Authors: T.V. Rotanova

Address: Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Siences, Ul. Miklukho-Maklaya 16/10, GSP Moscow, 117997 Russia. Phone: +7 (095) 335-4222; e-mail: rotanova@enzyme.siobc.ras.ru

Abstract:

It is established that ATP-dependent protease Lon family belongs to the serine-lysine peptide hydrolases clan. Significant similarity of amino acid sequences of proteases Lon and repressors LexA in the regions including the catalytic serine and lysine residues is revealed by comparing primary structures of different families of the enzymes with Ser - Lys catalytic dyad. The both Lon and LexA families are shown to be divided into two subfamilies in accordance with the nature of amino acids in the catalytically active serine environment. Putative DNA binding sites are revealed in proteolytic domains of Lon A subfamily. Similarities and distinctions of the all families peptide hydrolases of the clan in the regions of their active centers are discussed.

Key words: catalytic dyad Ser - Lys, ATP-dependent protease Lon repressors, LexA, subfamilies, signal peptidases, tail-specific proteases, C-terminal processing peptidases.

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