Article
The role of cysteine 41 in the enzymatic activities of the pertussis toxin S1 subunit as investigated by site-directed mutagenesis.
The Journal of biological chemistry - 15 Mar 1990
Locht C, Lobet Y, Feron C, Cieplak W, Keith J M
Abstract excerpt
The S1 subunit (Mr 28,000) of pertussis toxin expresses thiol-dependent enzymatic ADP-ribosyltransferase and NAD-glycohydrolase activities. Site-directed mutagenesis experiments were performed on the codon for Cys-41 of this subunit to investigate the role of this residue in both enzymatic activities. Deletion of Cys-41 caused a decrease in both activities below detectable levels, whereas replacement of this...
Topics
- Adenosine Triphosphate
- Base Sequence
- Binding Sites
- Catalysis
- Cholic Acids
- Cloning, Molecular
- Codon
- Cysteine
- Dithiothreitol
- Escherichia coli
- Kinetics