Small-molecule inhibitor: TLCK

Name

History: TLCK was described as an inhibitor of trypsin by Shaw et al. (1965).
Peptidases inhibited: TLCK inhibits many serine and cysteine peptidases. The serine peptidases are especially those with trypsin-like specificity. Peptidases inhibited include trypsin, subtilisin: Poulos et al., 1976) and oligopeptidase B: Morty et al., 2000). Cysteine peptidases that are inhibited include papain: Whitaker & Perez-Villasenor, 1968) and clostripain: Gilles & Keil, 1984). Significant reactions with thiol groups of non-peptidase proteins have also been described (e.g. Stöppler et al., 1996).
Mechanism: Inhibition is initially reversible and then becomes irreversible (see Class). TLCK provided early evidence of the presence of histidine in the active site of trypsin (Shaw et al., 1965).

CID at PubChem: 73094
ChEBI: 580921
Structure
Formula weight: 333
Related inhibitors: Many other halomethylketones have been evaluated as peptidase inhibitors (see Reviews).

Stability: Likely to be destroyed by reaction with small-molecule thiol compounds.

Inhibitor class: This compound is of the halomethylketone class of peptidase inhibitors. Such compounds are activated ketones that inhibit a variety of serine, cysteine and threonine peptidases.The halomethylketones have been reviewed by Powers et al. (2002), pp. 4646 - 4656.
Reviews: Powers et al., 2002, pp. 4646 - 4656.