Pal, P and Sengupta , K (2020) Computational-based insights into the phylogeny,structure, and function of Rhodococcus alkane-1-monooxygenase. 3 Biotech, 10 (301).

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Abstract

Alkane-1-monooxygenase of alkanotrophic Rhodococcus species has been characterized using standard bioinformatics tools to investigate phylogenetic relationships, and three-dimensional structure and functions. Results revealed that activity of the Rhodococcus alkane-1-monooxygenase would be optimum in alkaline pH as their isoelectric points were in the range of 7.5 to 9. Higher aliphatic index (87 to 95) indicated that these enzymes are thermostable. Extinction coefficient of the enzyme varied from 68,793 to 1,25,820 M−1 cm−1 and average molecular weight was 45 kDa. Secondary structures predicted maximum alpha-helical content rather than the other conformations such as sheets or turns. The instability index (II) of most stable query protein was 39.7% which was lowest among all 76 proteins analysed in this study. Predicted 3D structure of query protein revealed that it containsAlkane-1-monooxygenase of alkanotrophic Rhodococcus species has been characterized using standard bioinformatics tools to investigate phylogenetic relationships, and three-dimensional structure and functions. Results revealed that activity of the Rhodococcus alkane-1-monooxygenase would be optimum in alkaline pH as their isoelectric points were in the range of 7.5 to 9. Higher aliphatic index (87 to 95) indicated that these enzymes are thermostable. Extinction coefficient of the enzyme varied from 68,793 to 1,25,820 M−1 cm−1 and average molecular weight was 45 kDa. Secondary structures predicted maximum alpha-helical content rather than the other conformations such as sheets or turns. The instability index (II) of most stable query protein was 39.7% which was lowest among all 76 proteins analysed in this study. Predicted 3D structure of query protein revealed that it containstransport factor, and peroxiredoxin. The predicted tertiary model of R. rhodochrous alkane-1-monooxygenase (OOL33526.1) was deposited in Protein Model Database (Accession No.: PM0083166). The overall report is unique to best of our knowledge, and the importance of this study is to understand the theoretical aspects of structure and functions of alkane-1-monooxygenase of hydrocarbonoclastic strains of Rhodococcus.

Item Type:	Article
Subjects:	Cell Biology
Depositing User:	Mr. Rameshwar Nema
Date Deposited:	07 Feb 2021 12:57
Last Modified:	07 Feb 2021 12:57
URI:	http://nccs.sciencecentral.in/id/eprint/893

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