Sandbox Reserved 1070: Difference between revisions
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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 substrate GTP to allow for deprotonation of the C3 -OH groups of the ribose. The negatively charged Oxygens on the phosphate groups of GTP are stabilized by Mg2+ ions. | ||
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. | ||
