An HD-GYP Cyclic Di-Guanosine Monophosphate Phosphodiesterase with a Non-Heme Diiron鈥揅arboxylate Active Site

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• 作者：Kyle D. Miner ; Karl E. Klose ; Donald M. Kurtz ; Jr.
• 刊名：Biochemistry
• 出版年：2013
• 出版时间：August 13, 2013
• 年：2013
• 卷：52
• 期：32
• 页码：5329-5331
• 全文大小：203K
• 年卷期：v.52,no.32(August 13, 2013)
• ISSN：1520-4995

文摘

The intracellular level of the ubiquitous bacterial secondary messenger, cyclic di-(3鈥?5鈥?-guanosine monophosphate (c-di-GMP), represents a balance between its biosynthesis and degradation, the latter via specific phosphodiesterases (PDEs). One class of c-di-GMP PDEs contains a characteristic HD-GYP domain. Here we report that an HD-GYP PDE from Vibrio cholerae contains a non-heme diiron鈥揷arboxylate active site, and that only the reduced form is active. An engineered D-to-A substitution in the HD dyad caused loss of c-di-GMP PDE activity and of two iron atoms. This report constitutes the first demonstration that a non-heme diiron鈥揷arboxylate active site can catalyze the c-di-GMP PDE reaction and that this activity can be redox regulated in the HD-GYP class.