Kinetics of peptide cleavage
We detected burst and lag kinetics in the pre-steady state time courses of ATP and
peptide hydrolysis, respectively. The activation of peptidase activity in Lon is coordinated
with the build up of an enzyme intermediate formed after ATP hydrolysis.
Read more.
Pre-steady state kinetic analysis shows that ATP hydrolysis occurs before peptide
cleavage, providing support for the existence of an ATPase-coupled peptide
Substrate delivery step prior to peptide cleavage:
E. coli Lon adopted a “closed conformation” when bound to adenine nucleotide;
but this conformational change alone cannot activate the peptidase activity of Lon.
Furthermore, the chemical structure of the nucleotide base dictates the affinity Lon
for the nucleotide.
Read more.
 | 
