Structural insights into manganese-dependent arylsulfatase from <i>Enterococcus faecium</i> and its catalytic promiscuity.

ABSTRACT: Catalytic promiscuity, wherein enzymes catalyze multiple distinct reactions by stabilizing various transition states, is well documented in the alkaline phosphatase superfamily. In this study, we determined the crystal structure of an arylsulfatase from Enterococcus faecium (EfAS), revealing a homotetrameric assembly with a windmill-like architecture not observed in other known arylsulfatases or phosphonoester hydrolases. This quaternary structure is stabilized by hydrogen bonding, salt bridges, and hydrophobic interactions, while retaining full accessibility to the catalytic groove. Moreover, by incorporating a manganese ion in its active site, EfAS provides the first crystallographically confirmed example of a Mn²⁺-dependent arylsulfatase, addressing previous uncertaint

SUBMITTER: Guo L 

PROVIDER: S-EPMC12421950 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature