Sandbox Reserved 1070: Difference between revisions
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== Mechanism of Action == | == Mechanism of Action == | ||
Diguanylate cyclases only function efficiently as dimers, to bind both GGDEF domains holding the substrates. The presence of Zinc disrupts the ability of the two domains to overlap. | Diguanylate cyclases only function efficiently as dimers, to bind both GGDEF domains holding the substrates. The presence of Zinc disrupts the ability of the two domains to overlap. | ||
1. The enzyme coordinates the deprotonation of the C3 -OH groups of the ribose of GTP. | |||
1. The enzyme coordinates the deprotonation of the C3 -OH groups of the ribose of GTP. | |||
2. The deprotonated Oxygen then acts as a nucleophile to attack the 𝝰phosphate of GTP. | 2. The deprotonated Oxygen then acts as a nucleophile to attack the 𝝰phosphate of GTP. | ||
3. The β and γ phosphates of GTP are kicked off to form c-di-GMP. | 3. The β and γ phosphates of GTP are kicked off to form c-di-GMP. | ||
