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Results 1 - 10 of 14 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.47742251 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 Chem. Biodivers. 11 861-871 2014 Paenarthrobacter nitroguajacolicus 24934672
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.47742869 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 J. Biol. Chem. 289 8620-8632 2014 Paenarthrobacter nitroguajacolicus 24482238
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.47207895 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. Rii61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1 Eur. J. Biochem. 240 576-583 1996 Arthrobacter sp. 8856057
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.47207895 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. Rii61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1 Eur. J. Biochem. 240 576-583 1996 Pseudomonas putida 8856057
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.47207895 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. Rii61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1 Eur. J. Biochem. 240 576-583 1996 Pseudomonas putida 33/1 8856057
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.47207895 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. Rii61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1 Eur. J. Biochem. 240 576-583 1996 Arthrobacter sp. Ru61a 8856057
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.47207896 A novel type of oxygenolytic ring cleavage: 2,4-oxygenation and decarboxylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline FEMS Microbiol. Lett. 117 299-304 1994 Pseudomonas putida -
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.47684174 Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha/beta-hydrolase family Acta Crystallogr. Sect. F 63 378-381 2007 Pseudomonas putida 17565175
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.47684174 Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha/beta-hydrolase family Acta Crystallogr. Sect. F 63 378-381 2007 Pseudomonas putida 33/1 17565175
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.47207897 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 Biol. Chem. Hoppe-Seyler 373 343-349 1992 Pseudomonas putida 1515060
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