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Literature summary for 4.6.1.1 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

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

Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]

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

Molecular Weight [Da]

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
AC1
-
Bordetella pertussis
adenylyl cyclase
-
Bordetella pertussis
Cya
-
Bordetella pertussis

Turnover Number [1/s]

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

kcat/KM [mM/s]

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