| 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 17640875] |
|
| [EC 2.7.7.65 created 2008] |
| |
|
| |
|
Printable version