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. Author manuscript; available in PMC: 2026 Feb 7.
Published in final edited form as: Biochemistry. 2025 Nov 25;64(24):4661–4674. doi: 10.1021/acs.biochem.5c00539

Figure 2.

Figure 2.

Steady-state and pre-steady kinetics of PTP1B. (A) Steady-state (left) and stopped-flow (right) experiments were performed for WT and allosteric mutants with pNPP as the substrate. (B) Progress curves representing the formation of dephosphorylated peptides as a function of time with WT PTP1B. Black lines are the non-linear least squares fit to the gray data points. The peptide sequences are shown at the top of each panel. Identical experiments for the mutants are shown in the SI.