Inhibitory effects of alcohols on the activity of human matrix metalloproteinase 7 (matrilysin).
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.
Muta
Yuko
Y
Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Oneda
Hiroshi
H
Inouye
Kuniyo
K
D000438:Alcohols / Q000494:pharmacology*; D001665:Binding Sites; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D020783:Matrix Metalloproteinase 7 / Q000737:chemistry; D061965:Matrix Metalloproteinase Inhibitors; D013329:Structure-Activity Relationship
D000438:Alcohols; D061965:Matrix Metalloproteinase Inhibitors; D020783:Matrix Metalloproteinase 7