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Enzymatic characteristics of two novel Myxococcus xanthus enzymes, PdeA and PdeB, displaying 3′,5′‐ and 2′,3′‐cAMP phosphodiesterase, and phosphatase activities
Author(s) -
Kimura Yoshio,
Okazaki Nozomi,
Takegawa Kaoru
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.12.044
Subject(s) - myxococcus xanthus , phosphodiesterase , phosphatase , enzyme , biochemistry , nucleoside , chemistry , nucleotide , nucleotidase , nucleoside triphosphate , stereochemistry , biology , gene , mutant
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 Mn 2+ or Co 2+ . The K m 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).