| Title | Date | PubMed ID |
|---|
| Binding pockets and permeation channels for dioxygen through cofactorless 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase in association with its natural substrate, 3-hydroxy-2-methylquinolin-4(1H)-one. A perspective from molecular dynamics simulations. | 2014 Jun | 24934672 |
| Origin of the proton-transfer step in the cofactor-free (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase: effect of the basicity of an active site His residue. | 2014 Mar 21 | 24482238 |
| Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold. | 2010 Jan 12 | 20080731 |
| Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha/beta-hydrolase family. | 2007 May 1 | 17565175 |
| 2,4-dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Rü61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1. | 1996 Sep 15 | 8856057 |
| Microbial metabolism of quinoline and related compounds. XIV. Purification and properties of 1H-3-hydroxy-4-oxoquinoline oxygenase, a new extradiol cleavage enzyme from Pseudomonas putida strain 33/1. | 1992 Jun | 1515060 |