Acta NaturaeActa NaturaeActa Naturae2075-8251Acta Naturae Ltd1069910.32607/20758251-2011-3-1-93-98ArticlesСтатьиResearch ArticleComparative Bioinformatic Analysis of Active Site Structures in Evolutionarily Remote Homologues of α,β-Hydrolase Superfamily EnzymesComparative Bioinformatic Analysis of Active Site Structures in Evolutionarily Remote Homologues of α,β-Hydrolase Superfamily EnzymesSuplatovD A

Faculty of Bioengineering and Bioinformatics

ArzhanikV K

Faculty of Bioengineering and Bioinformatics

SvedasV K

Faculty of Bioengineering and Bioinformatics

Lomonosov Moscow State UniversityBelozersky Institute of Physicochemical Biology, Lomonosov Moscow State UniversityLomonosov Moscow State UniversityBelozersky Institute of Physicochemical Biology, Lomonosov Moscow State University1503201131VOL 3, NO1 (2011)ТОМ 3, №1 (2011)939817012020Copyright ©; 2011, Suplatov D.A., Arzhanik V.K., Svedas V.K.Copyright ©; 2011, Suplatov D.A., Arzhanik V.K., Svedas V.K.2011Suplatov D.A., Arzhanik V.K., Svedas V.K.Suplatov D.A., Arzhanik V.K., Svedas V.K.https://creativecommons.org/licenses/by/4.0https://actanaturae.ru/2075-8251/article/view/10699

Comparative bioinformatic analysis is the cornerstone of the study of enzymes’ structure-function relationship. However, numerous enzymes that derive from a common ancestor and have undergone substantial functional alterations during natural selection appear not to have a sequence similarity acceptable for a statistically reliable comparative analysis. At the same time, their active site structures, in general, can be conserved, while other parts may largely differ. Therefore, it sounds both plausible and appealing to implement a comparative analysis of the most functionally important structural elements - the active site structures; that is, the amino acid residues involved in substrate binding and the catalytic mechanism. A computer algorithm has been developed to create a library of enzyme active site structures based on the use of the PDB database, together with programs of structural analysis and identification of functionally important amino acid residues and cavities in the enzyme structure. The proposed methodology has been used to compare some α,β-hydrolase superfamily enzymes. The insight has revealed a high structural similarity of catalytic site areas, including the conservative organization of a catalytic triad and oxyanion hole residues, despite the wide functional diversity among the remote homologues compared. The methodology can be used to compare the structural organization of the catalytic and substrate binding sites of various classes of enzymes, as well as study enzymes’ evolution and to create of a databank of enzyme active site structures.

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