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• W1963525436 endingPage "1942" @default.
• W1963525436 startingPage "1935" @default.
• W1963525436 abstract "A series of 4H-3,1-benzoxazin-4-ones is reported that inhibit the serine proteases human cathepsin G and bovine chymotrypsin. The synthesis and kinetic parameters of the alkaline hydrolysis is described. These compounds act as acyl-enzyme inhibitors of both enzymes. The reaction of cathepsin G with 2-benzylamino-4H-3,1-benzoxazin-4-one (20) was studied in detail. A partition in deacylation of the initially formed acyl-enzyme was observed, leading to the formation of 2-(3-benzylureido)benzoic acid (26) and 3-benzylquinazoline-2,4-(1H,3H)-dione (27). A 6-methyl substitution strongly increased the acylation rate of both proteases. Introduction of an aryl moiety into the 2-substituent led to compounds with Ki values towards cathepsin G in the nanomolar range. Their inhibitory potency is stronger than that of other synthetic inhibitors of cathepsin G." @default.
• W1963525436 created "2016-06-24" @default.
• W1963525436 creator A5036207297 @default.
• W1963525436 creator A5085085591 @default.
• W1963525436 date "1997-10-01" @default.
• W1963525436 modified "2023-09-27" @default.
• W1963525436 title "Inhibition of cathepsin G by 4H-3,1-benzoxazin-4-ones" @default.
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• W1963525436 doi "https://doi.org/10.1016/s0968-0896(97)00128-4" @default.
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