EC Number   |
Reaction |
Reference |
|---|
   3.4.21.53 | hydrolysis of proteins in presence of ATP |
active site consists of catalytic Ser-Lys-Asp residues. Charged Lys-593 assists in lowering the pKa of the Ser550 hydroxyl group, and the water in the cavity acts as a proton acceptor during catalysis |
669297 |
| 3.4.21.53 | hydrolysis of proteins in presence of ATP |
active site contains a Ser-Lys dyad |
668464 |
| 3.4.21.53 | hydrolysis of proteins in presence of ATP |
binding of ATP induces a conformational change that facilitates the coupling of nucleotide hydrolysis with peptide substrate delivery to the peptidase activs site |
667610 |
| 3.4.21.53 | hydrolysis of proteins in presence of ATP |
hydrolysis of proteins in presence of ATP, mechanism |
29344, 29346, 29347, 29360, 29361 |
| 3.4.21.53 | hydrolysis of proteins in presence of ATP |
pre-steady state kinetic characterization. ATP hydrolysis occurs before peptide cleavage, with the former displaying a burst and the latter displaying a lag in the product production. ATP hydrolysis is used to generate an active enzyme that hydrolyzes peptide |
667645 |
| 3.4.21.53 | hydrolysis of proteins in presence of ATP |
presence of a catalytic Ser-Lys dyad. Definition of two enzyme subfamilies LonA and LonB, based on the consensus sequences in the active site of the proteolytic domain |
668465 |
| 3.4.21.53 | hydrolysis of proteins in presence of ATP |
proteolysis mechanism, overview |
755395 |
| 3.4.21.53 | hydrolysis of proteins in presence of ATP |
reaction may involve a substrate translocation step limiting the turnover rate |
696457 |
