Assessing the role of E451, D452, and H139 in the catalytic function of a Thermus thermophilus bacterial laccase

Key Points

• Bacterial laccase shows varied enzymatic activity based on mutations at key amino acid positions.
• The specific changes at E451, D452, and H139 significantly affect the catalytic function of Thermus thermophilus laccase.
• Analysis includes site-directed mutagenesis to assess the influence of specific amino acids on laccase activity.
• Understanding these effects may enable the development of more efficient laccase variants for industrial applications.