The Two Deubiquitinating Enzymes from Chlamydia trachomatis have Distinct Ubiquitin Recognition Properties

Abstract

effective concentration. We find that phosphorylation kinetics scale with the length of the intrinsically disordered linkers that join the enzyme and substrate, but that the scaling differs between substrates. Steady-state kinetics only partially predict rates of tethered reactions as product release may obscure the rate of phospho-transfer. Our results suggest that changes in signalling complex architecture not only enhance the rates of phosphorylation reactions, but may also alter the relative substrate usage. This suggests a mechanism for how anchoring proteins can allosterically modify the output from a signalling pathway.