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In silico comparative structural and functional analysis of arsenite methyltransferase from bacteria, fungi, fishes, birds, and mammals.

Ashutosh KabirajAnubhab LahaAnindya Sundar PanjaRajib Bandopadhyay
Published 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.
Keyphrases
  • molecular docking
  • drinking water
  • transcription factor
  • risk assessment
  • multidrug resistant