[The nature of differences in amidase and esterase activities of some acyltrypsins].
Specific trypsin substrates (esters, anilides, amides, peptides) were shown to accelerate deacetylation of monoacetylated trypsin. The amidase activity of monoacetyl-, monopropyonyl-, and tetraformyl-trypsin was not manifested if the amidase activity of native enzyme was suppressed in these preparations by the ester substrates (benzoylarginine ethyl ester or p-nitrophenyl acetate). Therefore the differences in the residual amidase and esterase activities of these acylated trypsin preparations found earlier did not contradict the universality of the acylenzyme mechanism. These differences are due to the strong deacylating effect of specific substrate in its complex with the enzyme modified with nonspecific acyl residue. The latter fact is suggested to be an experimental confirmation of the "induced fit" hypothesis.
D000581:Amidohydrolases / Q000378:metabolism; D001120:Arginine / Q000494:pharmacology / Q000031:analogs & derivatives; D004950:Esterases / Q000378:metabolism; D009578:Nitrobenzenes / Q000494:pharmacology; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000378:metabolism*; D014361:Trypsin Inhibitors / Q000494:pharmacology
D009578:Nitrobenzenes; D014361:Trypsin Inhibitors; D001120:Arginine; C009727:benzoylarginine ethyl ester; D004950:Esterases; D014357:Trypsin; D000581:Amidohydrolases
Priroda Razlichii V Velichinalh Amidaznoi I Zsteraznoi Aktivnostei Nekotorykh Atsiltripsinob