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. Author manuscript; available in PMC: 2014 Jun 18.
Published in final edited form as: Anal Chem. 2013 May 30;85(12):6136–6142. doi: 10.1021/ac401106e

Table 1.

Kinetic constants KM and Vmax for pTS13 dephosphorylation by recombinant PTPN1 and PTPN2 were determined by fitting the Michaelis-Menten equation to initial reaction rates obtained over a range of substrate concentrations. Kcat was calculated as Vmax/[E] where [E] is enzyme concentration.

Enzyme KM (nM) Vmax (nM s−1 ng−1) kcat (s−1)
PTPN1 770 ± 250 2.2 ± 0.25 21 ± 2.4
PTPN2 290 ± 54 3.1 ± 0.18 30 ± 1.7