The role of Gln269Leu mutation on the thermostability and structure of uricase from Aspergillus flavus.

ABSTRACT: Aspergillus flavus Urate oxidase (AFUOX) is promising for potential therapeutic applications, particularly in gout treatment. However, the enzyme's low thermostability and solubility limit its efficacy. A targeted mutation, substituting Gln with Leu at position 269 (Q269L) has been proposed to enhance its stability. The turnover number, catalytic efficiency, and specific activity of Q269L were 3.7 (s^-1), 53.2 (mM^-1. s^-1), and 3.926 U/mg, respectively. In comparison, for the wild type, these were 3.1 (S^-1), 35.1 (mM^-1. s^-1), and 4.018 U/mg, respectively. Notably, the wild type exhibited maximum activity at pH 9 and 25 °C, whereas the activity of Q269L was obtained at pH 9.5 and 30 °C. Furthermore, the half-life of Q269L at 40

SUBMITTER: Akhlaghi M 

PROVIDER: S-EPMC11894227 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature