Voprosy meditsinskoi khimii (ISSN 0042-8809)

Peptide hydrolases with catalytic dyad ser - lys. Similarity and distinctions of the activecenters of ATP-dependent proteases Lon, repressorslexa, signal peptidases and c-terminal processingproteases

   


1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Siences
PubMed Id: 12698553
Year: 2002 vol: 48  issue:6  pages: 541-552
Abstract: It is established that ATP-dependent protease Lon family belongs to the serine-lysinepeptide hydrolases clan. Significant similarity of amino acid sequences of proteases Lonand repressors LexA in the regions including the catalytic serine and lysine residues isrevealed 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 twosubfamilies in accordance with the nature of amino acids in the catalytically activeserine environment. Putative DNA binding sites are revealed in proteolytic domains of LonA subfamily. Similarities and distinctions of the all families peptide hydrolases of theclan in the regions of their active centers are discussed.
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Reference: Rotanova T.V., Peptide hydrolases with catalytic dyad ser - lys. Similarity and distinctions of the activecenters of ATP-dependent proteases Lon, repressorslexa, signal peptidases and c-terminal processingproteases, Voprosy meditsinskoi khimii, 2002, vol: 48(6), 541-552.
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