Diadenylate cyclase EC 2.7.7.85, DNA integrity scanning protein DisA is a DNA binding protein[1] participates in a DNA-damage check-point. DisA forms globular foci that rapidly scan along the chromosomes searching for lesions. Catalytic activity
| diadenylate cyclase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Diadenylate cyclase homooctamer, Thermotoga maritima | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.7.85 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- 2 ATP 2 diphosphate + cyclic di-3',5'-adenylate.
This enzyme has diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP likely acts as a signaling molecule that may couple DNA integrity with a cellular process. This rate-limiting step is the accessibility of the active site; mutating the possible exit tunnel (residues 128-130) increases product 2-fold despite Arg-130 being important for ATP-binding. Does not convert GTP to c-di-GMP.
References
edit- ^ Witte G, Hartung S, Büttner K, Hopfner KP (April 2008). "Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates". Molecular Cell. 30 (2): 167–78. doi:10.1016/j.molcel.2008.02.020. PMID 18439896.
