Enzymatic characteristics of two novel Myxococcus xanthus enzymes, PdeA and PdeB, displaying 3′,5′- and 2′,3′-cAMP phosphodiesterase, and phosphatase activities
Enzymatic characteristics of two novel Myxococcus xanthus enzymes, PdeA and PdeB, displaying 3′,5′- and 2′,3′-cAMP phosphodiesterase, and phosphatase activities
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DOI：
10.1016/j.febslet.2008.12.044
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发表时间：
2009-01-22
期刊：
影响因子：
3.5
通讯作者：
Takegawa, Kaoru
中科院分区：
文献类型：
--
作者：
Kimura, Yoshio;Okazaki, Nozomi;Takegawa, Kaoru
黄色粘球菌 PdeA 和 PdeB 是与 III 类 3',5'-环核苷酸磷酸二酯酶同源的酶，可将 3',5'- 和 2',3'-环 AMP (cAMP) 水解为腺苷，并且还表现出对核苷 5'-三-、5'-二-、5'- 和 3'- 单磷酸的磷酸酶活性，其中活性最高核苷5'-单磷酸。 PdeA 和 PdeB 的底物特异性与任何已知的 cNMP 磷酸二酯酶、核苷酸酶或磷酸酶没有相似之处。 50 μM Mn(2+) 或Co(2+) 刺激PdeA 和PdeB 酶活性。 3',5'-cAMP、2',3'-cAMP、5'-ATP 和 5'-AMP 的 PdeA 和 PdeB 的 K(m) 值在低微摩尔范围内 (1.4-12.5 μM)。 (C) 2008 年欧洲生化学会联合会。由 Elsevier B.V 出版。保留所有权利。
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 mu M 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 mu M). (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.