Caspases are very important molecules which are playing a key role for apoptosis. Deregulation of apoptosis
contributes to the pathogenesis of many human diseases. Therefore, the regulation of this protein can be controlled for the
therapeutic purpose. To determine molecular evolution, in silico of proteins is popular a method for certain laboratories
and biotechnology companies. It may help to detect that mutations often occur far away from the active site of the protein.
It can give us an insight thinking about drug development. Using sequence analysis and phylogenetic approach, we have
described about different human caspases and about their origin in terms of ancestral relationship. It was envisaged using
the tools of bioinformatics. Among the fourteen mammalian caspases defined, we are able to make use of twelve human
caspases, whose data is publicly available. It is evident from the data studied that human caspases 4 and 5 share the same
origin in comparison to human caspase 1 and caspase 12, irrespective of the fact that both share quite high level of similarity.
Although, human caspase related ancestral aspect had been studied earlier but the variation which seems to be quite peculiar
in this study is that the executioner, caspase 3 shares a remarkable high level of similarity with caspase 7 but this is not
applicable to human caspase 6, the other member of executioner group. Human caspases 3 and 7 were seen to have similar
substrate specificity but it was not evident in terms of the origin. Our findings are assumed to play a significant role in the
studies of programmed cell death, inflammatory responses and for scholarly studies in the near future.
Keywords: Apoptosis, bioinformatics, computational analysis, human caspases, molecular evolution, programmed cell death, Phylogenetic, Clustalw score, human inflammatory, Cladogram
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