title: [Theoretical aspects of the mechanism of proteolytic enzyme action. V. C-terminal specificity of serine proteinases].
abstract: Tetrahedral intermediates of the alpha-chymotrypsin acylation by N-protected amide dipeptide substrates having different leaving groups were analyzed by means of the molecular mechanic method. A predominant role of the C-terminal interactions in the leaving group protonation and in the development of a kinetic specificity was determined. The kinetic specificity of serine proteases was shown to be controlled by the transformation of various forms of tetrahedral substrate intermediates at the presteady stage.
authors.forename: S L
authors.initials: SL
authors.lastname: Aleksandrov
mesh_terms: D000215:Acylation; D002918:Chymotrypsin / Q000378:metabolism; D004151:Dipeptides / Q000378:metabolism; D006868:Hydrolysis; D007700:Kinetics; D012697:Serine Endopeptidases / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D004151:Dipeptides; D012697:Serine Endopeptidases; D002918:Chymotrypsin
vernacular_title: Teoreticheskie aspekty mekhanizma deĭstviia proteoliticheskikh fermentov. V. C-kontsevaia spetsifichnost' serinovykh proteinaz.