Article
Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation.
The Journal of biological chemistry - 7 Jul 2006
Wang Qiuyan, Yang Guangyu, Liu Yanli, Feng Yan
Abstract excerpt
It has been shown that highly conserved residues that form crucial structural elements of the catalytic apparatus may be used to account for the evolutionary history of enzymes. Using saturation mutagenesis, we investigated the role of a conserved residue (Arg(526)) at the active site of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 in substrate discrimination and catalytic mechanism. This...
Topics
- Aeropyrum
- Archaeal Proteins
- Binding Sites
- Enzyme Activation
- Esterases
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Peptide Hydrolases
- Structure-Activity Relationship
- Substrate Specificity