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Literature summary extracted from

  • Selwa, E.; Davi, M.; Chenal, A.; Sotomayor-Perez, A.C.; Ladant, D.; Malliavin, T.E.
    Allosteric activation of Bordetella pertussis adenylyl cyclase by calmodulin: molecular dynamics and mutagenesis studies (2014), J. Biol. Chem., 289, 21131-21141.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.6.1.1 Calmodulin maximal activity at 0.001 mM Bordetella pertussis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.6.1.1 expressed in Escherichia coli BLR and KRX cells Bordetella pertussis

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.1 N347A the mutant shows an enzymatic activity that is reduced by about half as well as 5fold reduced affinity for calmodulin Bordetella pertussis
4.6.1.1 R338A/D360A the mutant shows no affected catalytic efficiency but 6fold reduced affinity for calmodulin Bordetella pertussis
4.6.1.1 R338A/N347A/D360A the mutant shows 15% of wild type turnover and exhibits 200fold reduced affinity for calmodulin Bordetella pertussis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.6.1.1 0.6
-
ATP wild type enzyme, at pH 8.0 and 30°C Bordetella pertussis
4.6.1.1 1.5
-
ATP mutant enzyme R338A/D360A, at pH 8.0 and 30°C Bordetella pertussis
4.6.1.1 2.2
-
ATP mutant enzyme N347A, at pH 8.0 and 30°C Bordetella pertussis
4.6.1.1 3
-
ATP mutant enzyme R338A/D360A, at pH 8.0 and 30°C Bordetella pertussis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.6.1.1 50000
-
x * 50000, SDS-PAGE 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
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.6.1.1 DEAE-Sepharose column chromatography Bordetella pertussis

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
-
?

Subunits

EC Number Subunits Comment Organism
4.6.1.1 ? x * 50000, SDS-PAGE Bordetella pertussis

Synonyms

EC Number Synonyms Comment Organism
4.6.1.1 AC1
-
Bordetella pertussis
4.6.1.1 adenylyl cyclase
-
Bordetella pertussis
4.6.1.1 Cya
-
Bordetella pertussis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.6.1.1 650
-
ATP mutant enzyme R338A/D360A, at pH 8.0 and 30°C Bordetella pertussis
4.6.1.1 2250
-
ATP mutant enzyme N347A, at pH 8.0 and 30°C Bordetella pertussis
4.6.1.1 4600
-
ATP wild type enzyme, at pH 8.0 and 30°C Bordetella pertussis
4.6.1.1 6000
-
ATP mutant enzyme R338A/D360A, at pH 8.0 and 30°C Bordetella pertussis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.6.1.1 200
-
ATP mutant enzyme R338A/D360A, at pH 8.0 and 30°C Bordetella pertussis
4.6.1.1 1000
-
ATP mutant enzyme N347A, at pH 8.0 and 30°C Bordetella pertussis
4.6.1.1 4000
-
ATP mutant enzyme R338A/D360A, at pH 8.0 and 30°C Bordetella pertussis
4.6.1.1 7600
-
ATP wild type enzyme, at pH 8.0 and 30°C Bordetella pertussis