Hydrolase-like properties of a cofactor-independent dioxygenase.

Thierbach S, Büldt-Karentzopoulos K, Dreiling A, Hennecke U, König S, Fetzner S

Abstract

Mechanistic promiscuity: The (2-alkyl)-3-hydroxy-4(1H)-quinolone-cleaving dioxygenase Hod has an ?/?-hydrolase fold and a Ser/His/Asp triad in its active site. Isatoic anhydride, a suicide substrate of serine hydrolases, inactivates Hod by covalent modification of the active-site serine, thus indicating that the ?/?-hydrolase fold can accommodate dioxygenase chemistry without completely abandoning hydrolase-like properties.