[Hydrophobic interactions of serine proteases with low molecular weight compounds: partial effector displacement from the activated enzyme by the substrate].
1,2,3-tris-tri-beta-phenylethylaminopropane (a compound which can simultaneously interact with S1- and S2'-enzyme sites and has complicated grouping in the region analogous to "leaving group" of a substrate) has been studied for the effect on chymotriptic hydrolysis. Anomalously high inhibitory effect of some cumbersome organic compounds is explained on the base of the obtained data.
Verevka
S V
SV
Kolodzeĭskaia
M V
MV
D001665:Binding Sites / Q000187:drug effects; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D004789:Enzyme Activation / Q000187:drug effects; D006868:Hydrolysis; D015394:Molecular Structure; D008970:Molecular Weight; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology*; D012995:Solubility; D013379:Substrate Specificity; D014867:Water / Q000737:chemistry
D015842:Serine Proteinase Inhibitors; D014867:Water; D002918:Chymotrypsin
Gidrofobnye vzaimodeĭstviia serinovykh proteaz s nizkomolekuliarnymi soedineniiami: chastichnoe vytesnenie substratom éffektora iz aktivirovannogo fermenta.