Sandbox Reserved 1665: Difference between revisions
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Mutations in the NAD binding site occurred causing certain changes. Mutations in lys182 caused for there to be a removal of lysine side chained with a hydroxyl group in the NAD binding site. K182A and K182Q showed a lack of activity and a valine mutation (T234V) closely as well. | Mutations in the NAD binding site occurred causing certain changes. Mutations in lys182 caused for there to be a removal of lysine side chained with a hydroxyl group in the NAD binding site. K182A and K182Q showed a lack of activity and a valine mutation (T234V) closely as well. | ||
Mutations in the octanal binding site occurred as well and made certain changes to it. Asn 159, Trp 160, Ser 292, Leu 419, and Phe 456 were the amino acid residues that got most disrupted by the mutation. The reason behind this was that these amino acid residues were close to the catalytic cysteine site of AldC and those other residues received a lesser disruption from the activity. From the table above we can see N159 and L419 mutants lacked significant activity | Mutations in the octanal binding site occurred as well and made certain changes to it. Asn 159, Trp 160, Ser 292, Leu 419, and Phe 456 were the amino acid residues that got most disrupted by the mutation. The reason behind this was that these amino acid residues were close to the catalytic cysteine site of AldC and those other residues received a lesser disruption from the activity. From the table above we can see N159 and L419 mutants lacked significant activity | ||
Since the mutation occurred on Cys 291, we can see it caused a lack of activity between the two ligands NAD and Octanal in the protein. | |||
