The EAL Domain Protein VieA Is a Cyclic Diguanylate Phosphodiesterase

摘要: The newly recognized bacterial second messenger 3′,5′-cyclic diguanylic acid (cyclic diguanylate (c-di-GMP)) has been shown to regulate a wide variety of behaviors and traits. Biosynthesis degradation c-di-GMP have attributed the GGDEF EAL protein domains, respectively, based primarily on genetic evidence. Whereas domain was demonstrated possess cyclase activity in vitro, not tested directly for phosphodiesterase activity. This study describes analysis hydrolysis by an purified system. Vibrio cholerae VieA inversely biofilm-specific genes (vps) virulence (ctxA), presumably decreasing cellular pool c-di-GMP. maximally active at neutral pH, physiological ionic strength, ambient temperatures hydrolytic with Km 0.06 μm. unable hydrolyze cGMP. putative metal coordination site domain, Glu170, be necessary Furthermore, divalent cations Mg2+ Mn2+ were activity; conversely, Ca2+ Zn2+ potent inhibitors phosphodiesterase. Calcium inhibition provides potential mechanism regulation degradation.