. Author manuscript; available in PMC: 2009 Nov 1.

Published in final edited form as: Biochem J. 2008 Nov 1;415(3):367–375. doi: 10.1042/BJ20080779

Table 1. Comparison of catalytic rates on an optimal tetrapeptide substrate.

Data represent the mean and standard deviation of at least triplicate experiments. Substrate concentration 1–100 µM, final enzyme concentration 0.5–4 µM based on total protein concentration. Note that PLpro is substantially more active than the other DUBs on the peptide substrate.

k_cat/K_m (M⁻¹s¹) Ac-LRGG-AFC
OTU-1	PLpro	UCH-L3	IsoT
12.3 ± 0.5	408.2 ± 20	2.4 ±0.1	14.3 ± 3.2