两种新型黄色粘球菌酶PdeA和PdeB的酶学特性，它们具有3',5'-和2',3'-环磷酸腺苷磷酸二酯酶以及磷酸酶活性。

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

作者信息

Kimura Yoshio, Okazaki Nozomi, Takegawa Kaoru

机构信息

Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, Miki-cho, Kagawa, Japan.

出版信息

FEBS Lett. 2009 Jan 22;583(2):443-8. doi: 10.1016/j.febslet.2008.12.044. Epub 2008 Dec 27.

DOI:10.1016/j.febslet.2008.12.044

PMID:19114044

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 microM 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 microM).

摘要

黄色粘球菌的PdeA和PdeB是与III类3'，5'-环核苷酸磷酸二酯酶同源的酶，它们将3'，5'-和2'，3'-环磷酸腺苷（cAMP）水解为腺苷，并且对核苷5'-三磷酸、5'-二磷酸、5'-单磷酸和3'-单磷酸也表现出磷酸酶活性，对核苷5'-单磷酸的活性最高。PdeA和PdeB的底物特异性与任何已知的环核苷酸单磷酸磷酸二酯酶、核苷酸酶或磷酸酶均无相似性。PdeA和PdeB的酶活性受到50微摩尔的锰离子（Mn(2+)）或钴离子（Co(2+)）的刺激。PdeA和PdeB对3'，5'-cAMP、2'，3'-cAMP、5'-ATP和5'-AMP的米氏常数（K(m)）处于低微摩尔范围（1.4 - 12.5微摩尔）。