Literature summary for 4.6.1.1 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Bacillus anthracis

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Organism

Organism	UniProt	Comment	Textmining
Bacillus anthracis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Bacillus anthracis

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
Edema factor	-	Bacillus anthracis

pH Optimum

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

Ki Value [mM]

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

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Release 2023.1 (January 2023)