Structural and Functional Characteristics of Potent Dioxygenase from <i>Moesziomyces aphidis</i>.

ABSTRACT: Enzymatic C=C double bond cleavage to give carbonyl-species is an emerging alternative to ozonolysis, or stoichiometric use of metal-oxidants. The substrate scope of 4-His Fe dioxygenases, however, appears to be restricted to aromatic compounds with a hydroxy group at the 4-position of the aromatic ring. In-depth structural and functional characterization is a prerequisite to understand and ultimately to extend the substrate scope of this family of enzymes. Herein, Moesziomyces aphidis DSM 70725 aromatic dioxygenase (MapADO) is characterized through X-ray crystallography, biophysical as well as biochemical assays, substrate docking and mutagenesis. MapADO features a seven-bladed β-propeller fold and a Fe²⁺ center coordinated by four histidine residues and sh

SUBMITTER: Schober L 

PROVIDER: S-EPMC12308385 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature