Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Kessin, R.H.; Franke, J.
    Secreted adenylate cyclase of Bordetella pertussis: calmodulin requirements and partial purification of two forms (1986), J. Bacteriol., 166, 290-296.
    View publication on PubMedView publication on EuropePMC

General Stability

EC Number General Stability Organism
4.6.1.1 iodination, inactivation of free enzyme, enzyme-calmodulin complex stable 2 months Bordetella pertussis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.6.1.1 1.9
-
 ATP whole cells Bordetella pertussis
4.6.1.1 2.4
-
 ATP high molecular weight form Bordetella pertussis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.6.1.1 extracellular
-
 Bordetella pertussis
-
-

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.1 Bordetella pertussis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.6.1.1 partial purification Bordetella pertussis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.6.1.1 culture supernatant
-
 Bordetella pertussis
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.6.1.1 1600
-
-
 Bordetella pertussis

Storage Stability

EC Number Storage Stability Organism
4.6.1.1 -80°C, 50 mM Tris-HCl, pH 8, 6 mM MgCl2, 0.1% Triton X-100, several weeks 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'-cAMP + diphosphate
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
4.6.1.1 Calmodulin activation Bordetella pertussis