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Literature summary for 3.1.4.53 extracted from

  • Kimura, Y.; Okazaki, N.; Takegawa, K.
    Enzymatic characteristics of two novel Myxococcus xanthus enzymes, PdeA and PdeB, displaying 3',5'- and 2'3'-cAMP phosphodiesterase, and phosphatase activities (2009), FEBS Lett., 583, 443-448.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 cells Myxococcus xanthus

Inhibitors

Inhibitors Comment Organism Structure
EDTA PdeA and PdeB show 39% residual activity, respectively, for 3',5'-cAMP hydrolysis at 0.1 mM EDTA Myxococcus xanthus
additional information he 3',5'-phosphodiesterase activities of PdeA and PdeB are not inhibited by theophylline, 3-isobuthyl-1-methylxanthine, and beta-glycerophosphate Myxococcus xanthus
O-phospho-L-serine PdeA and PdeB show 59% and 73% residual activity, respectively, for 3',5'-cAMP hydrolysis at 5 mM phosphoserine Myxococcus xanthus
O-phospho-L-tyrosine PdeA and PdeB show 44% and 52% residual activity, respectively, for 3',5'-cAMP hydrolysis at 5 mM phosphotyrosine Myxococcus xanthus
orthovanadate PdeA and PdeB show 26% and 29% residual activity, respectively, for 3',5'-cAMP hydrolysis at 1 mM orthovanadate Myxococcus xanthus
Zn2+ the 3',5'-phosphodiesterase enzyme activities of PdeA and PdeB are reduced to 24% and 28%, respectively, by 0.05 mM Zn2+ at pH 8.0 in 50 mM Tris-HCl buffer Myxococcus xanthus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0033
-
3',5'-cAMP PdeA, in 50 mM Tris-HCl, pH 8.0, 0.05 mM MnCl2, at 40°C Myxococcus xanthus
0.005
-
3',5'-cAMP PdeB, in 50 mM Tris-HCl, pH 8.0, 0.05 mM MnCl2, at 40°C Myxococcus xanthus

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ the 3',5'-phosphodiesterase enzyme activities of PdeA and PdeB are stimulated 3.2fold and 1.98old, respectively, by 0.05 mM Co2+ at pH 8.0 in 50 mM Tris-HCl buffer Myxococcus xanthus
Mn2+ the 3',5'-phosphodiesterase enzyme activities of PdeA and PdeB are stimulated 4fold and 2.14old, respectively, by 0.05 mM Mn2+ at pH 8.0 in 50 mM Tris-HCl buffer Myxococcus xanthus
additional information the 3',5'-phosphodiesterase enzyme activities of PdeA and PdeB are not stimulated by 0.05 mM Ca2+, Mg2+, Fe2+, and Fe3+ Myxococcus xanthus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
PdeA, SDS-PAGE Myxococcus xanthus
29000
-
PdeA, calculated from amino acid sequence Myxococcus xanthus
31000
-
PdeB, calculated from amino acid sequence Myxococcus xanthus
34000
-
PdeB, SDS-PAGE Myxococcus xanthus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3',5'-cAMP + H2O Myxococcus xanthus
-
5'-AMP the reaction product, 5'-AMP, is further dephosphorylated to adenosine by PdeA and PdeB ?
additional information Myxococcus xanthus Myxococcus xanthus PdeA and PdeB, enzymes hydrolyze 3',5'- and 2',3'-cyclic AMP to adenosine, and also demonstrate phosphatase activity toward nucleoside 5'-tri-, 5'-di-, 5'- and 3'-monophosphates with highest activities for nucleoside 5'-monophosphates. PdeA and PdeB also show high phosphomonoesterase activities against 50-UMP, 3'-AMP, and 3'-GMP, low activities against 5'-dAMP, and no activities toward 2'-AMP and 2'-GMP ?
-
?

Organism

Organism UniProt Comment Textmining
Myxococcus xanthus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Talon CellThru column chromatography, gel filtration Myxococcus xanthus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3',5'-cAMP + H2O
-
Myxococcus xanthus 5'-AMP the reaction product, 5'-AMP, is further dephosphorylated to adenosine by PdeA and PdeB ?
additional information Myxococcus xanthus PdeA and PdeB, enzymes hydrolyze 3',5'- and 2',3'-cyclic AMP to adenosine, and also demonstrate phosphatase activity toward nucleoside 5'-tri-, 5'-di-, 5'- and 3'-monophosphates with highest activities for nucleoside 5'-monophosphates. PdeA and PdeB also show high phosphomonoesterase activities against 50-UMP, 3'-AMP, and 3'-GMP, low activities against 5'-dAMP, and no activities toward 2'-AMP and 2'-GMP Myxococcus xanthus ?
-
?

Synonyms

Synonyms Comment Organism
PdeA
-
Myxococcus xanthus
PdeB
-
Myxococcus xanthus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
the optimum temperatures for the 3',5'-cAMP phosphodiesterase activity of PdeA is 40°C Myxococcus xanthus
50
-
the optimum temperatures for the 3',5'-cAMP phosphodiesterase activity of PdeB is 50°C Myxococcus xanthus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50 55 heat treatment at 50°C or 55°C for 5 min slightly activates the phosphodiesterase activity of PdeB against 3',5'-cAMP by about 1.2fold of the control while PdeA activity is not activated by the heat treatment Myxococcus xanthus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00093
-
3',5'-cAMP PdeB, in 50 mM Tris-HCl, pH 8.0, 0.05 mM MnCl2, at 40°C Myxococcus xanthus
0.00096
-
3',5'-cAMP PdeA, in 50 mM Tris-HCl, pH 8.0, 0.05 mM MnCl2, at 40°C Myxococcus xanthus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8.5 PdeA and PdeB have slightly alkaline pH optima (pH 7.5-8.5) for 3',5'-cAMP hydrolysis in 0.1 M Tris-HCl buffer Myxococcus xanthus

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 7 PdeB shows no 3',5'-cAMP phosphodiesterase activity at or below pH 6.0, PdeA and PdeB activities are strongly inhibited by 0.1 M sodium phosphate buffer (pH 6.0 and 7.0) Myxococcus xanthus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.19
-
3',5'-cAMP PdeB, in 50 mM Tris-HCl, pH 8.0, 0.05 mM MnCl2, at 40°C Myxococcus xanthus
0.29
-
3',5'-cAMP PdeA, in 50 mM Tris-HCl, pH 8.0, 0.05 mM MnCl2, at 40°C Myxococcus xanthus