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Phosphodiesterases with EAL domains are enzymes that catalyze the hydrolysis of the bacterial second messenger cyclic di-GMP (c-di-GMP), which plays a crucial role in regulating bacterial behaviors such as motility, biofilm formation, and virulence. These enzymes are part of the larger family of diguanylate cyclases and phosphodiesterases that together modulate c-di-GMP levels within the cell, influencing various physiological processes in bacteria. The EAL domain is a conserved sequence motif found in these phosphodiesterases, which is essential for their catalytic activity and substrate binding. Mutations in the EAL domain, particularly in regions like loop 6, can significantly affect enzyme activity and substrate interaction, highlighting the domain's importance in bacterial signaling pathways.
Hydrolysis of cyclic di-GMP to linear pGpG, thus regulating bacterial behaviors such as biofilm formation and motility.
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