Computational analysis to comprehend the structure-function properties of fibrinolytic enzymes from Bacillus spp for their efficient integration into industrial applications Article Swipe

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Nitisha Boro , Pedro Alexandrino Fernandes , Ashis K. Mukherjee ·

YOU? · · 2024 · Open Access · · DOI: https://doi.org/10.1016/j.heliyon.2024.e33895

The alignment of sixty fibrinolytic serine protease enzymes (molecular mass 12-86 kDa) sequences showed 49 enzymes possess a conserved domain with a catalytic triad of Asp196, His242, and Ser569. The predicted instability and aliphatic indexes were 1.94-37.77, and 68.9-93.41, respectively, indicating high thermostability. The random coil means value suggested the predominance of this secondary structure in these proteases. A set of 50 amino acid residues representing motif 3 signifies the Peptidase S8/S53 domain that was invariably observed in 56 sequences. Additionally, 28 sequences have transmembrane helices, with two having the most disordered areas, and they pose 25 enzyme cleavage sites. A comparative analysis of the experimental work with the results of in-silico study put forward the characteristics of the enzyme sequences JF739176.1 and MF677779.1 to be considered when creating a potential mutant enzyme as these sequences are stable at high pH with thermostability and to exhibit αβ-fibrinogenase activity in both experimental and in-silico studies.

Related Topics

In Silico

Bacillus Subtilis

Biochemistry

Computational Biology

Concepts

In silico Thermostability Enzyme Bacillus subtilis Amino acid Biochemistry Catalytic triad Computational biology Protein domain Biology Bacillus pumilus Protease Sequence alignment Chemistry Peptide sequence Serine Genetics Bacteria Gene

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Type: article
Language: en
Landing Page: https://doi.org/10.1016/j.heliyon.2024.e33895
PDF: http://www.cell.com/article/S2405844024099262/pdf
OA Status: gold
Cited By: 6
References: 151
Related Works: 10
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Title: Computational analysis to comprehend the structure-function properties of fibrinolytic enzymes from Bacillus spp for their efficient integration into industrial applications

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Publication year: 2024

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Authors: Nitisha Boro, Pedro Alexandrino Fernandes, Ashis K. Mukherjee

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Landing page: https://doi.org/10.1016/j.heliyon.2024.e33895

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Concepts: In silico, Thermostability, Enzyme, Bacillus subtilis, Amino acid, Biochemistry, Catalytic triad, Computational biology, Protein domain, Biology, Bacillus pumilus, Protease, Sequence alignment, Chemistry, Peptide sequence, Serine, Genetics, Bacteria, Gene

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Cited by: 6

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