title: Hydrolase-like properties of a cofactor-independent dioxygenase.
abstract: Mechanistic promiscuity: The (2-alkyl)-3-hydroxy-4(1H)-quinolone-cleaving dioxygenase Hod has an α/β-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 α/β-hydrolase fold can accommodate dioxygenase chemistry without completely abandoning hydrolase-like properties.
authors.affiliation: Institute of Molecular Microbiology and Biotechnology, University of Muenster, Corrensstrasse 3, 48149 Muenster, Germany.
authors.forename: Sven
authors.initials: S
authors.lastname: Thierbach
authors.forename: Klaudia
authors.initials: K
authors.lastname: Büldt-Karentzopoulos
authors.forename: Alena
authors.initials: A
authors.lastname: Dreiling
authors.forename: Ulrich
authors.initials: U
authors.lastname: Hennecke
authors.forename: Simone
authors.initials: S
authors.lastname: König
authors.forename: Susanne
authors.initials: S
authors.lastname: Fetzner
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D049308:Dioxygenases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D006867:Hydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D011804:Quinolines / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D011804:Quinolines; D049308:Dioxygenases; D006867:Hydrolases