Diguanylate Cyclase
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Diguanylate Cyclase
In enzymology, diguanylate cyclase, also known as diguanylate kinase (), is an enzyme that catalysis, catalyzes the chemical reaction: 2 Guanosine triphosphate ↔ 2 diphosphate + cyclic di-3',5'-guanylate The Substrate (biochemistry), substrates of diguanylate cyclases (DGCs) are two molecules of guanosine triphosphate (GTP) and the product (biochemistry), products are two molecules of diphosphate and one molecule of cyclic di-3’,5’-guanylate (cyclic di-GMP). Degradation of cyclic di-GMP to guanosine monophosphate (GMP) is catalyzed by a phosphodiesterase (PDE). Structure Diguanylate cyclases are characterized by the conserved amino acid sequence motifs “GGDEF domain, GGDEF” (Gly-Gly-Aspartic acid, Asp-Glutamic acid, Glu-Phenylalanine, Phe) or “GGEEF” (Gly-Gly-Glu-Glu-Phe), which constitute the protein domain, domain of the DGC active site. These domains are often found coupled to other signaling domains within multidomain proteins. Often, GGDEF domains with DGC ...
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C-di-GMP
Cyclic di-GMP (also called cyclic diguanylate and c-di-Guanosine monophosphate, GMP) is a second messenger used in signal transduction in a wide variety of bacteria. Cyclic di-GMP is not known to be used by archaea, and has only been observed in eukaryotes in ''Dictyostelium''. The biological role of cyclic di-GMP was first uncovered when it was identified as an allosteric activator of a cellulose synthase found in ''Gluconacetobacter xylinus'' in order to produce microbial cellulose. In structure, it is a cycle containing only two guanine bases linked by ribose and phosphate. Contact with surfaces increases c-di-GMP which increases gene transcription, transcription, gene translation, translation, and Post-translational modification, post translation of exopolysaccharides (EPSs) and other extracellular polymeric substance matrix components (see the review by Jenal et al 2017). In bacteria, certain signals are communicated by synthesizing or degrading cyclic di-GMP. Cyclic di-GMP i ...
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