Article
Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli.
The Journal of biological chemistry - 25 Nov 1994
Singh S K, Maurizi M R
Abstract excerpt
ClpA, the regulatory subunit of Clp protease from Escherichia coli, has two ATP-binding sites in non-homologous regions of the protein, referred to as domain I and domain II. We have mutated the invariant lysine in the ATP-binding sites of domain I and domain II and studied the enzymatic properti...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Amino Acid Sequence
- Base Sequence
- Binding Sites
- Endopeptidase Clp
- Escherichia coli
- Escherichia coli Proteins
- Hydrolysis
- Molecular Sequence Data
- Mutation
- Oligodeoxyribonucleotides
- Oligopeptides
- Serine Endopeptidases