Abstract
The three methionine residues of subtilisin DY were specifically modified into methionine sulfoxide using increasing amounts of chloramine T. By means of subsequent treatment with cyanogen bromide, gel chromatography, Edman degradation of the obtained peptides and the known structure of subtilisin DY it was established that Met222 is exposed to the surrounding solution, Met124 is partially exposed and Met199 is buried. The data obtained were confirmed on a computer graphics space movable model of subtilisin Carlsberg where Met222 was seen to be on the surface of the molecule and Met199 shielded by Tyr262, Ala179 and Leu196. Upon oxidation of Met222 of subtilisin DY by chloramine T, 25% of its caseinolytic activity was lost. This can be explained by the immediate adjacency to the active-site Ser221. An additional 5% loss of activity was observed at each subsequent methionine modification.
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