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Literature summary for 4.6.1.1 extracted from
- Protein-protein docking and analysis reveal that two homologous bacterial adenylyl cyclase toxins interact with calmodulin differently (2008), J. Biol. Chem., 283, 23836-23845.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Calmodulin | activates, the N-terminal portion of CaM binds to the beta-hairpin region in the CA domain of CyaA, interaction mode, structure analysis of the calmodulin-CyaA complex and interface, and mechanism of catalytic activation, detailed overview. The N-terminus of CaM is linked to the C-terminus of CaM by a flexible linker with a defined degree of freedom. The potency of CaM D50C mutant to activate CyaA is enhanced about 10fold, mutants T26C or T41C | Bordetella pertussis |  |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A225C | a CyaA 1-373 mutant | Bordetella pertussis |
| A94C | a CyaA 1-373 mutant | Bordetella pertussis |
| additional information | upon insertion of the N-terminal adenylyl cyclase domain of Bordetella pertussis CyaA to its targeted eukaryotic cells, target cell calmodulin binds to this domain tightly with high affinity, the interaction activates the adenylyl cyclase activity of CyaA leading to a rise in intracellular cAMP levels to disrupt normal cellular signaling, the complex formation between N-CaM and CyaA contributes a 400fold increase of binding affinity between CyaA and CaM | Bordetella pertussis |
| Q260A/R262A | a CyaA 1-373 mutant, the mutant shows reduced calmodulin-dependent activation of CyaA compared to the wild-type CyaA | Bordetella pertussis |
| Q260C | the mutant shows about 1000fold reduced potency to be activated by calmodulin compared to the wild-type CyaA | Bordetella pertussis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state FRET experiments of wild-type and mutant enzyme and calmodulin, overview | Bordetella pertussis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the toxin is secreted | Bordetella pertussis | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates | Bordetella pertussis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP | Bordetella pertussis | - |
3',5'-cyclic-AMP + diphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bordetella pertussis | P0DKX7 | gene cyaA | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP | - |
Bordetella pertussis | 3',5'-cyclic-AMP + diphosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| adenylyl cyclase toxin | - |
Bordetella pertussis |
| CyaA | - |
Bordetella pertussis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Bordetella pertussis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Bordetella pertussis |
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