Biochemical Properties of a cAMP Phosphodiesterase in the Cyanobacterium Anabaena sp. strain PCC 7120

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概要

• 論文の詳細を見る

• rights: 日本微生物生態学会rights: 本文データは学協会の許諾に基づきCiNiiから複製したものであるrelation: IsVersionOf: http://ci.nii.ac.jp/naid/110001282480/A gene for cAMP phosphodiesterase, designated cpdA, was identified in the nitrogen-fixing cyanobacterium Anabaena sp. PCC 7120. The predicted amino acid sequence of the gene was similar to the sequences of cAMP phosphodiesterases from Thermosynechococcus elongatus, Escherichia coli and Haemophilus influenzae. The recombinant protein was purified by sequential column chromatography and its biochemical properties were determined. The Anabaena cAMP phosphodiesterase hydrolyzed cAMP and cGMP with similar levels of activity. The K_m value for cAMP was 45μM and the Vmax was 4.9μmol min^<-1> mg protein^<-1>. These values are similar to those of Escherichia coli cAMP phosphodiesterase. The enzyme was activated by divalent cations such as Fe^<2+> and Mn^<2+>. The tertiary structure of this enzyme was predicted by homology modeling. The deduced structure has two metal-binding sites in the catalytic domain.

• 日本微生物生態学会の論文

著者

• Ohmori Masayuki

  Graduate School Of Sci. And Technol. Saitama Univ.

• Ohmori Masayuki

  Department Of Biological Sciences Faculty Of Science And Engineering Chuo University

• Fujisawa Takatomo

  Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo

• Fujisawa Takatomo

  Department Of Life Sciences Graduate School Of Arts And Sciences The University Of Tokyo

• Ohmori Masayuki

  Department Of Biochemistry And Molecular Biology Faculty Of Science Saitama University

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