In silico comparative structural and functional analysis of arsenite methyltransferase from bacteria, fungi, fishes, birds, and mammals.
Ashutosh KabirajAnubhab LahaAnindya Sundar PanjaRajib BandopadhyayPublished in: Journal, genetic engineering & biotechnology (2023)
All of our in silico studies confirmed the fact that arsenite methyltransferase is a cytosolic stable enzyme with conserved sequences over a wide range of organisms. Thus, because of its stable and ubiquitous nature, arsenite methyltransferase could be employed in arsenic bioremediation.