Substrate recognition mechanisms of ʟ-glutamate oxidase from Streptomyces sp. and its conversion to ʟ-tyrosine oxidase.

ABSTRACT: ʟ-Amino acid oxidase (LAAO) is a flavoenzyme that catalyzes the oxidative deamination of ʟ-amino acids, producing α-keto acids, ammonia, and hydrogen peroxide. Among LAAOs, ʟ-glutamate oxidase (LGOX) from Streptomyces sp. X-119-6 exhibits exceptionally high substrate specificity for ʟ-glutamate. LGOX is expressed as a homodimeric precursor and undergoes proteolytic processing for maturation. Structural studies revealed that LGOX comprises an FAD-binding domain, a substrate-binding domain, and a helical domain. Conserved residues W653, R124, and Y562 that recognize the α-amino and α-carboxyl groups of the substrate exist in the putative active site. R305 was identified as a key determinant for side-chain recognition; its substitution with Glu conferred specific activity toward ʟ-arginine, e

SUBMITTER: Ueda Y 

PROVIDER: S-EPMC12724004 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature