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Information on EC 3.1.4.53 - 3',5'-cyclic-AMP phosphodiesterase and Organism(s) Homo sapiens and UniProt Accession Q08499

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.4 Phosphoric-diester hydrolases
                3.1.4.53 3',5'-cyclic-AMP phosphodiesterase
IUBMB Comments
Requires Mg2+ or Mn2+ for activity . This enzyme is specific for 3',5'-cAMP and does not hydrolyse other nucleoside 3',5'-cyclic phosphates such as cGMP (cf. EC 3.1.4.17, 3,5-cyclic-nucleotide phosphodiesterase and EC 3.1.4.35, 3,5-cyclic-GMP phosphodiesterase). It is involved in modulation of the levels of cAMP, which is a mediator in the processes of cell transformation and proliferation .
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Homo sapiens
UNIPROT: Q08499
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
pde4b, phosphodiesterase 4, phosphodiesterase-4, camp-phosphodiesterase, camp-specific phosphodiesterase, pde4d3, pde4d5, phosphodiesterase type 4, pde7b, pde7a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cAMP-phosphodiesterase 4D7
-
cAMP-specific phosphodiesterase
-
cAMP-specific phosphodiesterase 4D
-
cAMP-specific phosphodiesterase-4D5
-
cyclic AMP phosphodiesterase type 4
-
PDE4D
phosphodiesterase 4D
-
cAMP phosphodiesterase-4
-
-
cAMP-PDE
-
-
cAMP-phosphodiesterase
-
-
cAMP-phosphodiesterase 1C
-
-
cAMP-specific PDE
-
-
cAMP-specific PDE4D2
-
-
cAMP-specific phosphodiesterase
cAMP-specific phosphodiesterase-4D5
-
-
cAMPspecific PDE
-
-
cyclic AMP phosphodiesterase-4
-
-
cyclic AMP-specific phosphodiesterase
-
-
cyclic nucleotide phosphodiesterase
-
-
cyclic nucleotide phosphodiesterase 4
-
-
cyclic nucleotide phosphodiesterase 4D
-
-
cyclic nucleotide phosphodiesterase-8A
-
high affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
-
hPDE4A
-
-
hPDE4B
-
-
HSPDE4A4B
-
-
PDE-46
-
-
PDE-4D3
-
-
PDE1C
-
-
PDE4A
PDE4A1
isoform
PDE4A10
-
-
PDE4A4
-
isoform
PDE4B
PDE4B2
-
isoform
PDE4C
PDE4C2
-
isoform
PDE4D3
-
isoform
PDE4D5
-
-
PDE7A
PDE7A2
isoform
PDE7B
PDE8
-
-
PDE8A
PDE8A1
PDE8A catalytic domain
phosphodiesterase 4
-
-
phosphodiesterase 4 isoform A8
-
phosphodiesterase 4B
-
-
phosphodiesterase 7
-
-
phosphodiesterase 7B
-
isoform
phosphodiesterase type 4
-
-
phosphodiesterase type 5
-
-
phosphodiesterase-4
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
adenosine 3',5'-cyclic phosphate + H2O = AMP
show the reaction diagram
catalytic reaction mechanism, overview
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
3',5'-cyclic-AMP 5'-nucleotidohydrolase
Requires Mg2+ or Mn2+ for activity [2]. This enzyme is specific for 3',5'-cAMP and does not hydrolyse other nucleoside 3',5'-cyclic phosphates such as cGMP (cf. EC 3.1.4.17, 3,5-cyclic-nucleotide phosphodiesterase and EC 3.1.4.35, 3,5-cyclic-GMP phosphodiesterase). It is involved in modulation of the levels of cAMP, which is a mediator in the processes of cell transformation and proliferation [3].
CAS REGISTRY NUMBER
COMMENTARY hide
9036-21-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3',5'-cAMP + H2O
5'-AMP
show the reaction diagram
cAMP + H2O
5'-AMP
show the reaction diagram
-
-
-
?
cGMP + H2O
5'-GMP
show the reaction diagram
-
-
-
?
3',5'-cAMP + H2O
5'-AMP
show the reaction diagram
3',5'-cGMP + H2O
5'-GMP
show the reaction diagram
adenosine 3',5'-cyclic phosphate + H2O
adenosine 5'-phosphate
show the reaction diagram
cAMP + H2O
5'-AMP
show the reaction diagram
-
-
-
?
cAMP + H2O
AMP
show the reaction diagram
-
-
-
?
cGMP + H2O
5'-GMP
show the reaction diagram
-
-
-
?
guanosine 3',5'-cyclic phosphate + H2O
guanosine 5'-phosphate
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
3',5'-cAMP + H2O
5'-AMP
show the reaction diagram
-
-
-
?
3',5'-cAMP + H2O
5'-AMP
show the reaction diagram
-
-
-
-
?
adenosine 3',5'-cyclic phosphate + H2O
adenosine 5'-phosphate
show the reaction diagram
-
determination of reaction rate and mechanism using computational modeling, quantum mechanical/molecular mechanical-free energy perturbation, QM/MM-FE, and QM/MM-Poisson-Boltzmann surface area, PBSA, calculations. The onQM/MMreaction-coordinate calculations including the protein environment of any PDE-catalyzed reaction system identifies a unique catalytic reaction mechanism, overview
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
required
Mn2+
the enzyme requires the presence of at least 1 mM Mn2+ or Mg2+ for maximal activity in vitro
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-[(2-chloro-4-nitrophenyl)thio]-pyridine
-
4-[8-(3-nitrophenyl)-[1,7]naphthyridin-6-yl]benzoic acid
i.e. NVP
N-[2-(5-chloro-2-nitrophenylthio)phenyl]acetamide
10% inhibition at 0.01 mM
rolipram
PDE4 is specifically inhibited by rolipram
(2R,3R)-3-(6-amino-9H-purin-9-yl)nonan-2-ol
-
IC50: 0.31 mM, PDE4
(2Z)-9,10-dimethoxy-3-methyl-2-[(2,4,6-trimethylphenyl)imino]-2,3,6,7-tetrahydro-4H-pyrimido[6,1-a]isoquinolin-4-one
-
IC50: 0.00043 mM, PDE4
(4aS,8aR)-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
(R)-rolipram
-
3-(1-methyl-7-oxo-3-propyl-4,7-dihydro-1H-pyrazolo[4,3-d]pyrimidin-5-yl)-N-[2-(1-methylpyrrolidin-2-yl)ethyl]-4-propoxybenzenesulfonamide
-
-
3-(6-aminopurin-9-yl)nonan-2-ol hydrochloride
-
3-isobutyl-1-methyl-xanthine
-
-
3-isobutyl-1-methylxanthine
3-isobuytl-1-methylxanthine
-
4-[(2-chloro-4-nitrophenyl)thio]-pyridine
-
4-[8-(3-nitrophenyl)-[1,7]naphthyridin-6-yl]benzoic acid
i.e. NVP
6-(3,4-dimethoxyphenyl)-2-[4-(morpholinomethyl)benzyl]-4,5-dihydropyridazin-3(2H)-one
-
-
apigenin
-
-
apigenin-7-O-glucoside
-
-
apremilast
-
CC-10004, i.e. (S)-N-[2-[1-(3-ethoxy-4-methoxyphenyl)-2-methanesulfonylethyl]-1,3-dioxo-2,3-dihydro-1H-isoindol-4-yl]acetamide, oral phosphodiesterase-4 inhibitor, apremilast shows no marked selectivity among PDE4 isozymes
ASP9831
-
-
-
avanafil
-
-
AWD 12-250
-
-
AWD12-281
-
-
BRL-50481
-
PDE7 inhibitor
Caffeine
-
-
cAMP-N1-oxide
-
-
cGMP
-
5% inhibition at 0.1 mM
chamomile
-
inhibits cAMP-PDE activity
cilomilast
Cilostamide
-
IC50: 0.099 mM, PDE4
cis-(+)-4-(3,4-dimethoxyphenyl)-2-[4-(morpholinomethyl)benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-(+)-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-(+/-)-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-(-)-4-(3,4-dimethoxyphenyl)-2-[4-(morpholinomethyl)benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-(-)-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-2-[(E)-4-(1H-imidazol-1-yl)but-2-enyl]-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-2-[2-[2-(1H-imidazol-1-yl)ethoxy]ethyl]-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-2-[4-(1,4-dioxa-8-azaspiro[4.5]decan-8-ylmethyl)-benzyl]-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-2-[4-[(1H-imidazol-1-yl)methyl]benzyl]-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-4-(3,4-dimethoxyphenyl)-2-[2-(morpholinomethyl)benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-4-(3,4-dimethoxyphenyl)-2-[3-(morpholinomethyl)benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-4-(3,4-dimethoxyphenyl)-2-[4-(morpholinomethyl)benzyl]-4a,5,6,7,8,8a-hexahydrophthalazin-1(2H)-one
-
-
cis-4-(3,4-dimethoxyphenyl)-2-[4-(morpholinomethyl)benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-4-(3,4-dimethoxyphenyl)-2-[4-(piperidin-1-ylmethyl)benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-4-(3,4-dimethoxyphenyl)-2-[4-[(4-methylpiperazin-1-yl)methyl]benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-4-(3,4-dimethoxyphenyl)-2-[4-[(4-oxopiperidin-1-yl)-methyl]benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-4-(3,4-dimethoxyphenyl)-2-[4-[(dimethylamino)-methyl]benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
-
-
cis-5-(3,4-dimethoxyphenyl)-3-[4-(morpholinomethyl)benzyl]-3,4-diazabicyclo[4.1.0]hept-4-en-2-one
-
-
cis-5-(3,4-dimethoxyphenyl)-3-[4-(morpholinomethyl)benzyl]-3,4-diazabicyclo[4.2.0]oct-4-en-2-one hydrochloride
-
-
D-22888
-
-
denbufylline
-
dipyridamole
dipyridimole
-
E4021
-
-
erythro-9-(2-hydroxy-3-nonyl)adenine
-
7.4% inhibition at 0.1 mM
erythro-9-[3-(2-hydroxynonyl)]adenine
-
0.1 mM, 12% inhibition, wild-type enzyme
etazolate
-
ethyl 2-([4-(3-carbamoylpiperazin-1-yl)-6-[4-(dimethylamino)piperidin-1-yl]pyrimidin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
-
-
ethyl 2-([4-[(3,4-dimethoxybenzyl)amino]-6-(piperazin-1-yl)pyrimidin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
-
-
ethyl 2-([4-[4-(dimethylamino)piperidin-1-yl]-6-(4-hydroxypiperidin-1-yl)pyrimidin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
-
-
ethyl 2-([4-[4-(dimethylamino)piperidin-1-yl]-6-(4-methylpiperazin-1-yl)pyrimidin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
-
-
ethyl 2-([4-[4-(dimethylamino)piperidin-1-yl]-6-(morpholin-4-yl)pyrimidin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
-
-
ethyl 2-([4-[4-(dimethylamino)piperidin-1-yl]-6-[3-(hydroxymethyl)piperidin-1-yl]pyrimidin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
-
-
ethyl 2-([7-ethyl-6-[(4-sulfamoylbenzyl)amino]-7H-purin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
-
-
ethyl 2-[[4,6-bis(4-hydroxypiperidin-1-yl)pyrimidin-2-yl]amino]-4-methyl-1,3-thiazole-5-carboxylate
-
-
ethyl 2-[[4-[4-[2-(dimethylamino)ethyl]piperazin-1-yl]-6-(4-methylpiperazin-1-yl)pyrimidin-2-yl]amino]-4-methyl-1,3-thiazole-5-carboxylate
-
-
ethyl 3,5-dimethyl-1-phenyl-1H-pyrazole-4-carboxylate
ethyl 3,5-dimethyl-1-quinolin-8-yl-1H-pyrazole-4-carboxylate
ethyl 3,5-dimethyl-1H-pyrazole-4-carboxylate
ethyl 3-(4-chlorophenyl)-1-phenyl-1H-pyrazole-4-carboxylate
ethyl 3-methyl-5-(4-methylphenyl)-1H-pyrazole-4-carboxylate
ethyl 4-methyl-2-([4-(4-methylpiperazin-1-yl)-6-[methyl(3,4,5-trimethoxybenzyl)amino]pyrimidin-2-yl]amino)-1,3-thiazole-5-carboxylate
-
-
ethyl 4-methyl-2-([4-(methylamino)-6-[(4-sulfamoylbenzyl)amino]pyrimidin-2-yl]amino)-1,3-thiazole-5-carboxylate
-
-
ethyl 4-methyl-2-([4-(piperazin-1-yl)-6-[(4-sulfamoylbenzyl)amino]pyrimidin-2-yl]amino)-1,3-thiazole-5-carboxylate
-
-
ethyl 4-methyl-2-([4-[(4-sulfamoylbenzyl)amino]pyrimidin-2-yl]amino)-1,3-thiazole-5-carboxylate
-
-
ethyl 4-methyl-2-([4-[methyl(3,4,5-trimethoxybenzyl)amino]-6-(piperazin-1-yl)pyrimidin-2-yl]amino)-1,3-thiazole-5-carboxylate
-
-
ethyl 4-methyl-2-[[4-(piperazin-1-yl)-7-(3,4,5-trimethoxybenzyl)-6,7-dihydro-5H-pyrrolo[2,3-d]pyrimidin-2-yl]amino]-1,3-thiazole-5-carboxylate
-
-
ethyl 5-amino-1-(4a,5,6,7,8,9a-hexahydro[1]benzothieno[2,3-d]pyrimidin-4-yl)-1H-pyrazole-4-carboxylate
hyperoside
-
-
IC86340
-
-
-
IR-202
-
PDE7 inhibitor
IR-284
-
dual PDE4/PDE7 inhibitor
LAS-31025
-
-
lodenafil
-
-
luteolin
-
-
luteolin-7-O-glucoside
-
-
Milrinone
mirodenafil
-
-
N-[2-(5-chloro-2-nitrophenylthio)phenyl]acetamide
N-[3-(1H-imidazol-1-yl)propyl]-2-[cis-4-(3,4-dimethoxyphenyl)-1-oxo-4a,5,8,8a-tetrahydrophthalazin-2(1H)-yl]acetamide
-
-
N6-Monobutyryl-cAMP
-
-
N6-monobutyyl-cAMP
-
-
papaverine
-
patuletin-7-O-glucoside
-
-
pentoxifylline
-
-
quazinone
-
0.1 mM, 26% inhibition, wild-type enzyme
quinazolinamine
-
IC50: 0.34 mM, PDE4
R-rolipram
-
-
resveratrol
-
-
Ro-20-1724
-
inhibition of PDE4, resulting in increased intacelular cAMP
Ro20-1724
roflumilast
rolipram
RP-73401
-
IC50: 0.0000016 mM, PDE4
RPR-73401
-
-
RS-25344
-
phosphorylation of PDE-4D3 increases the sensitivity of the enzyme to inhibition by RS-25344 about 100fold
RS-33793
-
phosphorylation of PDE-4D3 increases the sensitivity of the enzyme to inhibition by RS-33793 about 330fold
SCH51866
-
-
sildenafil
tadalafil
theophylline
vardenafil
vinpocetine
zaprinast
zardaverine
Zn2+
-
more than 90% inhibition at 0.05 mM Zn2+ in the presence of 0.1 mM EDTA, inhibition can be greatly relieved with EDTA at 0.30 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
EDTA at 0.10 mM slightly activates PDE4
isoproterenol
-
0.001 mM isoproterenol triggers a sustained, 2fold increase in PDE4 activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0015
cAMP
pH 7.5, 25°C
0.427
cGMP
pH 7.5, 25°C
0.0007 - 0.0088
3',5'-cAMP
1.6
3',5'-cGMP
wild type PDE8A1 catalytic domain, in 20 mM Tris-HCl, pH 7.5, 4 mM MnCl2, at 24°C
0.000055 - 0.0244
adenosine 3',5'-cyclic phosphate
0.0001 - 0.0058
cAMP
0.24
cGMP
pH 7.5, 25°C
0.124
guanosine 3',5'-cyclic phosphate
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.4
cAMP
pH 7.5, 25°C
1.19
cGMP
pH 7.5, 25°C
4 - 4.3
3',5'-cAMP
1.6
3',5'-cGMP
wild type PDE8A1 catalytic domain, in 20 mM Tris-HCl, pH 7.5, 4 mM MnCl2, at 24°C
0.3 - 6.7
cAMP
0.48
cGMP
pH 7.5, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000085
(R)-rolipram
-
0.000068
apremilast
-
PDE4 purified from U-937 cells, using 0.001 mM cAMP as substrate, pH and temperature not specified in the publication
0.000114
cilomilast
30°C
0.00025 - 0.00038
R-rolipram
0.000037 - 0.0016
rolipram
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0073
4-[(2-chloro-4-nitrophenyl)thio]-pyridine
Homo sapiens
pH not specified in the publication, 30°C
0.00057
4-[8-(3-nitrophenyl)-[1,7]naphthyridin-6-yl]benzoic acid
Homo sapiens
pH 7.5, 25°C
0.31
(2R,3R)-3-(6-amino-9H-purin-9-yl)nonan-2-ol
Homo sapiens
-
IC50: 0.31 mM, PDE4
0.00043
(2Z)-9,10-dimethoxy-3-methyl-2-[(2,4,6-trimethylphenyl)imino]-2,3,6,7-tetrahydro-4H-pyrimido[6,1-a]isoquinolin-4-one
Homo sapiens
-
IC50: 0.00043 mM, PDE4
0.000085
(4aS,8aR)-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0322 - 0.175
3-isobutyl-1-methyl-xanthine
0.00737 - 0.698
3-isobutyl-1-methylxanthine
0.0059
3-isobuytl-1-methylxanthine
Homo sapiens
-
0.00018 - 0.0066
4-[(2-chloro-4-nitrophenyl)thio]-pyridine
0.00065 - 0.0057
4-[8-(3-nitrophenyl)-[1,7]naphthyridin-6-yl]benzoic acid
0.0041
apigenin
Homo sapiens
-
-
0.0102
apigenin-7-O-glucoside
Homo sapiens
-
-
0.00002 - 0.000074
apremilast
0.0004 - 0.0097
AWD 12-250
0.000015 - 0.0205
AWD12-281
0.0002
BRL-50481
Homo sapiens
-
pH and temperature not specified in the publication
2.401 - 2.91
cAMP-N1-oxide
0.000101
cilomilast
Homo sapiens
-
0.099
Cilostamide
Homo sapiens
-
IC50: 0.099 mM, PDE4
0.0000003
cis-(+)-4-(3,4-dimethoxyphenyl)-2-[4-(morpholinomethyl)benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000088
cis-(-)-4-(3,4-dimethoxyphenyl)-2-[4-(morpholinomethyl)benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000004
cis-2-[(E)-4-(1H-imidazol-1-yl)but-2-enyl]-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000052
cis-2-[2-[2-(1H-imidazol-1-yl)ethoxy]ethyl]-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000013
cis-2-[4-(1,4-dioxa-8-azaspiro[4.5]decan-8-ylmethyl)-benzyl]-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000007
cis-2-[4-[(1H-imidazol-1-yl)methyl]benzyl]-4-(3,4-dimethoxyphenyl)-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000013
cis-4-(3,4-dimethoxyphenyl)-2-[2-(morpholinomethyl)benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000014
cis-4-(3,4-dimethoxyphenyl)-2-[3-(morpholinomethyl)benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.000001
cis-4-(3,4-dimethoxyphenyl)-2-[4-(morpholinomethyl)benzyl]-4a,5,6,7,8,8a-hexahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000009
cis-4-(3,4-dimethoxyphenyl)-2-[4-(morpholinomethyl)benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000082
cis-4-(3,4-dimethoxyphenyl)-2-[4-(piperidin-1-ylmethyl)benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.000002
cis-4-(3,4-dimethoxyphenyl)-2-[4-[(4-methylpiperazin-1-yl)methyl]benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000009
cis-4-(3,4-dimethoxyphenyl)-2-[4-[(4-oxopiperidin-1-yl)-methyl]benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000097
cis-4-(3,4-dimethoxyphenyl)-2-[4-[(dimethylamino)-methyl]benzyl]-4a,5,8,8a-tetrahydrophthalazin-1(2H)-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000459
cis-5-(3,4-dimethoxyphenyl)-3-[4-(morpholinomethyl)benzyl]-3,4-diazabicyclo[4.1.0]hept-4-en-2-one
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.0000164
cis-5-(3,4-dimethoxyphenyl)-3-[4-(morpholinomethyl)benzyl]-3,4-diazabicyclo[4.2.0]oct-4-en-2-one hydrochloride
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.00008 - 0.0048
D-22888
0.0005
denbufylline
Homo sapiens
-
0.0011 - 0.00194
dipyridamole
0.009
dipyridimole
Homo sapiens
-
0.015
E4021
Homo sapiens
-
-
0.000082
ethyl 2-([4-(3-carbamoylpiperazin-1-yl)-6-[4-(dimethylamino)piperidin-1-yl]pyrimidin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.000031
ethyl 2-([4-[(3,4-dimethoxybenzyl)amino]-6-(piperazin-1-yl)pyrimidin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.000076
ethyl 2-([4-[4-(dimethylamino)piperidin-1-yl]-6-(4-hydroxypiperidin-1-yl)pyrimidin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.000083
ethyl 2-([4-[4-(dimethylamino)piperidin-1-yl]-6-(4-methylpiperazin-1-yl)pyrimidin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00013
ethyl 2-([4-[4-(dimethylamino)piperidin-1-yl]-6-(morpholin-4-yl)pyrimidin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00012
ethyl 2-([4-[4-(dimethylamino)piperidin-1-yl]-6-[3-(hydroxymethyl)piperidin-1-yl]pyrimidin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00001
ethyl 2-([7-ethyl-6-[(4-sulfamoylbenzyl)amino]-7H-purin-2-yl]amino)-4-methyl-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.000063
ethyl 2-[[4,6-bis(4-hydroxypiperidin-1-yl)pyrimidin-2-yl]amino]-4-methyl-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.000056
ethyl 2-[[4-[4-[2-(dimethylamino)ethyl]piperazin-1-yl]-6-(4-methylpiperazin-1-yl)pyrimidin-2-yl]amino]-4-methyl-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00027 - 0.00031
ethyl 3,5-dimethyl-1-phenyl-1H-pyrazole-4-carboxylate
0.017 - 0.019
ethyl 3,5-dimethyl-1-quinolin-8-yl-1H-pyrazole-4-carboxylate
0.015 - 0.019
ethyl 3,5-dimethyl-1H-pyrazole-4-carboxylate
0.00088 - 0.0015
ethyl 3-(4-chlorophenyl)-1-phenyl-1H-pyrazole-4-carboxylate
0.06 - 0.082
ethyl 3-methyl-5-(4-methylphenyl)-1H-pyrazole-4-carboxylate
0.000039
ethyl 4-methyl-2-([4-(4-methylpiperazin-1-yl)-6-[methyl(3,4,5-trimethoxybenzyl)amino]pyrimidin-2-yl]amino)-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.0001
ethyl 4-methyl-2-([4-(methylamino)-6-[(4-sulfamoylbenzyl)amino]pyrimidin-2-yl]amino)-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00001
ethyl 4-methyl-2-([4-(piperazin-1-yl)-6-[(4-sulfamoylbenzyl)amino]pyrimidin-2-yl]amino)-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00022
ethyl 4-methyl-2-([4-[(4-sulfamoylbenzyl)amino]pyrimidin-2-yl]amino)-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00001
ethyl 4-methyl-2-([4-[methyl(3,4,5-trimethoxybenzyl)amino]-6-(piperazin-1-yl)pyrimidin-2-yl]amino)-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.000006
ethyl 4-methyl-2-[[4-(piperazin-1-yl)-7-(3,4,5-trimethoxybenzyl)-6,7-dihydro-5H-pyrrolo[2,3-d]pyrimidin-2-yl]amino]-1,3-thiazole-5-carboxylate
Homo sapiens
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.025 - 0.05
ethyl 5-amino-1-(4a,5,6,7,8,9a-hexahydro[1]benzothieno[2,3-d]pyrimidin-4-yl)-1H-pyrazole-4-carboxylate
0.0118
hyperoside
Homo sapiens
-
-
0.000085
IR-202
Homo sapiens
-
pH and temperature not specified in the publication
0.00421 - 0.00728
LAS-31025
0.0013
luteolin
Homo sapiens
-
-
0.0149
luteolin-7-O-glucoside
Homo sapiens
-
-
0.0033 - 0.00635
Milrinone
0.0021
N-[2-(5-chloro-2-nitrophenylthio)phenyl]acetamide
Homo sapiens
pH not specified in the publication, 30°C
0.0000143
N-[3-(1H-imidazol-1-yl)propyl]-2-[cis-4-(3,4-dimethoxyphenyl)-1-oxo-4a,5,8,8a-tetrahydrophthalazin-2(1H)-yl]acetamide
Homo sapiens
-
in Tris-HCl (pH 7.6), 100 mM NaCl, 150 mM MgCl2, and 0.5% (w/v) polyethylene glycol 6000, at 30°C
0.561 - 1.13
N6-monobutyyl-cAMP
0.0149
patuletin-7-O-glucoside
Homo sapiens
-
-
0.34
quinazolinamine
Homo sapiens
-
IC50: 0.34 mM, PDE4
0.000042 - 0.0022
Ro20-1724
0.00001 - 0.18
rolipram
0.0000016
RP-73401
Homo sapiens
-
IC50: 0.0000016 mM, PDE4
0.000001 - 0.0178
RPR-73401
0.000113
SB 207499
Homo sapiens
-
0.000105
SCH 351591
Homo sapiens
-
0.0015
SCH51866
Homo sapiens
-
PDE7B expressed in transfected COS-7 cells
0.00319 - 0.0861
sildenafil
0.01
tadalafil
Homo sapiens
-
IC50: above 10000 nM, PDE4
0.002055 - 0.0046
vardenafil
0.059
vinpocetine
Homo sapiens
-
-
0.0525
zaprinast
Homo sapiens
-
mutant enzyme D440N
0.01
additional information
Homo sapiens
-
IC 50 for sildenafil and tadalafil is above 10000 nM, PDE7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the level of PDE4D transcripts in gsp+ tumors is significantly higher than that found in gsp- adenomas
Manually annotated by BRENDA team
numerous PDE4D gene-derived variants including PDE4D3, PDE4D5, PDE4D7, PDE4D8, and PDE4D9
Manually annotated by BRENDA team
-
lung epithelial cell
Manually annotated by BRENDA team
-
carcinoma of salivary gland
Manually annotated by BRENDA team
-
phosphodiesterase 4 is detected in smooth muscle cells of the wall, and in the cytoplasm of luminal endothelial cells of cavernous arteries
Manually annotated by BRENDA team
-
presence of isoform PDE4 in nonvascular smooth musculature of the corpus carnosum
Manually annotated by BRENDA team
-
sinusoidal endothelial and subendothelialn layer of clitoris, presence of isoform PDE4
Manually annotated by BRENDA team
-
human middle ear epithelial cell
Manually annotated by BRENDA team
-
PDE4
Manually annotated by BRENDA team
-
gingiva-derived malignant melanoma cell, expression of variants PDE4B and PDE4D
Manually annotated by BRENDA team
-
monocytic cells may express different PDE4 isozymes, depending on their state of activation or differentiation. These isozymes could thus regulate intracellular cAMP levels at various stages of monocyte activation and could thereby be important in limiting the inflammatory response
Manually annotated by BRENDA team
-
human bronchial epithelial cell
Manually annotated by BRENDA team
-
cultured, PDE7
Manually annotated by BRENDA team
-
abundantly present in the fibromusclular stroma as well as in glandular structures of the transition zone
Manually annotated by BRENDA team
-
carcinoma of salivary gland
Manually annotated by BRENDA team
-
PDE4
Manually annotated by BRENDA team
-
PDE7
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
of luminal endothelial cells of cavernous arteries
Manually annotated by BRENDA team
small part of enzyme is associated with the plasma membrane
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
isoform PDE4D7 is important in prostate cancer progression and ischemic stroke
malfunction
metabolism
physiological function
additional information
-
PDE4 is a cAMP-specific PDE which has four subfamilies, A thru D, that include over 50 isoforms
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PDE4D_HUMAN
809
0
91115
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
125000
x * 125000, SDS-PAGE, recombinant protein
38800
-
x * 39000, SDS-PAGE, x * 38800, deduced from gene sequence, both N-terminally truncated enzyme
39000
-
x * 39000, SDS-PAGE, x * 38800, deduced from gene sequence, both N-terminally truncated enzyme
58000
x * 58000, SDS-PAGE of isoform PDE4B5
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
the enzyme is phosphorylated and activated by protein kinase A within upstream conserved region 1 and inhibited by phosphorylation at serine 42 within the N-terminal region
phosphoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitor 4-[8-(3-nitrophenyl)-[1,7]naphthyridin-6-yl]benzoic acid, comparison with isoforms PDE4A, PDE4B, PDE4C. Inhibitor binds in the same conformation to the deep cAMP substrate pocket and interacts with the same residues in each instance. Detailed structural comparison
catalytic domain of inactive mutant D201N in complex with substrate cAMP at 1.56 A resolution. Q369 forms only one hydrogen bond ith the adenine of cAMP. Structural comparison between isoform PDE4D2-cAMP and PDE10A2-cAMP shows an anti configuration of cAMP in PDE4, but syn in PDE10
-
hanging drop method, PDE4D2 in complex with the nonselective inhibitor 3-isobutyl-1-methylxanthine
-
hanging-drop vapor-diffusion method, crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP (2.0 A), 8-Br-AMP (2.13 A), and rolipram (2.0 A)
-
in complex with inhibitor 4-[8-(3-nitrophenyl)-[1,7]naphthyridin-6-yl]benzoic acid, comparison with isoforms PDE4A, PDE4C, PDE4D. Inhibitor binds in the same conformation to the deep cAMP substrate pocket and interacts with the same resiudues in each instance. Detailed structural comparison
in complex with inhibitor 4-[8-(3-nitrophenyl)-[1,7]naphthyridin-6-yl]benzoic acid, comparison with isoforms PDE4B, PDE4C, PDE4D. Inhibitor binds in the same conformation to the deep cAMP substrate pocket and interacts with the same residues in each instance. Detailed structural comparison
molecular dynamics simulations. The second bridging ligand in the active site is HO- rather than H2O, serving as a nucleophile to initialize the catalytic hydrolysis of cAMP
-
NMR and CD analysis of the N-terminal 38mer peptide of isoform PDE4D5 which contains the entire signaling scaffold protein RACK1 interaction domain together with a portion of the beta-arrestin binding site. The peptiode has a distinct amphipathic helical structure. Study on binding to RACK1 and to beta-arrestin
unliganded PDE8A1 and in complex with 3-isobuytl-1-methylxanthine, hanging drop vapour diffusion method, using 100 mM sodium cacodylate (pH 6.5), 15% 2-propanol, 30% ethylene glycol, and 8-10% PEG3350 at 4°C
unliganded, detailed structural comparison with isoforms PDE4A, PDE4B, PDE4C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S42A
the mutant with 170% activity compared to the wild type enzyme is not phosphorylated at serine 42
S42D
the mutant with increased activity compared to the wild type enzyme is not phosphorylated at serine 42
A590C
-
mutation has no significant influence on substrate affinity or specificity
D440A
-
unlike wild type enzyme, the mutant enzyme shows activity with cGMP
D440N
-
unlike wild type enzyme, the mutant enzyme shows activity with cGMP
F484Y
-
mutation has no significant influence on substrate affinity or specificity
H305P
the mutation is associated with micronodular adrenocortical disease
L391A
-
mutation has no significant influence on substrate affinity or specificity
P595I
-
mutation leads to 7fold decrease of substrate affinity and an 14fold decrease of the affinity towards the PDE4-specific inhibitor rolipram
T748F
the mutation increases the PDE8A1 sensitivity to several nonselective or family selective PDE inhibitors, the catalytic efficiency of the mutant is about 2fold better than that of the wild type PDE8A1
V501A
-
mutation has no significant influence on substrate affinity or specificity
W375Q
-
mutation abolishes catalytic activity
W605I
-
mutation abolishes catalytic activity
W605V
-
mutation abolishes catalytic activity
W605Y
-
mutation abolishes catalytic activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
soluble HSPDE4A10 is more thermostable (T0.5: 11 min) than the particulate enzyme (T0.5: 5 min)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose column chromatography, and Superdex 200 gel filtration
ammonium sulfate fractionation and amylose-resin column chromatography
-
from inclusion bodies
-
gel filtration
-
Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
expression in Escherichia coli as N-terminal glutathione S-transferase-fusion protein
cloned and expressed in Sf9 cells with recombinant baculovirus infection
-
Epac1-camps-PDE4A1 fusion protein is expressed in HEK-293 cells
expressed in COS1 cells
-
expressed in Escherichia coli strain BL21
expressed in transfected COS7 cells. The human PDE4A species, h6.1 (HSPDE4A4C), which lacks the N-terminal extension of PDE-46, is an entirely soluble species when expressed in COS7 cells
-
expression in baculovirus transfected Sf9 cells
expression in COS-7 cell
expression in Sf9 insect cells
expression in Spodoptera frugiperda
-
expression of the catalytic domain in Escherichia coli
-
recombinant PDE7B expressed in transfected COS-7 cells
-
the catalytic domain of human PDE4D is cloned from HL-60 cells and expressed in Escherichia coli JM109 cells
-
transient expression of the engineered human PDE4A10 open reading frame in COS7 cells allows detection of a 121000 Da protein in both soluble and particulate fractions. PDE4A10 is localized primarily to the perinuclear region of COS7 cells
-
When expressed in COS-7 cells, PDE4A8 localizes predominantly in the cytosol, but 20% of the enzyme was associated with membrane fractions
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform PDE4D7 doubles in activity after forskolin treatment
p53 inactivates isoform PDE4D by inducing the expression of miR-139-5p which directly binds to the target sequence at 3'-UTR of PDE4D mRNA
2fold increased PDE7B mRNA expression in chronic lymphocytic leukemia correlates with a 10fold higher expression of PDE7B protein and results in an increased contribution of PDE7 to total PDE activity
-
isoform PDE1C expression is highly induced in neointimal smooth muscle cells of human coronary arteries
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
refolding is initiated by addition of 0.03 mg/ml protein to a buffer of 0.5 M Tris-HCl pH 7.0, 20 mM MgCl2, 20 mM MnCl2, 0.020 mM ZnSO4, 0.7 M arginine, 30% glycerol, 10 mM NaCl, 1 mM KCl, and 10 mM dithiothreitol, at 4°C for three days
refolding to active enzyme from inclusion bodies requires high concentrations of arginine hydrochloride, ethylene glycol, and magnesium chloride at pH 8.5
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
development of cell-permeable peptide reagents based upon the N-terminal region of PDE4D5 that allow for the selective disruption of PDE4D5 targeting to specific signalling scaffolds, namely beta-arrestin and RACK1
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
O'Grady, S.M.; Jiang, X.; Maniak, P.J.; Birmachu, W.; Scribner, L.R.; Bulbulian, B.; Gullikson, G.W.
Cyclic AMP-dependent Cl secretion is regulated by multiple phosphodiesterase subtypes in human colonic epithelial cells
J. Membr. Biol.
185
137-144
2002
Homo sapiens
Manually annotated by BRENDA team
Richter, W.; Hermsdorf, T.; Kronbach, T.; Dettmer, D.
Refolding and Purification of Recombinant Human PDE7A: Expressed in Escherichia coli as Inclusion Bodies
Protein Expr. Purif.
25
138-148
2002
Homo sapiens
Manually annotated by BRENDA team
Ahlstrom, M.; Pekkinen, M.; Huttunen, M.; Lamberg-Allardt, C.
Cyclic nucleotide phosphodiesterases (PDEs) in human osteoblastic cells; the effect of PDE inhibition on cAMP accumulation
Cell. Mol. Biol. Lett.
10
305-319
2005
Homo sapiens
Manually annotated by BRENDA team
Bischoff, E.
Potency, selectivity, and consequences of nonselectivity of PDE inhibition
Int. J. Impot. Res.
16
S11-S14
2004
Homo sapiens
Manually annotated by BRENDA team
Huai, Q.; Liu, Y.; Francis, S.H.; Corbin, J.D.; Ke, H.
Crystal structures of phosphodiesterases 4 and 5 in complex with inhibitor 3-isobutyl-1-methylxanthine suggest a conformation determinant of inhibitor selectivity
J. Biol. Chem.
279
13095-13101
2004
Homo sapiens
Manually annotated by BRENDA team
Xu, R.X.; Rocque, W.J.; Lambert, M.H.; Vanderwall, D.E.; Luther, M.A.; Nolte, R.T.
Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram
J. Mol. Biol.
337
355-365
2004
Homo sapiens
Manually annotated by BRENDA team
Card, G.L.; Blasdel, L.; England, B.P.; Zhang, C.; Suzuki, Y.; Gillette, S.; Fong, D.; Ibrahim, P.N.; Artis, D.R.; Bollag, G.; Milburn, M.V.; Kim, S.H.; Schlessinger, J.; Zhang, K.Y.
A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design
Nat. Biotechnol.
23
201-207
2005
Homo sapiens
Manually annotated by BRENDA team
Oelke, M.; Hedlund, P.; Albrecht, K.; Ellinghaus, P.; Stief, C.G.; Jonas, U.; Andersson, K.E.; Uckert, S.
Expression of cAMP and cGMP-phosphodiesterase isoenzymes 3, 4, and 5 in the human clitoris: immunohistochemical and molecular biology study
Urology
67
1111-1116
2006
Homo sapiens
Manually annotated by BRENDA team
Waldkirch, E.; Uckert, S.; Yildirim, H.; Sohn, M.; Jonas, U.; Stief, C.G.; Andersson, K.E.; Hedlund, P.
Cyclic AMP-specific and cyclic GMP-specific phosphodiesterase isoenzymes in human cavernous arteries--immunohistochemical distribution and functional significance
World J. Urol.
23
405-410
2005
Homo sapiens
Manually annotated by BRENDA team
Murray, F.; Patel, H.H.; Suda, R.Y.; Zhang, S.; Thistlethwaite, P.A.; Yuan, J.X.; Insel, P.A.
Expression and activity of cAMP phosphodiesterase isoforms in pulmonary artery smooth muscle cells from patients with pulmonary hypertension: role for PDE1
Am. J. Physiol. Lung Cell Mol. Physiol.
292
L294-L303
2007
Homo sapiens
Manually annotated by BRENDA team
Bolger, G.B.; Baillie, G.S.; Li, X.; Lynch, M.J.; Herzyk, P.; Mohamed, A.; Mitchell, L.H.; McCahill, A.; Hundsrucker, C.; Klussmann, E.; Adams, D.R.; Houslay, M.D.
Scanning peptide array analyses identify overlapping binding sites for the signalling scaffold proteins, beta-arrestin and RACK1, in cAMP-specific phosphodiesterase PDE4D5
Biochem. J.
398
23-36
2006
Homo sapiens
Manually annotated by BRENDA team
Baillie, G.S.; Adams, D.R.; Bhari, N.; Houslay, T.M.; Vadrevu, S.; Meng, D.; Li, X.; Dunlop, A.; Milligan, G.; Bolger, G.B.; Klussmann, E.; Houslay, M.D.
Mapping binding sites for the PDE4D5 cAMP-specific phosphodiesterase to the N- and C-domains of beta-arrestin using spot-immobilized peptide arrays
Biochem. J.
404
71-80
2007
Homo sapiens, Homo sapiens (Q08499)
Manually annotated by BRENDA team
Wang, H.; Peng, M.S.; Chen, Y.; Geng, J.; Robinson, H.; Houslay, M.D.; Cai, J.; Ke, H.
Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors
Biochem. J.
408
193-201
2007
Homo sapiens, Homo sapiens (P27815), Homo sapiens (Q08499)
Manually annotated by BRENDA team
Mackenzie, K.F.; Topping, E.C.; Bugaj-Gaweda, B.; Deng, C.; Cheung, Y.F.; Olsen, A.E.; Stockard, C.R.; Mitchell, L.H.; Baillie, G.S.; Grizzle, W.E.; Devivo, M.; Houslay, M.D.; Wang, D.; Bolger, G.B.
Human PDE4A8, a novel brain-expressed PDE4 cAMP-specific phosphodiesterase that has undergone rapid evolutionary change
Biochem. J.
411
361-369
2007
Homo sapiens (P27815), Homo sapiens
Manually annotated by BRENDA team
Xiong, Y.; Lu, H.T.; Li, Y.; Yang, G.F.; Zhan, C.G.
Characterization of a catalytic ligand bridging metal ions in phosphodiesterases 4 and 5 by molecular dynamics simulations and hybrid quantum mechanical/molecular mechanical calculations
Biophys. J.
91
1858-1867
2006
Homo sapiens
Manually annotated by BRENDA team
Smith, K.J.; Baillie, G.S.; Hyde, E.I.; Li, X.; Houslay, T.M.; McCahill, A.; Dunlop, A.J.; Bolger, G.B.; Klussmann, E.; Adams, D.R.; Houslay, M.D.
1H NMR structural and functional characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, beta-arrestin and RACK1
Cell. Signal.
19
2612-2624
2007
Homo sapiens, Homo sapiens (Q08499)
Manually annotated by BRENDA team
Uckert, S.; Oelke, M.; Stief, C.G.; Andersson, K.E.; Jonas, U.; Hedlund, P.
Immunohistochemical distribution of cAMP- and cGMP-phosphodiesterase (PDE) isoenzymes in the human prostate
Eur. Urol.
49
740-745
2006
Homo sapiens
Manually annotated by BRENDA team
Wang, H.; Robinson, H.; Ke, H.
The molecular basis for different recognition of substrates by phosphodiesterase families 4 and 10
J. Mol. Biol.
371
302-307
2007
Homo sapiens
Manually annotated by BRENDA team
Cheung, Y.F.; Kan, Z.; Garrett-Engele, P.; Gall, I.; Murdoch, H.; Baillie, G.S.; Camargo, L.M.; Johnson, J.M.; Houslay, M.D.; Castle, J.C.
PDE4B5, a novel, super-short, brain-specific cAMP phosphodiesterase-4 variant whose isoform-specifying N-terminal region is identical to that of cAMP phosphodiesterase-4D6 (PDE4D6)
J. Pharmacol. Exp. Ther.
322
600-609
2007
Mus musculus, Homo sapiens (Q07343), Homo sapiens
Manually annotated by BRENDA team
Spoto, G.; della Malva, M.; Rubini, C.; Fioroni, M.; Piattelli, A.; Serra, E.; Di Nicola, M.; Santoleri, F.
cAMP phosphodiesterase activity evaluation in human carcinoma of salivary glands
Nucleosides Nucleotides Nucleic Acids
25
1113-1117
2006
Homo sapiens
Manually annotated by BRENDA team
Narita, M.; Murata, T.; Shimizu, K.; Nakagawa, T.; Sugiyama, T.; Inui, M.; Hiramoto, K.; Tagawa, T.
A role for cyclic nucleotide phosphodiesterase 4 in regulation of the growth of human malignant melanoma cells
Oncol. Rep.
17
1133-1139
2007
Homo sapiens
Manually annotated by BRENDA team
Brown, D.M.; Hutchison, L.; Donaldson, K.; MacKenzie, S.J.; Dick, C.A.; Stone, V.
The effect of oxidative stress on macrophages and lung epithelial cells: the role of phosphodiesterases 1 and 4
Toxicol. Lett.
168
1-6
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Fisher, D.A.; Smith, J.F.; Pillar, J.S.; Denis, S.H.St.; Cheng, J.B.
Isolation and characterization of PDE8A, a novel human cAMP-specific phosphodiesterase
Biochem. Biophys. Res. Commun.
246
570-577
1998
Homo sapiens (O60658), Homo sapiens
Manually annotated by BRENDA team
Sasaki, T.; Kotera, J.; Yuasa, K.; Omori, K.
Identification of human PDE7B, a cAMP-specific phosphodiesterase
Biochem. Biophys. Res. Commun.
271
575-583
2000
Homo sapiens
Manually annotated by BRENDA team
Gardner, C.; Robas, N.; Cawkill, D.; Fidock, M.
Cloning and characterization of the human and mouse PDE7B, a novel cAMP-specific cyclic nucleotide phosphodiesterase
Biochem. Biophys. Res. Commun.
272
186-192
2000
Homo sapiens (Q9NP56), Homo sapiens, Mus musculus (Q9QXQ1), Mus musculus
Manually annotated by BRENDA team
Bian, H.; Zhang, J.; Wu, P.; Lori, A.; Varty, Y.J.; Maywood, T.; Hey, J.A.; Wang, P.
Differential type 4 cAMP-specific phosphodiesterase (PDE4) expression and functional sensitivity to PDE4 inhibitors among rats, monkeys and humans
Biochem. Pharmacol.
68
2229-2236
2004
Rattus norvegicus (P14270), Rattus norvegicus (P14646), Rattus norvegicus (P54748), Homo sapiens (P27815), Homo sapiens (Q07343), Homo sapiens (Q08493), Homo sapiens (Q08499), Homo sapiens
Manually annotated by BRENDA team
Lynch, M.J.; Baillie, G.S.; Houslay, M.D.
cAMP-specific phosphodiesterase-4D5 (PDE4D5) provides a paradigm for understanding the unique non-redundant roles that PDE4 isoforms play in shaping compartmentalized cAMP cell signalling
Biochem. Soc. Trans.
35
938-941
2007
Homo sapiens
Manually annotated by BRENDA team
Amegadzie, B.Y.; Hanning, C.R.; McLaughlin, M.M.; Burman, M.; Cieslinski, L.B.; Livi, G.P.; Torphy, T.J.
Characterization of two human cAMP-specific phosphodiesterase subtypes expressed in baculovirus-infected insect cells
Cell Biol. Int.
19
477-484
1995
Homo sapiens
Manually annotated by BRENDA team
Richter, W.; Unciuleac, L.; Hermsdorf, T.; Kronbach, T.; Dettmer, D.
Identification of substrate specificity determinants in human cAMP-specific phosphodiesterase 4A by single-point mutagenesis
Cell. Signal.
13
159-167
2001
Homo sapiens
Manually annotated by BRENDA team
Houslay, M.D.; Baillie, G.S.; Maurice, D.H.
cAMP-Specific phosphodiesterase-4 enzymes in the cardiovascular system: a molecular toolbox for generating compartmentalized cAMP signaling
Circ. Res.
100
950-966
2007
Homo sapiens (P27815), Homo sapiens (Q07343), Homo sapiens (Q08499), Mus musculus (Q01063)
Manually annotated by BRENDA team
Horvath, A.; Giatzakis, C.; Tsang, K.; Greene, E.; Osorio, P.; Boikos, S.; Libe, R.; Patronas, Y.; Robinson-White, A.; Remmers, E.; Bertherat, J.; Nesterova, M.; Stratakis, C.A.
A cAMP-specific phosphodiesterase (PDE8B) that is mutated in adrenal hyperplasia is expressed widely in human and mouse tissues: a novel PDE8B isoform in human adrenal cortex
Eur. J. Hum. Genet.
16
1245-1253
2008
Homo sapiens, Homo sapiens (O95263), Mus musculus
Manually annotated by BRENDA team
McLaughlin, M.M.; Cieslinski, L.B.; Burman, M.; Torphy, T.J.; Livi, G.P.
A low-Km, rolipram-sensitive, cAMP-specific phosphodiesterase from human brain. Cloning and expression of cDNA, biochemical characterization of recombinant protein, and tissue distribution of mRNA
J. Biol. Chem.
268
6470-6476
1993
Homo sapiens (Q07343), Homo sapiens
Manually annotated by BRENDA team
Huston, E.; Pooley, L.; Julien, P.; Scotland, G.; McPhee, I.; Sullivan, M.; Bolger, G.; Houslay, M.D.
The human cyclic AMP-specific phosphodiesterase PDE-46 (HSPDE4A4B) expressed in transfected COS7 cells occurs as both particulate and cytosolic species that exhibit distinct kinetics of inhibition by the antidepressant rolipram
J. Biol. Chem.
271
31334-31344
1996
Homo sapiens
Manually annotated by BRENDA team
Persani, L.; Borgato, S.; Lania, A.; Filopanti, M.; Mantovani, G.; Conti, M.; Spada, A.
Relevant cAMP-specific phosphodiesterase isoforms in human pituitary: effect of Gs(alpha) mutations
J. Clin. Endocrinol. Metab.
86
3795-3800
2001
Homo sapiens (P27815), Homo sapiens (Q07343), Homo sapiens (Q08493), Homo sapiens (Q08499), Homo sapiens
Manually annotated by BRENDA team
Xin, W.; Tran, T.M.; Richter, W.; Clark, R.B.; Rich, T.C.
Roles of GRK and PDE4 activities in the regulation of beta2 adrenergic signaling
J. Gen. Physiol.
131
349-364
2008
Homo sapiens
Manually annotated by BRENDA team
Verghese, M.W.; McConnell, R.T.; Lenhard, J.M.; Hamacher, L.; Jin, S.L.C.
Regulation of distinct cyclic AMP-specific phosphodiesterase (phosphodiesterase type 4) isoenzymes in human monocytic cells
Mol. Pharmacol.
47
1164-1171
1995
Homo sapiens
Manually annotated by BRENDA team
Alvarez, R.; Sette, C.; Yang, D.; Eglen, R.M.; Wilhelm, R.; Shelton, E.R.; Conti, M.
Activation and selective inhibition of a cyclic AMP-specific phosphodiesterase, PDE-4D3
Mol. Pharmacol.
48
616-622
1995
Homo sapiens
Manually annotated by BRENDA team
Rena, G.; Begg, F.; Ross, A.; Mackenzie, C.; McPhee, I.; Campbell, L.; Huston, E.; Sullivan, M.; Houslay, M.D.
Molecular cloning, genomic positioning, promoter identification, and characterization of the novel cyclic AMP-specific phosphodiesterase PDE4A10
Mol. Pharmacol.
59
996-1011
2001
Homo sapiens
Manually annotated by BRENDA team
Zhu, S.; Gan, Z.; Li, Z.; Liu, Y.; Yang, X.; Deng, P.; Xie, Y.; Yu, M.; Liao, H.; Zhao, Y.; Zhao, L.; Liao, F.
The measurement of cyclic nucleotide phosphodiesterase 4 activities via the quantification of inorganic phosphate with malachite green
Anal. Chim. Acta
636
105-110
2009
Homo sapiens
Manually annotated by BRENDA team
Wang, H.; Yan, Z.; Yang, S.; Cai, J.; Robinson, H.; Ke, H.
Kinetic and structural studies of phosphodiesterase-8A and implication on the inhibitor selectivity
Biochemistry
47
12760-12768
2008
Homo sapiens (O60658), Homo sapiens
Manually annotated by BRENDA team
Nanda, K.; Chatterjee, M.; Arya, R.; Mukherjee, S.; Saini, K.S.; Dastidar, S.; Ray, A.
Optimization and validation of a reporter gene assay for screening of phosphodiesterase inhibitors in a high throughput system
Biotechnol. J.
3
1276-1279
2008
Homo sapiens
Manually annotated by BRENDA team
Herget, S.; Lohse, M.J.; Nikolaev, V.O.
Real-time monitoring of phosphodiesterase inhibition in intact cells
Cell. Signal.
20
1423-1431
2008
Homo sapiens (P27815)
Manually annotated by BRENDA team
Goldhoff, P.; Warrington, N.M.; Limbrick, D.D.; Hope, A.; Woerner, B.M.; Jackson, E.; Perry, A.; Piwnica-Worms, D.; Rubin, J.B.
Targeted inhibition of cyclic AMP phosphodiesterase-4 promotes brain tumor regression
Clin. Cancer Res.
14
7717-7725
2008
Homo sapiens
Manually annotated by BRENDA team
Santos-Silva, A.J.; Cairrao, E.; Morgado, M.; Alvarez, E.; Verde, I.
PDE4 and PDE5 regulate cyclic nucleotides relaxing effects in human umbilical arteries
Eur. J. Pharmacol.
582
102-109
2008
Homo sapiens (P27815), Homo sapiens (Q07343), Homo sapiens (Q08493), Homo sapiens (Q08499), Homo sapiens (Q13946), Homo sapiens
Manually annotated by BRENDA team
Maschi, O.; Cero, E.D.; Galli, G.V.; Caruso, D.; Bosisio, E.; DellAgli, M.
Inhibition of human cAMP-phosphodiesterase as a mechanism of the spasmolytic effect of Matricaria recutita L
J. Agric. Food Chem.
56
5015-5020
2008
Homo sapiens
Manually annotated by BRENDA team
Togo, S.; Liu, X.; Wang, X.; Sugiura, H.; Kamio, K.; Kawasaki, S.; Kobayashi, T.; Ertl, R.F.; Ahn, Y.; Holz, O.; Magnussen, H.; Fredriksson, K.; Skold, C.M.; Rennard, S.I.
PDE4 inhibitors roflumilast and rolipram augment PGE2 inhibition of TGF-beta1-stimulated fibroblasts
Am. J. Physiol. Lung Cell Mol. Physiol.
296
L959-L969
2009
Homo sapiens
Manually annotated by BRENDA team
Guo, J.; Watson, A.; Kempson, J.; Carlsen, M.; Barbosa, J.; Stebbins, K.; Lee, D.; Dodd, J.; Nadler, S.G.; McKinnon, M.; Barrish, J.; Pitts, W.J.
Identification of potent pyrimidine inhibitors of phosphodiesterase 7 (PDE7) and their ability to inhibit T cell proliferation
Bioorg. Med. Chem. Lett.
19
1935-1938
2009
Homo sapiens
Manually annotated by BRENDA team
Kagayama, K.; Morimoto, T.; Nagata, S.; Katoh, F.; Zhang, X.; Inoue, N.; Hashino, A.; Kageyama, K.; Shikaura, J.; Niwa, T.
Synthesis and biological evaluation of novel phthalazinone derivatives as topically active phosphodiesterase 4 inhibitors
Bioorg. Med. Chem.
17
6959-6970
2009
Homo sapiens
Manually annotated by BRENDA team
Schafer, P.H.; Parton, A.; Gandhi, A.K.; Capone, L.; Adams, M.; Wu, L.; Bartlett, J.B.; Loveland, M.A.; Gilhar, A.; Cheung, Y.F.; Baillie, G.S.; Houslay, M.D.; Man, H.W.; Muller, G.W.; Stirling, D.I.
Apremilast, a cAMP phosphodiesterase-4 inhibitor, demonstrates anti-inflammatory activity in vitro and in a model of psoriasis
Br. J. Pharmacol.
159
842-855
2010
Homo sapiens
Manually annotated by BRENDA team
Hatzimouratidis, K.; Hatzichristou, D.G.
Phosphodiesterase type 5 inhibitors: unmet needs
Curr. Pharm. Des.
15
3476-3485
2009
Homo sapiens
Manually annotated by BRENDA team
Zhang, L.; Murray, F.; Zahno, A.; Kanter, J.R.; Chou, D.; Suda, R.; Fenlon, M.; Rassenti, L.; Cottam, H.; Kipps, T.J.; Insel, P.A.
Cyclic nucleotide phosphodiesterase profiling reveals increased expression of phosphodiesterase 7B in chronic lymphocytic leukemia
Proc. Natl. Acad. Sci. USA
105
19532-19537
2008
Homo sapiens
Manually annotated by BRENDA team
Rampersad, S.; Ovens, J.; Huston, E.; Umana, M.; Wilson, L.; Netherton, S.; Lynch, M.; Baillie, G.; Houslay, M.; Maurice, D.
Cyclic AMP phosphodiesterase 4D (PDE4D) tethers EPAC1 in a vascular endothelial cadherin (VE-Cad)-based signaling complex and controls cAMP-mediated vascular permeability
J. Biol. Chem.
285
33614-33622
2010
Homo sapiens
Manually annotated by BRENDA team
Chen, X.; Zhao, X.; Xiong, Y.; Liu, J.; Zhan, C.G.
Fundamental reaction pathway and free energy profile for hydrolysis of intracellular second messenger adenosine 3',5'-cyclic monophosphate (cAMP) catalyzed by phosphodiesterase-4
J. Phys. Chem. B
115
12208-12219
2011
Homo sapiens
Manually annotated by BRENDA team
Lakics, V.; Karran, E.H.; Boess, F.G.
Quantitative comparison of phosphodiesterase mRNA distribution in human brain and peripheral tissues
Neuropharmacology
59
367-374
2010
Homo sapiens (O60658), Homo sapiens (O95263), Homo sapiens (P27815), Homo sapiens (Q07343), Homo sapiens (Q08493), Homo sapiens (Q08499), Homo sapiens (Q13946), Homo sapiens (Q9NP56)
Manually annotated by BRENDA team
Adderley, S.P.; Sprague, R.S.; Stephenson, A.H.; Hanson, M.S.
Regulation of cAMP by phosphodiesterases in erythrocytes
Pharmacol. Rep.
62
475-482
2010
Homo sapiens
Manually annotated by BRENDA team
Weninger, S.; Van Craenenbroeck, K.; Cameron, R.T.; Vandeput, F.; Movsesian, M.A.; Baillie, G.S.; Lefebvre, R.A.
Phosphodiesterase 4 interacts with the 5-HT4(b) receptor to regulate cAMP signaling
Cell. Signal.
26
2573-2582
2014
Homo sapiens
Manually annotated by BRENDA team
Lee, J.; Komatsu, K.; Lee, B.C.; Lim, J.H.; Jono, H.; Xu, H.; Kai, H.; Zhang, Z.J.; Yan, C.; Li, J.D.
Phosphodiesterase 4B mediates extracellular signal-regulated kinase-dependent up-regulation of mucin MUC5AC protein by Streptococcus pneumoniae by inhibiting cAMP-protein kinase A-dependent MKP-1 phosphatase pathway
J. Biol. Chem.
287
22799-22811
2012
Homo sapiens
Manually annotated by BRENDA team
Garcia, A.M.; Brea, J.; Morales-Garcia, J.A.; Perez, D.I.; Gonzalez, A.; Alonso-Gil, S.; Gracia-Rubio, I.; Ros-Simo, C.; Conde, S.; Cadavid, M.I.; Loza, M.I.; Perez-Castillo, A.; Valverde, O.; Martinez, A.; Gil, C.
Modulation of cAMP-specific PDE without emetogenic activity: new sulfide-like PDE7 inhibitors
J. Med. Chem.
57
8590-8607
2014
Homo sapiens (Q07343), Homo sapiens (Q08499), Homo sapiens (Q13946), Homo sapiens
Manually annotated by BRENDA team
Wahlang, B.; McClain, C.; Barve, S.; Gobejishvili, L.
Role of cAMP and phosphodiesterase signaling in liver health and disease
Cell. Signal.
49
105-115
2018
Homo sapiens
Manually annotated by BRENDA team
Cai, Y.; Nagel, D.J.; Zhou, Q.; Cygnar, K.D.; Zhao, H.; Li, F.; Pi, X.; Knight, P.A.; Yan, C.
Role of cAMP-phosphodiesterase 1C signaling in regulating growth factor receptor stability, vascular smooth muscle cell growth, migration, and neointimal hyperplasia
Circ. Res.
116
1120-1132
2015
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Cao, B.; Wang, K.; Liao, J.M.; Zhou, X.; Liao, P.; Zeng, S.X.; He, M.; Chen, L.; He, Y.; Li, W.; Lu, H.
Inactivation of oncogenic cAMP-specific phosphodiesterase 4D by miR-139-5p in response to p53 activation
eLife
5
e15978
2016
Homo sapiens (Q08499), Homo sapiens
Manually annotated by BRENDA team
Byrne, A.M.; Elliott, C.; Hoffmann, R.; Baillie, G.S.
The activity of cAMP-phosphodiesterase 4D7 (PDE4D7) is regulated by protein kinase A-dependent phosphorylation within its unique N-terminus
FEBS Lett.
589
750-755
2015
Homo sapiens (Q08499)
Manually annotated by BRENDA team
Huang, Y.M.; Huber, G.; McCammon, J.A.
Electrostatic steering enhances the rate of cAMP binding to phosphodiesterase Brownian dynamics modeling
Protein Sci.
24
1884-1889
2015
Homo sapiens (Q08499)
Manually annotated by BRENDA team