Domain Fusion of Two Oxygenases Affords Organophosphonate Degradation in Pathogenic Fungi.

ABSTRACT: Proteins of the HD-domain superfamily employ a conserved histidine-aspartate (HD) dyad to coordinate diverse metallocofactors. While most known HD-domain proteins are phosphohydrolases, new additions to this superfamily have emerged such as oxygenases and lyases, expanding their functional repertoire. To date, three HD-domain oxygenases have been identified, all of which employ a mixed-valent Fe^IIFe^III cofactor to activate their substrates and utilize molecular oxygen to afford cleavage of C-C or C-P bonds via a diferric superoxo intermediate. Phylogenetic analysis reveals an uncharacterized multidomain protein in the pathogenic soil fungus Fonsecaea multimorphosa, herein designated PhoF. PhoF consists of an N-terminal Fe^II/α-ketoglutarate-dependent

SUBMITTER: Langton M 

PROVIDER: S-EPMC9177745 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature