Hydrolase-like properties of a cofactor-independent dioxygenase.
Thierbach S, Büldt-Karentzopoulos K, Dreiling A, Hennecke U, König S, Fetzner S
Research article (journal) | Peer reviewedAbstract
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.
Details about the publication
Journal: ChemBioChem
Volume: 13
Issue: 8
Page range: 1125-1127
Status: Published
Release year: 2012
Language in which the publication is written: English
Authors from the University of Münster
| Büldt-Karentzopoulos, Klaudia | Institute of Molecular Microbiology and Biotechnology |
| Fetzner, Susanne | Professur für Molekulare Mikrobiologie und Biotechnologie (Prof. Fetzner) |
| Hennecke, Ulrich | Professur für Organische Chemie (Prof. Studer) |
| König, Simone | Interdisciplinary Centre for Clinical Research (IZKF) |
| Thierbach, Sven | Professur für Molekulare Mikrobiologie und Biotechnologie (Prof. Fetzner) |