Identi cation of key amino acid residues toward improving the catalytic activity and substrate speci city of plant-derived cytochrome p450 monooxygenases cyp716a subfamily enzyme for triterpenoid production in saccharomyces cerevisiae

HIGHLIGHTS

• who: CYP and colleagues from the University of Colorado Boulder, United States have published the research work: Identi cation of key amino acid residues toward improving the catalytic activity and substrate speci city of plant-derived cytochrome P450 monooxygenases CYP716A subfamily enzyme for triterpenoid production in Saccharomyces cerevisiae, in the Journal: (JOURNAL)
• what: In this study, the key amino_acid residues in the ligand-binding_site of CYP716A12 required for the catalytic activity of enzyme and substrate specificity were investigated through homology modeling, structural alignment, in silico site-directed_mutagenesis, and a docking profile from molecular docking analysis . . .
  

   

  

  If you want to have access to all the content you need to log in!

  Thanks :)

  Username or Email

  Password

  Remember me

  Lost your password?

  If you don't have an account, you can create one here.