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Information on EC 3.1.4.35 - 3',5'-cyclic-GMP phosphodiesterase and Organism(s) Bos taurus
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3.1.4.35 3',5'-cyclic-GMP phosphodiesteraseSpecify your search results
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- 3.1.4.35
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guanylate
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vasodilator
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placebo
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hemodynamic
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-
cgmp-dependent
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placebo-controlled
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guanylyl
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intercourse
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prostatectomy
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double-blind
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prostanoids
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on-demand
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alpha-blocker
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The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phosphodiesterase type 5, phosphodiesterase-5, pde-5, phosphodiesterase 5, cgmp phosphodiesterase, pde5a, cyclic gmp phosphodiesterase, phosphodiesterase type-5, pde6b, cgmp-phosphodiesterase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3',5'-cyclic GMP phosphodiesterase
-
-
-
-
cGMP phosphodiesterase
cGMP-PDE
-
-
-
-
cyclic 3',5'-GMP phosphodiesterase
-
-
-
-
cyclic GMP phosphodiesterase
-
-
-
-
cyclic guanosine 3',5'-monophosphate phosphodiesterase
-
-
-
-
cyclic guanosine 3',5'-phosphate phosphodiesterase
-
-
-
-
guanosine cyclic 3',5'-phosphate phosphodiesterase
-
-
-
-
PDE5
phosphodiesterase cGMP
-
-
-
-
phosphodiesterase, guanosine cyclic 3',5'-phosphate
-
-
-
-
cGMP phosphodiesterase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
SYSTEMATIC NAME
IUBMB Comments
3',5'-cyclic-GMP 5'-nucleotidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9068-52-4
-
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
2'-O-anthraniloyl-cGMP + H2O
?
-
phosphorylation increases affinity for hydrolysis of 2'-O-anthraniloyl-cGMP by about 3fold
-
-
?
3',5'-cAMP + H2O
5'-AMP
-
activity with 3',5'-cAMP is higher than with 3',5'-cGMP, PDE6
-
-
?
3',5'-cGMP + H2O
5'-GMP
-
-
-
-
?
3',5'-cGMP + H2O
5'-GMP
-
allosteric cGMP-binding sites of PDE5 could regulate cGMP signaling by sequestering cGMP from cGMP-dependent protein kinase and perhaps from the PDE5 catalytic site as well. The cGMP sequestered by binding of cGMP to PDE5 R domain significantly dampens activation of cGMP-dependent protein kinase and hydrolysis of cGMP by PDE5 C domain
-
-
?
3',5'-cGMP + H2O
5'-GMP
-
activity with 3',5'-cAMP is higher than with 3',5'-cGMP, PDE6
-
-
?
3',5'-cGMP + H2O
5'-GMP
-
PDE5 and PDE6 show specificity for cGMP relative to cAMP
-
-
?
additional information
?
-
-
preincubation with cGMP increases catalytic activity for cGMP degradation, thus elevated cellular cGMP initiates a physiological negative feedback on the cGMP pathway by increasing the affinity of the PDE5 catalytic site for cGMP
-
-
?
additional information
?
-
-
analysis of diverse complxes formed by subunits Pgamma with GTP or GDP and outer segments, the complexes are extracted from membranes and isolated. Analysis of the function of the single complexes in PDE regulation, overview
-
-
?
additional information
?
-
-
interaction between the PDE6 gamma subunit with tubulin alpha and beta, specificity and mechanism, detailed 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
3',5'-cGMP + H2O
5'-GMP
-
allosteric cGMP-binding sites of PDE5 could regulate cGMP signaling by sequestering cGMP from cGMP-dependent protein kinase and perhaps from the PDE5 catalytic site as well. The cGMP sequestered by binding of cGMP to PDE5 R domain significantly dampens activation of cGMP-dependent protein kinase and hydrolysis of cGMP by PDE5 C domain
-
-
?
3',5'-cGMP + H2O
5'-GMP
-
PDE5 and PDE6 show specificity for cGMP relative to cAMP
-
-
?
additional information
?
-
-
preincubation with cGMP increases catalytic activity for cGMP degradation, thus elevated cellular cGMP initiates a physiological negative feedback on the cGMP pathway by increasing the affinity of the PDE5 catalytic site for cGMP
-
-
?
additional information
?
-
-
analysis of diverse complxes formed by subunits Pgamma with GTP or GDP and outer segments, the complexes are extracted from membranes and isolated. Analysis of the function of the single complexes in PDE regulation, overview
-
-
?
additional information
?
-
-
interaction between the PDE6 gamma subunit with tubulin alpha and beta, specificity and mechanism, detailed overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-6-(3-(3-cyclopropyl-3-((1R,2R)-2-hydroxycyclohexyl)ureido)-propoxy)-2(1H)-quinolinone
-
IC50: 0.0121 mM, PDE5
2-cyclohexyl-2-methyl-N1-[3-(2-oxo-1,2-dihydro-6-quinolyl,oxy)propyl]-1-hydrazinecarboxamide
-
IC50: 0.0027 mM, PDE5
6-(3-(3-cyclooctyl-3-((1R,2R)-2-hydroxycyclohexyl)ureido)-propoxy)-2(1H)-quinolinone
-
IC50: 0.0025 mM, PDE5
8-methoxymethyl-isobutylmethylxanthine
-
inhibits isoform PDE5, is 3times more potent in inhibiting PDE5 than PDE1
dioclein
-
dioclein is at least 11times more potent in inhibiting calmodulin-activated PDE1 than other PDE types. Among PDE1-PDE5, dioclein is at least 11fold more selective for the activated PDE1 isoform compared to PDE5 (16fold)
sildenafil
-
preincubation with cGMP increases catalytic activity for cGMP degradation, but also for binding of inhibitor
tadalafil
-
preincubation with cGMP increases catalytic activity for cGMP degradation, but also for binding of inhibitor
tadalafil
-
cGMP modestly but significantly increases the affinity of PDE5 for tadalafil by 1.7fold
vardenafil
-
preincubation with cGMP increases catalytic activity for cGMP degradation, but also for binding of inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-subunit of transducin
-
activation of isoform PDE6 by binding to the inhibitory gamma-subunit
-
cGMP
-
preincubation with cGMP increases catalytic activity for cGMP degradation, this increase may be caused by binding of cGMP to either the PDE5 allosteric sites, catalytic sites, or both. Full-length GAF-B subdomain conjoined with catalytic domain is sufficient for this conversion
additional information
-
phosphorylation acts in concert with allosteric cGMP binding to stimulate the PDE5 catalytic site, which should promote negative feedback regulation of the cGMP pathway in intact cells
-
light
-
activation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0036
3',5'-cGMP
-
chimaeric PDE5/PDE6 catalytic domain, pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.55
3',5'-cGMP
-
chimaeric PDE5/PDE6 catalytic domain, pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0085
3-isobutyl-1-methylxanthine
-
chimaeric PDE5/6 catalytic domain, pH and temperature not specified in the publication
0.0015
Pgamma-inhibitory peptide
-
chimaeric PDE5/6 catalytic domain, pH and temperature not specified in the publication
-
0.0029
Pgamma-inhibitory peptide Pgamma63-87
-
chimaeric PDE5/6 catalytic domain, pH and temperature not specified in the publication
-
0.0121
Pgamma-inhibitory peptide Pgamma70-87
-
chimaeric PDE5/6 catalytic domain, pH and temperature not specified in the publication
-
0.000025
sildenafil
-
chimaeric PDE5/6 catalytic domain, pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0121
(-)-6-(3-(3-cyclopropyl-3-((1R,2R)-2-hydroxycyclohexyl)ureido)-propoxy)-2(1H)-quinolinone
Bos taurus
-
IC50: 0.0121 mM, PDE5
0.0027
2-cyclohexyl-2-methyl-N1-[3-(2-oxo-1,2-dihydro-6-quinolyl,oxy)propyl]-1-hydrazinecarboxamide
Bos taurus
-
IC50: 0.0027 mM, PDE5
0.0025
6-(3-(3-cyclooctyl-3-((1R,2R)-2-hydroxycyclohexyl)ureido)-propoxy)-2(1H)-quinolinone
Bos taurus
-
IC50: 0.0025 mM, PDE5
0.0055
8-methoxymethyl-isobutylmethylxanthine
Bos taurus
-
isoform PDE5, pH and temperature not specified in the publication
0.023
dioclein
Bos taurus
-
isoform PDE5, pH and temperature not specified in the publication
0.000002
sildenafil
Bos taurus
-
isoform PDE5, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
evolution
-
mechanisms for PDE activation are similar in mammalian and amphibian photoreceptors as well as in rods and cones
malfunction
-
identification of a Pgamma-depleted PDE as Palphabetagamma, detailed overview
physiological function
-
cyclic GMP phosphodiesterase in bovine rod photoreceptor outer segments comprises a catalytic subunit complex, Palphabeta, and two inhibitory subunits Pgamma, and is regulated by the a subunit of transducin. The mechanism for PDE regulation involves complex formations between the gamma subunits with outer segments, overview. Pgamma as a complex with the GTP-bound transducin a subunit, GTP-Talpha, dissociates from Palphabetagammagamma on membranes, and the Palphabetagammagamma becomes Pgamma-depleted
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). PDE6A_BOVIN
859
0
99341
Swiss-Prot
other Location (Reliability: 1)
PDE6B_BOVIN
853
0
98331
Swiss-Prot
other Location (Reliability: 1)
PDE6C_BOVIN
855
0
98798
Swiss-Prot
other Location (Reliability: 1)
CNCG_BOVIN
83
0
9102
Swiss-Prot
other Location (Reliability: 2)
CNRG_BOVIN
87
0
9669
Swiss-Prot
other Location (Reliability: 2)
PDE5A_BOVIN
865
0
98627
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
88000
88000
-
88000, alpha-subunit, + 84000, beta-subunit, + 1100, gamma-subunit, inhibitory, SDS-PAGE
88000
-
88000, alpha-subunit + 84000, beta-subunit + 13000-14000, gamma-subunit, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
88000, alpha-subunit, + 84000, beta-subunit, + 1100, gamma-subunit, inhibitory, SDS-PAGE
?
-
88000, alpha-subunit + 84000, beta-subunit + 13000-14000, gamma-subunit, SDS-PAGE
additional information
-
alpha-subunit of transducin interacts with the inhibitory gamma subunit of PDE6 thereby activating the enzyme. Interaction requires activated alpha-subunit of transducin and involves the C-terminus of PDE6 gamma-subunit, particularly residue 73
additional information
-
enzyme forms a catalytic Palphabeta heterodimer in complex with two Pgamma inhibitory subunits. The N-terminal V16-F30 region of inhibitory subunit Pgamma interacts with the Palphabeta GAFa domain, and the Pgamma F73-I87 C-terminus interacts with the Palphabeta catalytic domain, indicating a linear and extended interaction between Pgamma and Palphabeta. Pgamma may interact with Palpha and Pbeta simultaneously
additional information
-
rod photoreceptor cGMP phosphodiesterase consists of a catalytic subunit complex, Palphabeta, and two inhibitory subunits, Pgamma. Isolation of Palphalphabetagammaagammadelta and Palphabetagammadeltadelta suggests that one C-terminus of Palphabeta is involved in the Palphabetagammagamma interaction with membranes, and that Pgamma dissociation opens another C-terminus for Pdelta, a prenyl-binding protein, binding, which may lead to the expression of high PDE activity. Extraction, isolation and analysis of diverse subunit complexes, detailed overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
PDE5 is phosphorylated at Ser92 by cyclic nucleotide-dependent protein kinases, phosphorylation activates PDE5 catalytic site independently of cGMP binding to the allosteric sites
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chimaeric PDE5/PDE6 catalytic domain complexed with sildenafil or 3-isobutyl-1-methylxanthine and the Pgamma-inhibitory peptide Pgamma70-87, hanging drop vapor diffusion method, using 100 mM Tris (pH 8.5), 200 mM MgSO4, 12% (w/v) PEG-3350, and 2.5% (v/v) ethanol, at 4°C
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C68A
-
expression of isoform PDE6 wild-type and mutant C68A gamma-subunit in Escherichia coli, preparation of homogeneous and isotopically labeled protein for NMR analysis
D644A
-
10% and 4% of maximal activity in the absence of Mn2+ and Mg2+, respectively
D714A
-
33% and 22% of maximal activity in the absence of Mn2+ and Mg2+, respectively
D754A
-
59% and 28% of maximal activity in the absence of Mn2+ and Mg2+, respectively
E632A
-
20% and 16% of maximal activity in the absence of Mn2+ and Mg2+, respectively
E672A
-
3% and 8% of maximal activity in the absence of Mn2+ and Mg2+, respectively
H603A
-
38% and 22% of maximal activity in the absence of Mn2+ and Mg2+, respectively
H607A
-
3.9% and 13% of maximal activity in the absence of Mn2+ and Mg2+, respectively
H643A
-
3% and less than 1% of maximal activity in the absence of Mn2+ and Mg2+, respectively
H647A
-
less than 1% of maximal activity in the absence of Mn2+ and Mg2+, respectively
H675A
-
9% and 4% of maximal activity in the absence of Mn2+ and Mg2+, respectively
N604A
-
less than 2% of maximal activity in the absence of Mn2+ and Mg2+, respectively
N661A
-
the substitution moderately increases the Km value for cGMP hydrolysis but it markedly decreases the potency of PDE5/6cd inhibition by Pgamma inhibitory peptide
additional information
-
expression of isoform PDE6 wild-type and mutant C68A gamma-subunit in Escherichia coli, preparation of homogeneous and isotopically labeled protein for NMR analysis
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM morpholinopropanesulfonic acid, 1.5 mM MgCl2, 0.1 mM phenylmethylsulfonyl fluoride, 1 mM dithiothreitol, 50% glycerol, pH 7.5, more than 6 months
-
-20°C, purified isoenzyme PDE6R and PDE6C can be stored for several months with minimal loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of isoform PDE6 gamma-subunit in Escherichia coli, preparation of homogeneous and isotopically labeled protein for NMR analysis
-
NiSO4-charged His-bind resin column chromatography and benzamidine Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chimaeric PDE5/PDE6 catalytic domain is expressed in Escherichia coli BL21-codon plus cells
-
expression of isoform PDE6 gamma-subunit in Escherichia coli as an intein-fusion with chitin binding domain. Preparation of homogeneous and isotopically labeled protein for NMR analysis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamazaki, A.; Tatsumi, M.; Bitensky, M.W.
Purification of rod outer segment GTP-binding protein subunits and cGMP phosphodiesterase by single-step column chromatography
Methods Enzymol.
159
702-710
1988
Bos taurus
Deterre, P.; Bigay, J.; Robert, M.; Pfister, C.; Kuhn, H.; Chabre, M.
Activation of retinal rod cyclic GMP-phosphodiesterase by transducin: characterization of the complex formed by phosphodiesterase inhibitor and transducin alpha-subunit
Proteins Struct. Funct. Genet.
1
188-193
1986
Bos taurus
Hurley, J.B.; Stryer, L.
Purification and characterization of the gamma regulatory subunit of the cyclic GMP phosphodiesterase from retinal rod outer segments
J. Biol. Chem.
257
11094-11099
1982
Bos taurus
Hurley, J.B.
Isolation and assay of a phosphodiesterase inhibitor from retinal rod outer segments
Methods Enzymol.
81
542-547
1982
Bos taurus
Liebman, P.A.; Tavormina Evanczuk, A.
Real time assay of rod disk membrane cGMP phosphodiesterase and its controller enzymes
Methods Enzymol.
81
532-542
1982
Bos taurus
Caretta, A.; Stein, P.J.
Light- and nucleotide-dependent binding of phosphodiesterase to rod disk membranes: correlation with light-scattering changes and vesicle aggregation
Biochemistry
25
2335-2341
1986
Bos taurus
Sitaramayya, A.; Liebman, P.A.
Phosphorylation of rhodopsin and quenching of cyclic GMP phosphodiesterase activation by ATP at weak bleaches
J. Biol. Chem.
258
12106-12109
1983
Bos taurus
Artemyev, N.O.; Natochin, M.; Busman, M.; Schey, K.L.; Ha mM, H.E.
Mechanism of photoreceptor cGMP phosphodiesterase inhibition by its gamma subunits
Proc. Natl. Acad. Sci. USA
93
5407-5412
1996
Bos taurus
Artemyev, N.O.; Hamm, H.E.
Two-site high-affinity interaction between inhibitory and catalytic subunits of rod cyclic GMP phosphodiesterase
Biochem. J.
283
273-279
1992
Bos taurus
-
Whalen, M.M.; Bitensky, M.W.; Takemoto, D.J.
The effect of the gamma-subunit of the cyclic GMP phosphodiesterase of bovine and frog (Rana catesbiana) retinal rod outer segments on the kinetic parameters of the enzyme
Biochem. J.
265
655-658
1990
Bos taurus, Lithobates catesbeianus
Srivastava, D.; Fox, D.A.; Hurwitz, R.L.
Effects of magnesium on cyclic GMP hydrolysis by the bovine retinal rod cyclic GMP phosphodiesterase
Biochem. J.
308
653-658
1995
Bos taurus
Oppert, B.; Cunnick, J.M.; Hurt, D.; Tamoto, D.J.
Identification of the retinal cyclic GMP phosphodiesterase inhibitory gamma-subunit interaction sites on the catalytic alpha-subunit
J. Biol. Chem.
266
16607-16613
1991
Bos taurus
Thomas, M.K.; Francis, S.H.; Corbin, J.D.
Characterization of a purified bovine lung cGMP-binding cGMP phosphodiesterase
J. Biol. Chem.
265
14964-14970
1990
Bos taurus
Natochin, M.; Artemyev, N.O.
An interface of interaction between photoreceptor cGMP phosphodiesterase catalytic subunits and inhibitory gamma subunits
J. Biol. Chem.
271
19964-19969
1996
Bos taurus
Udovichenko, I.P.; Cunnick, J.; Gonzales, K.; Takemoto, D.J.
Phosphorylation of bovine rod photoreceptor cyclic GMP phosphodiesterase
Biochem. J.
295
49-55
1993
Bos taurus
Tar, A.; Ting, T.D.; Ho, Y.K.
Purification of bovine retinal cGMP phosphodiesterase
Methods Enzymol.
238
3-12
1994
Bos taurus
Otto-Bruc, A.; Antonny, B.; Vuong, T.M.; Chardin, P.; Chabre, M.
Interaction between the retinal cyclic GMP phosphodiesterase inhibitor and transducin. Kinetics and affinity studies
Biochemistry
32
8636-8645
1993
Bos taurus
Oppert, B.; Gonzalez, K.; Hurt, D.; Cunnick, J.; Takemoto, D.
Retinal cyclic-GMP phosphodiesterase gamma-subunit: use of mutant synthetic peptides to define function
Biochem. Biophys. Res. Commun.
181
306-309
1991
Bos taurus
Oppert, B.; Takemoto, D.J.
Identification of the gamma-subunit interaction sites in the retinal cyclic-GMP phosphodiesterase gamma-subunit
Biochem. Biophys. Res. Commun.
178
474-479
1991
Bos taurus
Sudo, T.; Tachibana, K.; Toga, K.; Tochizawa, S.; Inoue, Y.; Kimura, Y.; Hidaka, H.
Potent effects of novel anti-platelet aggregatory cilostamide analogues on recombinant cyclic nucleotide phosphodiesterase isozyme activity
Biochem. Pharmacol.
59
347-356
2000
Bos taurus
Francis, S.H.; Turko, I.V.; Grimes, K.A.; Corbin, J.D.
Histidine-607 and histidine-643 provide important interactions for metal support of catalysis in phosphodiesterase-5
Biochemistry
39
9591-9596
2000
Bos taurus
Kotera, J.; Francis, S.H.; Grimes, K.A.; Rouse, A.; Blount, M.A.; Corbin, J.D.
Allosteric sites of phosphodiesterase-5 sequester cyclic GMP
Front. Biosci.
9
378-386
2004
Bos taurus
Bischoff, E.
Potency, selectivity, and consequences of nonselectivity of PDE inhibition
Int. J. Impot. Res.
16
S11-S14
2004
Bos taurus, Homo sapiens, Bos taurus PDE6
Pentia, D.C.; Hosier, S.; Collupy, R.A.; Valeriani, B.A.; Cote, R.H.
Purification of PDE6 isozymes from mammalian retina
Methods Mol. Biol.
307
125-140
2005
Bos taurus
Blount, M.A.; Beasley, A.; Zoraghi, R.; Sekhar, K.R.; Bessay, E.P.; Francis, S.H.; Corbin, J.D.
Binding of tritiated sildenafil, tadalafil, or vardenafil to the phosphodiesterase-5 catalytic site displays potency, specificity, heterogeneity, and cGMP stimulation
Mol. Pharmacol.
66
144-152
2004
Bos taurus
Guo, L.W.; Muradov, H.; Hajipour, A.R.; Sievert, M.K.; Artemyev, N.O.; Ruoho, A.E.
The inhibitory gamma subunit of the rod cGMP phosphodiesterase binds the catalytic subunits in an extended linear structure
J. Biol. Chem.
281
15412-15422
2006
Bos taurus
Grant, J.E.; Guo, L.W.; Vestling, M.M.; Martemyanov, K.A.; Arshavsky, V.Y.; Ruoho, A.E.
The N terminus of GTP gamma S-activated transducin alpha-subunit interacts with the C terminus of the cGMP phosphodiesterase gamma-subunit
J. Biol. Chem.
281
6194-6202
2006
Bos taurus
Blount, M.A.; Zoraghi, R.; Bessay, E.P.; Beasley, A.; Francis, S.H.; Corbin, J.D.
Conversion of phosphodiesterase-5 (PDE5) catalytic site to higher affinity by PDE5 inhibitors
J. Pharmacol. Exp. Ther.
323
730-737
2007
Bos taurus
Guo, L.W.; Assadi-Porter, F.M.; Grant, J.E.; Wu, H.; Markley, J.L.; Ruoho, A.E.
One-step purification of bacterially expressed recombinant transducin alpha-subunit and isotopically labeled PDE6 gamma-subunit for NMR analysis
Protein Expr. Purif.
51
187-197
2007
Bos taurus
Reingruber, J.; Holcman, D.
Estimating the rate constant of cyclic GMP hydrolysis by activated phosphodiesterase in photoreceptors
J. Chem. Phys.
129
145102
2008
Bos taurus, Homo sapiens
Goncalves, R.L.; Lugnier, C.; Keravis, T.; Lopes, M.J.; Fantini, F.A.; Schmitt, M.; Cortes, S.F.; Lemos, V.S.
The flavonoid dioclein is a selective inhibitor of cyclic nucleotide phosphodiesterase type 1 (PDE1) and a cGMP-dependent protein kinase (PKG) vasorelaxant in human vascular tissue
Eur. J. Pharmacol.
620
78-83
2009
Bos taurus
Barren, B.; Gakhar, L.; Muradov, H.; Boyd, K.K.; Ramaswamy, S.; Artemyev, N.O.
Structural basis of phosphodiesterase 6 inhibition by the C-terminal region of the gamma-subunit
EMBO J.
28
3613-3622
2009
Bos taurus
Yamazaki, A.; Bondarenko, V.A.; Matsuura, I.; Tatsumi, M.; Kurono, S.; Komori, N.; Matsumoto, H.; Hayashi, F.; Yamazaki, R.K.; Usukura, J.
Mechanism for the regulation of mammalian cGMP phosphodiesterase6. 1: identification of its inhibitory subunit complexes and their roles
Mol. Cell. Biochem.
339
215-233
2010
Bos taurus
Yamazaki, A.; Tatsumi, M.; Bondarenko, V.A.; Kurono, S.; Komori, N.; Matsumoto, H.; Matsuura, I.; Hayashi, F.; Yamazaki, R.K.; Usukura, J.
Mechanism for the regulation of mammalian cGMP phosphodiesterase6. 2: isolation and characterization of the transducin-activated form
Mol. Cell. Biochem.
339
235-251
2010
Bos taurus
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