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Unusually large electrostatic field effect of the buried aspartate in serine proteinases: Source of catalytic power
Author(s) -
NáraySzabó Gábor
Publication year - 1983
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560230241
Subject(s) - serine , substituent , catalytic triad , nucleophile , chemistry , triad (sociology) , coulomb , serine protease , catalysis , stereochemistry , computational chemistry , physics , biochemistry , enzyme , electron , quantum mechanics , psychology , psychoanalysis , protease
Calculating the electrostatic potential around the Ser–His–Asp catalytic triad in serine proteinases the very important substituent effect of the buried aspartate is revealed. It is found that the strong Coulomb field of this distant but charged side chain considerably enhances the nucleophilicity of the active serine hydroxyl group. The interpretation of the vital importance of aspartate may replace the “charge–relay” hypothesis which seems to be disproved in the light of recent experiments.