The Enzyme Database

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EC 2.7.7.65     
Accepted name: diguanylate cyclase
Reaction: 2 GTP = 2 diphosphate + cyclic di-3′,5′-guanylate
For diagram of cyclic di-3′,5′-guanylate biosynthesis and breakdown, click here
Glossary: cyclic di-3′,5′-guanylate = c-di-GMP = c-di-guanylate = cyclic-bis(3′→5′) dimeric GMP
Other name(s): DGC; PleD
Systematic name: GTP:GTP guanylyltransferase (cyclizing)
Comments: A GGDEF-domain-containing protein that requires Mg2+ or Mn2+ for activity. The enzyme can be activated by BeF3, a phosphoryl mimic, which results in dimerization [3]. Dimerization is required but is not sufficient for diguanylate-cyclase activity [3]. Cyclic di-3′,5′-guanylate is an intracellular signalling molecule that controls motility and adhesion in bacterial cells. It was first identified as having a positive allosteric effect on EC 2.4.1.12, cellulose synthase (UDP-forming) [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 146316-82-7
References:
1.  Ryjenkov, D.A., Tarutina, M., Moskvin, O.V. and Gomelsky, M. Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain. J. Bacteriol. 187 (2005) 1792–1798. [PMID: 15716451]
2.  Méndez-Ortiz, M.M., Hyodo, M., Hayakawa, Y. and Membrillo-Hernández, J. Genome-wide transcriptional profile of Escherichia coli in response to high levels of the second messenger 3′,5′-cyclic diguanylic acid. J. Biol. Chem. 281 (2006) 8090–8099. [PMID: 16418169]
3.  Paul, R., Abel, S., Wassmann, P., Beck, A., Heerklotz, H. and Jenal, U. Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization. J. Biol. Chem. 282 (2007) 29170–29177. [PMID: 17640875]
[EC 2.7.7.65 created 2008]
 
 


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