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Information on EC 3.1.4.53 - 3',5'-cyclic-AMP phosphodiesterase and Organism(s) Pseudomonas aeruginosa and UniProt Accession D4P095
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3.1.4.53 3',5'-cyclic-AMP phosphodiesteraseIUBMB 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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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
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, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
KEGG
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
9036-21-9
-
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
3',5'-cAMP + H2O
5'-AMP
CpdA possesses 3',5'-cAMP phosphodiesterase activity in vitro
-
-
?
adenosine 3',5'-cyclic phosphate + H2O
adenosine 5'-phosphate
-
-
-
?
additional information
?
-
iron and conserved residues are essential for CpdA activity, the catalytic mechanism for Pseudomonas aeruginosa CpdA utilizes a Fe3+-Fe2+ center
-
-
?
additional information
?
-
-
iron and conserved residues are essential for CpdA activity, the catalytic mechanism for Pseudomonas aeruginosa CpdA utilizes a Fe3+-Fe2+ center
-
-
?
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'-cAMP + H2O
5'-AMP
CpdA possesses 3',5'-cAMP phosphodiesterase activity in vitro
-
-
?
additional information
?
-
iron and conserved residues are essential for CpdA activity, the catalytic mechanism for Pseudomonas aeruginosa CpdA utilizes a Fe3+-Fe2+ center
-
-
?
additional information
?
-
-
iron and conserved residues are essential for CpdA activity, the catalytic mechanism for Pseudomonas aeruginosa CpdA utilizes a Fe3+-Fe2+ center
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
additional information
Fe2+
Fe2+ is required for enzyme activity. The catalytic mechanism for CpdA utilizes a Fe3+-Fe2+ center. Addition of 0.01 mM FeCl2, as a source of Fe2+, results in an 2fold stimulation of CpdA activity
Fe2+
iron and conserved residues are essential for CpdA activity
additional information
the addition of Mg2+, Mn2+, Zn2+, and Ca2+ has no effect on CdpA
additional information
-
the addition of Mg2+, Mn2+, Zn2+, and Ca2+ has no effect on CdpA
additional information
no effect on enzyme activity by Mg2+, Mn2+, Zn2+, and Ca2+
additional information
-
no effect on enzyme activity by Mg2+, Mn2+, Zn2+, and Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-alpha'-dipyridyl
treatment of CpdA with the Fe2+-specific chelator alpha-alpha'-dipyridyl results in a nearly complete loss of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0067
3',5'-cAMP
the addition of FeCl2 does not significantly influence substrate affinity of CdpA increases the rate of the 5'-AMP production, pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
deletion of cpdA results in the accumulation of intracellular cAMP and altered regulation of Pseudomonas aeruginosa virulence traits
malfunction
deletion of cpdA results in the accumulation of intracellular cAMP and altered regulation of Pseudomonas aeruginosa virulence traits. The cpdA mutant has a cAMP-independent small-colony, slow-growth phenotype
physiological function
CpdA is required for cAMP homeostasis and virulence factor regulation, CpdA affects vfr expression and Vfr protein levels and production of virulence factors ExoS, ToxA, and protease IV
physiological function
CpdA possesses 3',5'-cAMP phosphodiesterase activity in vitro and that it utilizes an iron-dependent catalytic mechanism. The cAMP-dependent transcription factor Vfr directly regulates cpdA expression in response to intracellular cAMP accumulation, thus providing a feedback mechanism for controlling cAMP levels and fine-tuning virulence factor expression. CpdA affects vfr expression and Vfr protein levels. CpdA affects production of virulence factors ExoS, ToxA, and protease IV
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D63A
the mutant shows less than 0.1% of wild type CpdA activity
H23A
the mutant shows less than 0.1% of wild type CpdA activity
N93A
the mutant shows less than 0.1% of wild type CpdA activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Sephacryl S-200 gel filtration
recombinant His-tagged enzyme from Escherichia coli strain M15(pREP4) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cpdA, DNA and mino acid sequenc determination and analysis, expression of His-tagged enzyme in Escherichia coli strain M15(pREP4)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cpdA expression is positively regulated by cAMP-Vfr. cAMP-Vfr binds to the cpdA promoter region, suggesting that in vivo, cpdA transcription is directly activated by cAMP-Vfr
the cAMP-dependent transcription factor Vfr directly activates expression of cpdA in response to elevated intracellular cAMP
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fuchs, E.L.; Brutinel, E.D.; Klem, E.R.; Fehr, A.R.; Yahr, T.L.; Wolfgang, M.C.
In vitro and in vivo characterization of the Pseudomonas aeruginosa cAMP phosphodiesterase CpdA required for cAMP homeostasis and virulence factor regulation
J. Bacteriol.
192
2779-2790
2010
Pseudomonas aeruginosa (D4P095), Pseudomonas aeruginosa
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Release 2023.1 (January 2023)
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