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Excavating the functionally crucial active-site residues of the DXS protein of Bacillus subtilis by exploring its closest homologues.

Ashish RunthalaTavakala Harsha SaiVandana KamjulaSuresh C PhularaVikrant Singh RajputKarthikeyan Sangapillai
Published in: Journal, genetic engineering & biotechnology (2020)
The study excavates the vital functional, phylogenetic, and conserved residues across the active site of the DXS protein, the key rate-limiting controller of the entire pathway. It would aid to computationally understand the evolutionary landscape of this industrially useful enzyme and would allow us to widen its substrate repertoire to increase the enzymatic yield of unnatural molecules for in vivo and in vitro applications.
Keyphrases
  • bacillus subtilis
  • amino acid
  • protein protein
  • binding protein
  • transcription factor
  • hydrogen peroxide
  • gene expression
  • dna methylation
  • nitric oxide