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. 1999 Aug 31;96(18):10403–10408. doi: 10.1073/pnas.96.18.10403

Table 1.

Inhibition of proteasome catalytic activities

Compound kassociation = kobs/[I] (M−1s−1)
Chymotrypsin-like activity Trypsin-like activity PGPH activity
Epoxomicin 35,400  ±  1400 287  ±  71 34  ±  4.8
(40–80 nM) (6–10 μM) (25–75 μM)
clasto-lactacystin 8,530  ±  280 253  ±  41 37  ±  4.7
β-Lactone (200–400 nM) (6–10 μM) (25–75 μM)
NLVS 6,790  ±  919 5.3  ±  2.8 6.4  ±  2.3
(200–400 nM) (50–100 μM) (50–100 μM)

The rate of covalent inhibition (kassociation) of the three major proteasome catalytic activities were determined for epoxomicin, clasto-lactacystin β-lactone, and peptide vinyl sulfone, NLVS. A range of concentrations was used to determine the kassociation for inhibition of individual enzymatic activities.