Title : Analysis of the HD-GYP domain cyclic dimeric GMP phosphodiesterase reveals a role in motility and the enzootic life cycle of Borrelia burgdorferi.

Pub. Date : 2011 Aug

PMID : 21670168






3 Functional Relationships(s)
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1 Here we demonstrate that BB0374/PdeB specifically hydrolyzed c-di-GMP with a K(m) of 2.9 nM, confirming that it is a functional phosphodiesterase. bis(3',5')-cyclic diguanylic acid phosphodiesterase 6B, cGMP, rod receptor, beta polypeptide Mus musculus
2 pdeB single mutant cells exhibit significantly increased flexing, indicating a role for c-di-GMP in motility. bis(3',5')-cyclic diguanylic acid phosphodiesterase 6B, cGMP, rod receptor, beta polypeptide Mus musculus
3 Identification of this role of pdeB increases our understanding of the c-di-GMP signaling network in motility regulation and the life cycle of B. burgdorferi. bis(3',5')-cyclic diguanylic acid phosphodiesterase 6B, cGMP, rod receptor, beta polypeptide Mus musculus