Journal of Basic Research in Medical Sciences
مجله ی تحقیقات پایه در علوم پزشکی
Journal of Basic Research in Medical Sciences
Medical Sciences
http://jbrms.medilam.ac.ir
1
admin
2383-0506
2383-0972
doi
en
jalali
1398
12
1
gregorian
2020
3
1
7
2
online
1
fulltext
en
Analysis to describe the catalytic critical residue of keratinase mojavensis using peptidase inhibitors: A docking-based bioinformatics study
Bioinformatics
Bioinformatics
پژوهشي
Research
<div><strong>Introduction:</strong> Vital catalysts have long been widely used in the food industry, but with new applications in many industries, such as the chemical industry, they have become even more important. In biocatalysis, all parts of the cell, cell extract, purified enzyme, inactive cell, or inactive enzymes are used as catalysts in various processes. Enzymes are essential for various industrial, pharmaceutical, and especially biotechnological processes. Keratinase is produced by various microorganisms in the presence of keratin as a substrate. It mainly targets disulfide bonds. In this study, the biochemical properties of keratinase enzymes derived from <a name="_Hlk45139910"><em>Bacillus mojavensis</em> </a>(<em>B. mojavensis</em>) were investigated.<span dir="RTL"></span><br>
<strong>Materials and methods:</strong> The 3D structure of keratinases from <em>B. mojavensis</em> was created using Modeler software, and the model's validation and refinement indicators, including Prosa, Z-score, and Ramachandran Graph confirmed the high quality of the modeled protein. The PMSF, Pepstatin and leupeptin structures were prepared from the PubChem database server and introduced to the MVD software along with the 3D structure of the keratinase for molecular docking.<br>
<strong>Results:</strong> The binding energies (Eaint#) for the Mojavensis-PMSF, Mojavensis-Pepstatin and Mojavensis-Leupeptin complexes were -71.73, -334.1 and -211.2, respectively. In all three Mojavensis-PMSF, Mojavensis-Pepstatin and Mojavensis-Leupeptin complexes, the Serine 277 keratinase mojavensis formed a hydrogen bond with inhibitors. Serine 295 also interacted with inhibitors in both of Pepstatin and Leupeptin complexes. Glutamic 299 keratinase mojavensis also interacted with PMSF and Leupeptin. All three PMSF, Pepstatin and leupeptin peptidase inhibitors were able to interact with keratinase mojavensis.<br>
<strong>Conclusion: </strong>Docking results showed that Serine amino acids 277 and 295 in the active site of keratinase mojavensis, may play a key role in its catalytic function.</div>
Bioinformatics, Keratinase, Enzyme, Homology modeling, Docking
13
28
http://jbrms.medilam.ac.ir/browse.php?a_code=A-10-495-1&slc_lang=en&sid=1
Somayeh
Rahimnahal
s.rahimnahal@yahoo.com
10031947532846003825
10031947532846003825
No
Department of Animal Science, Ilam University, Ilam, Iran
Morteza
Shams
shamsimorteza55@gmail.com
10031947532846003826
10031947532846003826
No
Zoonotic Diseases Research Center, Ilam University of Medical Sciences, Ilam, Iran
Hossein
Tarrahimofrad
10031947532846003827
10031947532846003827
No
Department of Animal Biotechnology, National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran
Yahya
Mohammadi
mohamadi_yahya@yahoo.com
10031947532846003828
10031947532846003828
Yes
Department of Animal Science, Ilam University, Ilam, Iran