Enzymatic characteristics of two novel Myxococcus xanthus enzymes, PdeA and PdeB, displaying 3′,5′- and 2′,3′-cAMP phosphodiesterase, and phosphatase activities

Yoshio Kimura, Nozomi Okazaki, Kaoru Takegawa

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Myxococcus xanthus PdeA and PdeB, enzymes homologous to class III 3′,5′-cyclic nucleotide phosphodiesterases, hydrolyzed 3′,5′- and 2′,3′-cyclic AMP (cAMP) to adenosine, and also demonstrated phosphatase activity toward nucleoside 5′-tri-, 5′-di-, 5′- and 3′-monophosphates with highest activities for nucleoside 5′-monophosphates. The substrate specificities of PdeA and PdeB show no similarity to that of any known cNMP phosphodiesterase, nucleotidase, or phosphatase. The enzyme activities of PdeA and PdeB were stimulated by 50 μM Mn2+ or Co2+. The Km values of PdeA and PdeB for 3′,5′-cAMP, 2′,3′-cAMP, 5′-ATP, and 5′-AMP were in the low micromolar range (1.4-12.5 μM).

Original languageEnglish
Pages (from-to)443-448
Number of pages6
JournalFEBS Letters
Volume583
Issue number2
DOIs
Publication statusPublished - Jan 22 2009

Fingerprint

Myxococcus xanthus
5'-Nucleotidase
Phosphoric Diester Hydrolases
Phosphoric Monoester Hydrolases
Cyclic AMP
nucleotidase
Nucleosides
Enzymes
Cyclic Nucleotides
Enzyme activity
Adenosine Monophosphate
Substrate Specificity
Adenosine
Adenosine Triphosphate
Substrates

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

Cite this

Enzymatic characteristics of two novel Myxococcus xanthus enzymes, PdeA and PdeB, displaying 3′,5′- and 2′,3′-cAMP phosphodiesterase, and phosphatase activities. / Kimura, Yoshio; Okazaki, Nozomi; Takegawa, Kaoru.

In: FEBS Letters, Vol. 583, No. 2, 22.01.2009, p. 443-448.

Research output: Contribution to journalArticle

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