Influence of mutations at different distances from the active center on the activity and stability of laccase 13B22.

ABSTRACT: Laccases with high catalytic efficiency and high thermostability can drive a broader application scope. However, the structural distribution of key amino acids capable of significantly influencing the performance of laccases has not been explored in depth. Thirty laccase 13B22 mutants with changes in amino acids at distances of 5 Å (first shell), 5-8 Å (second shell), and 8-12 Å (third shell) from the active center were validated experimentally with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) as substrate. Twelve of these mutants (first shell, 1; second shell, 4; third shell, 7) showed higher catalytic efficiency than the wild-type enzyme. Mutants D511E and I88L-D511E showed 5.36- and 10.58-fold increases in k_cat/K_m, respectively, with increases in o

SUBMITTER: Zhang R 

PROVIDER: S-EPMC12116972 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature