG, respectively, and four R subunits (R1alpha, RIbeta, RIIalpha and RIIbeta), encoded by PKRAR1A, PKRAR1B, PKRAR2A and PKRAR2B, respectively. Yeast (Saccharomyces cerevisiae) has three C subunits (Tpk1, Tpk2, and Tpk3) encoded by the paralogous genes TPK1, TPK2 and TPK3, respectively, and a single R subunit (Bcy1) encoded by the BCY1 gene. Some validated substrates of the enzyme include cAMP-response element-binding protein (CREB), phosphorylase kinase alpha subunit (PHKA), and tyrosine 3-monooxygenase (TH) in mammals; Adr1, Whi3, Nej1, and Pyk1 in yeast.
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Bos taurus
UNIPROT: P00517
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The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
hide
ATP
+
a [protein]-(L-serine/L-threonine)
=
ADP
+
a [protein]-(L-serine/L-threonine) phosphate
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
camp-dependent protein kinase, a kinase, cyclic amp-dependent protein kinase, camp-pka, camp/protein kinase a, capk, prkaca, camp dependent protein kinase, camp-dependent pka, cyclic amp-dependent protein kinase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cAMP-dependent protein kinase, alpha-catalytic subunit
-
A kinase
-
-
-
-
ATP:protein phosphotransferase (cAMP-dependent)
-
-
-
-
cAMP-dependent protein kinase
-
-
-
-
cAMP-dependent protein kinase A
-
-
cAMP-dependent protein kinase, beta-1 catalytic subunit
-
cAMP-dependent protein kinase, beta-2-catalytic subunit
-
cPKA
-
catalytic subunit of cAMP-dependent protein kinase
PK-25
-
-
-
-
PKA C-alpha
-
-
-
-
PKA C-beta
-
-
-
-
PKA C-gamma
-
-
-
-
PKA catalytic (C) subunit
-
-
-
-
protein kinase A
type I PKA
-
-
type I protein kinase A
-
-
type II PKA
-
-
type II protein kinase A
-
-
type IIbeta cyclic AMP-dependent protein kinase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
show the reaction diagram
activation mechanism
-
SYSTEMATIC NAME
IUBMB Comments
ATP:protein Ser/Thr-phosphotransferase (3',5'-cAMP-dependent)
This eukaryotic enzyme recognizes the sequence -Arg-Arg-X-Ser*/Thr*-Hpo, where * indicates the phosphorylated residue and Hpo indicates a hydrophobic residue.The inactive holoenzyme is a heterotetramer composed of two regulatory (R) subunits and two catalytic (C) subunits. Each R subunit occludes the active site of a C subunit and contains two binding sites for 3',5'-cyclic-AMP (cAMP). Binding of cAMP activates the enzyme by causing conformational changes that release two free monomeric C subunits from a dimer of the R subunits, i.e. R2C2 + 4 cAMP = R2(cAMP)4 + 2 C. Activity requires phosphorylation of a conserved Thr in the activation loop (T-loop) sequence (Thr198 in human Calpha; Thr224 in budding yeast Tpk2), installed by auto-phosphorylation or by the 3-phosphoinositide-dependent protein kinase-1 (PDPK1). Certain R2C2 combinations can be localized to particular subcellular regions by their association with diverse species of 'A Kinase-Anchoring Proteins' (AKAPs). The enzyme has been characterized from many organisms. Humans have three C units (Calpha, Cbeta, and Cgamma) encoded by the paralogous genes PRKACA, PRKACB and PRKACG, respectively, and four R subunits (R1alpha, RIbeta, RIIalpha and RIIbeta), encoded by PKRAR1A, PKRAR1B, PKRAR2A and PKRAR2B, respectively. Yeast (Saccharomyces cerevisiae) has three C subunits (Tpk1, Tpk2, and Tpk3) encoded by the paralogous genes TPK1, TPK2 and TPK3, respectively, and a single R subunit (Bcy1) encoded by the BCY1 gene. Some validated substrates of the enzyme include cAMP-response element-binding protein (CREB), phosphorylase kinase alpha subunit (PHKA), and tyrosine 3-monooxygenase (TH) in mammals; Adr1, Whi3, Nej1, and Pyk1 in yeast.
CAS REGISTRY NUMBER
COMMENTARY hide
142008-29-5
-
142008-29-5
cAMP-dependent protein kinase
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + BKCa channel ZERO
ADP + phosphorylated BKCa channel ZERO
show the reaction diagram
-
recombinant murine HA-tagged tetrameric protein expressed in HEK-293 cells, phosphorylation at Ser899 activates the channel
-
-
?
ATP + G protein-coupled receptor GRK1
ADP + phosphorylated G protein-coupled receptor GRK1
show the reaction diagram
ATP + G protein-coupled receptor GRK7
ADP + phosphorylated G protein-coupled receptor GRK7
show the reaction diagram
ATP + Kemptide
ADP + Kemptide phosphate
show the reaction diagram
ATP + Kemptide
ADP + phosphorylated Kemptide
show the reaction diagram
-
activity of catalytic PKA subunit
-
-
?
ATP + Leu-Arg-Arg-Ala-Ser-Leu-Gly
ADP + Leu-Arg-Arg-Ala-phospho-Ser-Leu-Gly
show the reaction diagram
-
commercial artificial heptapeptide substrate kemptide
-
-
?
ATP + N-(8-([4-[3-(ethoxycarbonyl)-6,8,8-trimethyl-2-oxo-7,8-dihydro-2H-pyrano[3,2-g]quinolin-9(6H)-yl]butanoyl]amino)octanoyl)-GRTGRRFSYP-amide
ADP + N-(8-([4-[3-(ethoxycarbonyl)-6,8,8-trimethyl-2-oxo-7,8-dihydro-2H-pyrano[3,2-g]quinolin-9(6H)-yl]butanoyl]amino)octanoyl)-GRTGRRFpSYP-amide
show the reaction diagram
-
-
-
-
?
ATP + N-(8-([[7-(diethylamino)-2-oxo-2H-chromen-3-yl]carbonyl]amino)octanoyl)-GRTGRRFSYP-amide
ADP + N-(8-([[7-(diethylamino)-2-oxo-2H-chromen-3-yl]carbonyl]amino)octanoyl)-GRTGRRFpSYP-amide
show the reaction diagram
-
-
-
-
?
ATP + N-(8-[[(11-oxo-2,3,6,7-tetrahydro-1H,5H,11H-pyrano[2,3-f]pyrido[3,2,1-ij]quinolin-10-yl)carbonyl]amino]octanoyl)-GRTGRRFSYP-amide
ADP + N-(8-[[(11-oxo-2,3,6,7-tetrahydro-1H,5H,11H-pyrano[2,3-f]pyrido[3,2,1-ij]quinolin-10-yl)carbonyl]amino]octanoyl)-GRTGRRFpSYP-amide
show the reaction diagram
-
-
-
-
?
ATP + NDUFS-4 protein
ADP + phosphorylated NDUFS-4 protein
show the reaction diagram
-
-
-
-
?
ATP + NF-kappaB p65
ADP + phoshorylated NF-kappaB p65
show the reaction diagram
-
phosphorylation by the catalytic subunit of PKA
-
-
?
ATP + small heat shock-related protein HSP20
ADP + phosphorylated small heat shock-related protein HSP20
show the reaction diagram
-
-
-
-
?
ATP + tyrosine hydroxylase
ADP + phosphorylated tyrosine hydroxylase
show the reaction diagram
-
activity of catalytic PKA subunit
-
-
?
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
ATP + G protein-coupled receptor GRK1
ADP + phosphorylated G protein-coupled receptor GRK1
show the reaction diagram
-
-
-
-
?
ATP + G protein-coupled receptor GRK7
ADP + phosphorylated G protein-coupled receptor GRK7
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
regulation of GRK1 and GRK7 by cAMP level during light and dark phases
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cAMP
dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Ca2+ activates calpain which activates the cAMP-dependent protein kinase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
staurosporine
-
(Rp)-adenosine 3',5'-cyclic monophosphothioate
-
i.e. (Rp)-cAMPS, analogue of cAMP, competitive inhibition of PKA activation by cAMP, binding site structure
(Sp)-adenosine 3',5'-cyclic monophosphothioate
-
i.e. (Sp)-cAMPS, analogue of cAMP, competitive inhibition of PKA activation by cAMP, binding site structure
Acetylsalicylic acid
-
a non-steroidal anti-inflammatory drug, decreases adrenaline- or dibutyryl cAMP-stimulated glycerol release in isolated adipocytes
alsterpaullone
-
21% inhibition of CDK2 at 0.01 mM
H2O2
-
H2O2 inhibits activation of PKA, but inhibition can be reverted with dithiothreitol or with thioredoxin reductase plus thioredoxin, H2O2 is ineffective if the PKA holoenzyme is preincubated with cAMP, if added to the catalytic alpha-subunit, which is active independently of cAMP activation, or if the catalytic alpha-subunit is substituted by ist C199A mutant in the reconstituted holoenzyme
indirubin-3'-monoxime
-
20% inhibition of CDK2 at 0.01 mM
naproxen
-
a non-steroidal anti-inflammatory drug, decreases adrenaline- or dibutyryl cAMP-stimulated glycerol release in isolated adipocytes
nimesulide
-
a non-steroidal anti-inflammatory drug, decreases adrenaline- or dibutyryl cAMP-stimulated glycerol release in isolated adipocytes
piroxicam
-
a non-steroidal anti-inflammatory drug, decreases adrenaline- or dibutyryl cAMP-stimulated glycerol release in isolated adipocytes
PKI
-
-
-
purvalanol
-
18% inhibition of CDK2 at 0.01 mM
roscovitine
-
7% inhibition of CDK2 at 0.01 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-bromo-cAMP
-
0.1 mM
calpain
-
activates the PKA holoenzyme in a cAMP-independent fashion. A variety of agents, including inhibitors of the electron transport chain, activate calpain in a Ca2+-dependent manner, which, in turn, catalyzes the proteolysis of the R subunit, thereby releasing the C subunit in its active form, overview
-
dibutyryl-cAMP
forskolin
-
activation at 0.01 mM
isoproterenol
-
activation at 0.001 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019
N-(8-([4-[3-(ethoxycarbonyl)-6,8,8-trimethyl-2-oxo-7,8-dihydro-2H-pyrano[3,2-g]quinolin-9(6H)-yl]butanoyl]amino)octanoyl)-GRTGRRFSYP-amide
-
pH and temperature not specified in the publication
0.0022
N-(8-([[7-(diethylamino)-2-oxo-2H-chromen-3-yl]carbonyl]amino)octanoyl)-GRTGRRFSYP-amide
-
pH and temperature not specified in the publication
0.0062
N-(8-[[(11-oxo-2,3,6,7-tetrahydro-1H,5H,11H-pyrano[2,3-f]pyrido[3,2,1-ij]quinolin-10-yl)carbonyl]amino]octanoyl)-GRTGRRFSYP-amide
-
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
7.4
-
assay at
7.5
-
assay at
7.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21
-
assay at room temperature
25
-
assay at
30
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme is anchored to a variety of intracellular locations via interaction with A-kinase anchoring proteins
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
PKA activity at the mitochondria is associated with the regulation of apoptosis, mitochondrial respiration, and ATP synthesis. Mitochondrial cAMP-dependent protein kinase is regulted by the protease calpain. Upon exposure of bovine heart mitochondria to digitonin, Ca2+, and a variety of electron transport chain inhibitors, the regulatory subunits of the PKA holoenzyme are digested by calpain, releasing active catalytic subunits. The proteolysis can be attenuated by calpain inhibitor I
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KAPCA_BOVIN
351
0
40620
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
amino acid sequence of the catalytic subunit
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
beta2, the cAMP-dependent protein kinase is a serine/threonine kinase that exists as an inactive tetrameric holoenzyme consisting of two regulatory subunits and two catalytic subunits. It is activated by digestion of the regulatory subunits through calpain releasing the active catalytic ssubunits
tetramer
-
alpha2beta2, the cAMP-dependent protein kinase is a serine/threonine kinase that exists as an inactive tetrameric holoenzyme consisting of two regulatory subunits and two catalytic subunits. It is activated by digestion of the regulatory subunits through calpain
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphate groups at Thr196 and Ser337
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the protein kinase catalytic subunit with staurosporine bound to the adenosine pocket
crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors 1-(5-isoquinolinesulfonyl)-2-methylpiperazine, N-[2-(methylamino)ethyl]-5-isoquinolinesulfonamide and N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide
purified recombinant regulatory subunit deletion mutant RIalpha bound to cAMP analogue ligands (Rp)-cAMPS or (Sp)-cAMPS resulting in (Rp)-RIalpha and (Sp)-RIalpha, hanging drop vapour diffusion method, mixing of 0.002ml protein solution containing 12 mg/ml protein in 50 mM MES, pH 7.5, 0.2 M NaCl, 2 mM EDTA, 2 mM EGTA, and 10 mM DTT, with 0.002 ml reservoir solution containing 1.0 M ammonium sulfate, 12.5% glycerol, 10 mM DTT, 0.1 M sodium acetate, pH 5.5, 22.5°C, 1 week, X-ray diffraction structure determination and analysis at 2.3-2.4 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C199A
-
the mutant of the catalytic alpha-subunit in the holoenzyme leads to insensitivity towards H2O2
D170A
-
site-directed mutagenesis of the regulatory subunit RIalpha, the mutation selectively reduces the negative cooperativity between the cAMP- and C-recognition sites, i.e. the KD for the regulatory-catalytic subunit complex in the presence of cAMP is reduced by more than 12fold, without significantly compromising the high affinity of the regulatory subunit for both binding partners, conformational shifts upon mutation, and physiological implications of the dual functionality of the D170A mutant, overview
I204A
-
site-directed mutagenesis, subunit RIalpha residue mutation, slightly impaired activation of subunit C, mutant show a slightly lower melting temperature compared to the wild-type subunit RIalpha
L203A
-
site-directed mutagenesis, subunit RIalpha residue mutation, slightly impaired activation of subunit C, mutant show a slightly lower melting temperature compared to the wild-type subunit RIalpha
R241A
-
site-directed mutagenesis, subunit RIalpha residue mutation, slightly impaired activation of subunit C, mutant show a slightly lower melting temperature compared to the wild-type subunit RIalpha
Y229A
-
site-directed mutagenesis, subunit RIalpha residue mutation, slightly impaired activation of subunit C, mutant show a slightly lower melting temperature compared to the wild-type subunit RIalpha
additional information
-
generation of a construct RIalpha-(98-381) subunit comprising both cyclic nucleotide binding domains, in the presence and absence of cAMP, mapping the effects of cAMP binding at single residue resolution, NMR study, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant regulatory subunit deletion mutant RIalpha by affinity chromatography, elution with cGMP, and dialysis
-
recombinant wild-type and mutant subunit RIalpha residues 91-244 construct dimers from Escherichia coli strain BL21(DE3) by cAMP affinity chromatography, dialysis, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
distinct expression of catalytic subunit C, regulatory subunit RIalpha, and regulatory subunit RIIbeta in Escherichia coli strain 222
-
expressed in HeLa cells
-
expression of regulatory subunit deletion mutant RIalpha comprising residues 1-91
-
expression of wild-type and mutant subunit RIalpha residues 91-244 constructs, containing the minimal motifs for cAMP-dependent tight binding of subunit C, in Escherichia coli strain BL21(DE3)
-
isolation of a full-length cDNA clone coding for Cbeta2 isoform of the bovine C-subunit
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant catalytic subunit C, regulatory subunit RIalpha, and regulatory subunit RIIbeta from Escherichia coli strain 222 by cAMP-affinity chromatography, gel filtration, and dialysis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bramson, H.N.; Thomas, N.; Matsueda, R.; Nelson, N.C.; Taylor, S.S.; Kaiser, E.T.
Modification of the catalytic subunit of bovine heart cAMP-dependent protein kinase with affinity labels related to peptide substrates
J. Biol. Chem.
257
10575-10581
1982
Bos taurus (P00517), Bos taurus
Manually annotated by BRENDA team
Engh, R.A.; Girod, A.; Kinzel, V.; Huber, R.; Bossemeyer, D.
Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89. Structural implications for selectivity
J. Biol. Chem.
271
26157-26164
1996
Bos taurus (P00517)
Manually annotated by BRENDA team
Prade, L.; Engh, R.A.; Girod, A.; Kinzel, V.; Huber, R.; Bossemeyer, D.
Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential
Structure
5
1627-1637
1997
Bos taurus (P00517)
Manually annotated by BRENDA team
Shoji, S.; Ericsson, L.H.; Walsh, K.A.; Fischer, E.H.; Titani, K.
Amino acid sequence of the catalytic subunit of bovine type II adenosine cyclic 3',5'-phosphate dependent protein kinase
Biochemistry
22
3702-3709
1983
Bos taurus (P00517)
Manually annotated by BRENDA team
Shoji, S.; Parmelee, D.C.; Wade, R.D.; Kumar, S.; Ericsson, L.H.; Walsh, K.A.; Neurath, H.; Long, G.L.; Demaille, J.G.; Fischer, E.H.; Titani, K.
Complete amino acid sequence of the catalytic subunit of bovine cardiac muscle cyclic AMP-dependent protein kinase
Proc. Natl. Acad. Sci. USA
78
848-851
1981
Bos taurus (P00517), Bos taurus
Manually annotated by BRENDA team
Wiemann, S.; Kinzel, V.; Pyerin, W.
Cloning of the C alpha catalytic subunit of the bovine cAMP-dependent protein kinase
Biochim. Biophys. Acta
1171
93-96
1992
Bos taurus (P05131), Bos taurus
Manually annotated by BRENDA team
Showers, M.O.; Maurer, R.A.
A cloned bovine cDNA encodes an alternate form of the catalytic subunit of cAMP-dependent protein kinase
J. Biol. Chem.
261
16288-16291
1986
Bos taurus (P05131), Bos taurus
Manually annotated by BRENDA team
Bain, J.; McLauchlan, H.; Elliott, M.; Cohen, P.
The specificities of protein kinase inhibitors: an update
Biochem. J.
371
199-204
2003
Bos taurus
Manually annotated by BRENDA team
Vigil, D.; Blumenthal, D.K.; Brown, S.; Taylor, S.S.; Trewhella, J.
Differential effects of substrate on type I and type II PKA holoenzyme dissociation
Biochemistry
43
5629-5636
2004
Bos taurus
Manually annotated by BRENDA team
Wu, J.; Jones, J.M.; Nguyen-Huu, X.; Ten Eyck, L.F.; Taylor, S.S.
Crystal structures of RIalpha subunit of cyclic adenosine 5'-monophosphate (cAMP)-dependent protein kinase complexed with (Rp)-adenosine 3',5'-cyclic monophosphothioate and (Sp)-adenosine 3',5'-cyclic monophosphothioate, the phosphothioate analogues of cAMP
Biochemistry
43
6620-6629
2004
Bos taurus
Manually annotated by BRENDA team
Viste, K.; Kopperud, R.K.; Christensen, A.E.; Doskeland, S.O.
Substrate enhances the sensitivity of type I protein kinase a to cAMP
J. Biol. Chem.
280
13279-13284
2005
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Horner, T.J.; Osawa, S.; Schaller, M.D.; Weiss, E.R.
Phosphorylation of GRK1 and GRK7 by cAMP-dependent protein kinase attenuates their enzymatic activities
J. Biol. Chem.
280
28241-28250
2005
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Tian, L.; Coghill, L.S.; McClafferty, H.; MacDonald, S.H.; Antoni, F.A.; Ruth, P.; Knaus, H.G.; Shipston, M.J.
Distinct stoichiometry of BKCa channel tetramer phosphorylation specifies channel activation and inhibition by cAMP-dependent protein kinase
Proc. Natl. Acad. Sci. USA
101
11897-11902
2004
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Vigil, D.; Lin, J.H.; Sotriffer, C.A.; Pennypacker, J.K.; McCammon, J.A.; Taylor, S.S.
A simple electrostatic switch important in the activation of type I protein kinase A by cyclic AMP
Protein Sci.
15
113-121
2006
Bos taurus
Manually annotated by BRENDA team
Zentella de Pina, M.; Vazquez-Meza, H.; Agundis, C.; Pereyra, M.A.; Pardo, J.P.; Villalobos-Molina, R.; Pina, E.
Inhibition of cAMP-dependent protein kinase A: a novel cyclo-oxygenase-independent effect of non-steroidal anti-inflammatory drugs in adipocytes
Auton. Autacoid. Pharmacol.
27
85-92
2007
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Abu-Abed, M.; Das, R.; Wang, L.; Melacini, G.
Definition of an electrostatic relay switch critical for the cAMP-dependent activation of protein kinase A as revealed by the D170A mutant of RIalpha
Proteins
69
112-124
2007
Bos taurus
Manually annotated by BRENDA team
Komalavilas, P.; Penn, R.B.; Flynn, C.R.; Thresher, J.; Lopes, L.B.; Furnish, E.J.; Guo, M.; Pallero, M.A.; Murphy-Ullrich, J.E.; Brophy, C.M.
The small heat shock-related protein, HSP20, is a cAMP-dependent protein kinase substrate that is involved in airway smooth muscle relaxation
Am. J. Physiol. Lung Cell Mol. Physiol.
294
L69-L78
2008
Bos taurus
Manually annotated by BRENDA team
De Rasmo, D.; Panelli, D.; Sardanelli, A.M.; Papa, S.
cAMP-dependent protein kinase regulates the mitochondrial import of the nuclear encoded NDUFS4 subunit of complex I
Cell. Signal.
20
989-997
2008
Bos taurus
Manually annotated by BRENDA team
de Pina, M.Z.; Vazquez-Meza, H.; Pardo, J.P.; Rendon, J.L.; Villalobos-Molina, R.; Riveros-Rosas, H.; Pina, E.
Signaling the signal, cyclic AMP-dependent protein kinase inhibition by insulin-formed H2O2 and reactivation by thioredoxin
J. Biol. Chem.
283
12373-12386
2008
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Grueb, M.; Bartz-Schmidt, K.U.; Rohrbach, J.M.
Adrenergic regulation of cAMP/protein kinase A pathway in corneal epithelium and endothelium
Ophthalmic Res.
40
322-328
2008
Bos taurus
Manually annotated by BRENDA team
Shell, J.R.; Lawrence, D.S.
Proteolytic regulation of the mitochondrial cAMP-dependent protein kinase
Biochemistry
51
2258-2264
2012
Bos taurus
Manually annotated by BRENDA team
Shell, J.R.; Lawrence, D.S.
Probes of the mitochondrial cAMP-dependent protein kinase
Biochim. Biophys. Acta
1834
1359-1363
2013
Bos taurus
Manually annotated by BRENDA team
Byeon, I.J.; Dao, K.K.; Jung, J.; Keen, J.; Leiros, I.; Doskeland, S.O.; Martinez, A.; Gronenborn, A.M.
Allosteric communication between cAMP binding sites in the RI subunit of protein kinase A revealed by NMR
J. Biol. Chem.
285
14062-14070
2010
Bos taurus
Manually annotated by BRENDA team