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Literature summary extracted from

  • Guo, Q.; Jureller, J.E.; Warren, J.T.; Solomaha, E.; Florian, J.; Tang, W.J.
    Protein-protein docking and analysis reveal that two homologous bacterial adenylyl cyclase toxins interact with calmodulin differently (2008), J. Biol. Chem., 283, 23836-23845.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.6.1.1 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

EC Number Protein Variants Comment Organism
4.6.1.1 A225C a CyaA 1-373 mutant Bordetella pertussis
4.6.1.1 A94C a CyaA 1-373 mutant Bordetella pertussis
4.6.1.1 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
4.6.1.1 Q260A/R262A a CyaA 1-373 mutant, the mutant shows reduced calmodulin-dependent activation of CyaA compared to the wild-type CyaA Bordetella pertussis
4.6.1.1 Q260C the mutant shows about 1000fold reduced potency to be activated by calmodulin compared to the wild-type CyaA Bordetella pertussis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.6.1.1 additional information
-
 additional information steady-state FRET experiments of wild-type and mutant enzyme and calmodulin, overview Bordetella pertussis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.6.1.1 extracellular the toxin is secreted Bordetella pertussis
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.6.1.1 Ca2+ activates Bordetella pertussis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.6.1.1 ATP Bordetella pertussis
-
 3',5'-cyclic-AMP + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.1 Bordetella pertussis P0DKX7 gene cyaA
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.1 ATP
-
 Bordetella pertussis 3',5'-cyclic-AMP + diphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.6.1.1 adenylyl cyclase toxin
-
 Bordetella pertussis
4.6.1.1 CyaA
-
 Bordetella pertussis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.6.1.1 30
-
 assay at Bordetella pertussis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6.1.1 7.2
-
 assay at Bordetella pertussis