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

BRENDA support

Literature summary extracted from

  • Gupta, M.; Alam, S.; Bhatnagar, R.
    Kinetic characterization and ligand binding studies of His351 mutants of Bacillus anthracis adenylate cyclase (2006), Arch. Biochem. Biophys., 446, 28-34.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.6.1.1 expression in Escherichia coli Bacillus anthracis

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.1 H351A mutant with no enzyme activity Bacillus anthracis
4.6.1.1 H351F mutant with 40fold decreased enzyme activity Bacillus anthracis
4.6.1.1 H351N mutant with 34fold decreased enzyme activity Bacillus anthracis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.6.1.1 3'-dATP competitive inhibition Bacillus anthracis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.6.1.1 0.14
-
 ATP wild type, pH 8.0, 25°C Bacillus anthracis
4.6.1.1 0.17
-
 ATP mutant H351N, pH 8.0, 25°C Bacillus anthracis
4.6.1.1 0.19
-
 ATP mutant H351F, pH 8.0, 25°C Bacillus anthracis

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.1 Bacillus anthracis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.6.1.1
-
 Bacillus anthracis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.1 ATP
-
 Bacillus anthracis 3',5'-cAMP + diphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.6.1.1 Edema factor
-
 Bacillus anthracis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6.1.1 8
-
 wild type and mutants H351A, H351N, H351F Bacillus anthracis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.6.1.1 0.104
-
 3'-dATP wild type Bacillus anthracis
4.6.1.1 0.132
-
 3'-dATP mutant H351N Bacillus anthracis
4.6.1.1 0.146
-
 3'-dATP mutant H351F Bacillus anthracis