Inhibitory Effects of Alcohols on the Activity of Human Matrix Metalloproteinase 7 (Matrilysin)

Abstract

Aliphatic alcohols inhibited the activity of human matrix metalloproteinase 7 (matrilysin) competitively with K_i of 6.1–19.4% (v/v) or 0.66–4.80 M. From the relationship between the structures of alcohols and their K_i values, alcohols are considered to bind the hydrophobic S1′ subsite most plausibly, and the size of the pocket was estimated to be large enough to accommodate the length of 1-butanol (4-carbon chain) and the bulk of tertiary alcohols. Alcohols might be suitable probes for exploring the active-site geometry of enzymes.