Unraveling the Structural and Functional Insights of Bacterial HCN Synthase Enzyme

Introduction: The present study investigates the structural and functional attributes of HCN synthase, known for its role in metals recovery from natural and secondary sources and gaining attention in the field of biohydrometallurgy. Methods: The nucleotide sequences of 23 bacterial strains in reference to Pseudomonas aeruginosa were procured from the UniPROT and were subjected to analyses using SWISS-MODEL, PDBsum, ESBRI, MEME, InterProScan, and MEGA X. Results: Multiple sequence alignment showed a total of sixteen 100% conserved positions in the aligned region. The physico-chemical characteristics showed molecular weight between 39.24–46.79 kDa, pI range of 4.99–10.43, instability index from 26.69–50.66, and aliphatic index ranging from 83.07-101.59. The amino acid contents - Leucine (10.3%), Alanine (9.8%), Glycine (9.3%), Valine (6.8%), and Glutamic acid (6.3%) were found predominantly. The secondary structure revealed that the enzyme is dominated by 37.44% of amino acid residues in random coils, 36.97% in alpha-helices and 17.50% in extended sheets. Discussion: The secondary structure prediction revealed that the enzyme consists of twelve α- helices that interact through nineteen helix-helix interactions along with twenty-three beta strands and three gamma turns. Moreover, the tertiary structure prediction showed the structural stability, consistency, and reliability of the HCN synthase protein. In addition, functional analysis unveiled the transmembrane regions, protein-protein interactions, post-translational modifications, and phosphorylation sites of the protein. Conclusion: Fundamentally, the study uncovered valuable perspectives on a stable and consistent structure of HCN synthase, providing significant insights into its characteristics. Thus, the present study improves the understanding of HCN synthase and offers a foundation for future research.