Журнал протеомики и биоинформатики
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Bacterial Serine Proteases: Computational and Statistical Approach to Understand Temperature Adaptability

Tilak Raj, Nikhil Sharma, Savitri and Tek Chand Bhalla

Proteases belong to the group of hydrolases which tend to break the chemical bond joining two amino acids together. Chymotrypsin the first serine protease to be discovered by the scientists in our pancreas revolutionized their study both in the living system and their applications in the industry. Computational tools and techniques to analyse and identify proteases from organisms inhabiting extreme of habitats has opened avenues to study as to what contributes sequentially and structurally to whithstand extreme of pH or temperature. Keeping this in view sixteen amino acid sequnces of serine proteases from mesophilic, thermophilic, hyperthermophilic and psychrophilic organisms were critically analyzed to identify the variation in the physiochemical properties and their amino acids which are responsible in making them to adapt in various extreme conditions. Physiochemical properties and their analysis showed negatively charged residues (Asp+Glu) to be stastically significant contributing for the stability of proteases. Multiple sequence alignment of the amino acid sequences of serine proteases showed catalytic triad (Asp-130; His-163 and Ser- 315) to be conserved in all the four groups. Amino acids Ala (A), Arg (R), Asn (N), Asp (D), Cys (C), Gly (G), Phe (F), Tyr (Y) and Val (V) were found to be stastically significant. Cysteine (C) was exceptionally high in the psychrophilic serine proteases in comparison to their counterpart. Phylogenetic analysis using Neighbour Joining (NJ) method distinguished thermophilic, mesophilic, hyperthermophilic and psychrophilic serine proteases into their respected groups.