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Protein Engineering vol. 4 no. 8 pp. 919-922, 1991
© 1991 Oxford University Press

RESEARCH-ARTICLE

The role of electrostatic interactions in the mechanism of peptide bond hydrolysis by a Ser-Lys catalytic dyad

Steve N. Slilaty1 and Huy Khang Vu

Genetic Engineering Section, Biotechnology Research Institute. National Research Council of Canada 6100 Royalmount Avenue, Montreal, Quebec, Canada H4P 2R2

1To whom correspondence should be addressed

General-base catalysis in the active site of serine proteases is carried out by the imidazole side chain of a histidine. During formation of the transition state, an adjacent carboxylic acid group stabilizes the positive charge that forms on the general-base catalyst and as a result contributes several orders of magnitude to the catalytic efficiency of these enzymes. In the recently discovered family of self-cleaving proteins exemplified by the LexA repressor of Escherichia coli, instead of the imidazole of a histidine, the active-site general-base catalyst was found to be the {varepsilon}-amino of a lysine. The considerably higher capacity of the lysine side chain for proton acceptance raises interesting questions concerning the role of electrostatic interactions in the mechanism of proton transfer by this highly basic group. The negative charge elimination studies described here and their effects on the kmax and pK of LexA self-cleavage are consistent with a model in which electrostatic interactions between an acidic side chain and the general-base catalyst form a barrier to proton transfer. The implications are that the {varepsilon}-amino group, unlike the imidazole group, is capable of effecting proton transfer without the intervention of a countercharge.

Keywords: general-base catalysis/LexA repressor/mutagenesis

Received May 31, 1991; accepted July 25, 1991.


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