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Results 1 - 10 of 19 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Display the reaction diagram Show all sequences 1.13.11.48207896 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 Arthrobacter sp. -
Display the reaction diagram Show all sequences 1.13.11.48207896 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 Arthrobacter sp. Ru61a -
Display the reaction diagram Show all sequences 1.13.11.48207895 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 reaction diagram Show all sequences 1.13.11.48207895 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 reaction diagram Show all sequences 1.13.11.48285259 Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases J. Bacteriol. 181 5725-5733 1999 Arthrobacter sp. 10482514
Display the reaction diagram Show all sequences 1.13.11.48658042 Dioxygenases without requirement for cofactors and their chemical model reaction: compulsory order ternary complex mechanism of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion Biochemistry 43 14485-14499 2004 Paenarthrobacter ilicis 15533053
Display the reaction diagram Show all sequences 1.13.11.48658042 Dioxygenases without requirement for cofactors and their chemical model reaction: compulsory order ternary complex mechanism of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion Biochemistry 43 14485-14499 2004 Paenarthrobacter ilicis Ru61a 15533053
Display the reaction diagram Show all sequences 1.13.11.48673207 Dioxygenases without requirement for cofactors: Identification of amino acid residues involved in substrate binding and catalysis, and testing for rate-limiting steps in the reaction of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase Curr. Microbiol. 51 344-352 2005 Paenarthrobacter nitroguajacolicus 16187153
Display the reaction diagram Show all sequences 1.13.11.48673207 Dioxygenases without requirement for cofactors: Identification of amino acid residues involved in substrate binding and catalysis, and testing for rate-limiting steps in the reaction of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase Curr. Microbiol. 51 344-352 2005 Paenarthrobacter nitroguajacolicus Rü61a 16187153
Display the reaction diagram Show all sequences 1.13.11.48673207 Dioxygenases without requirement for cofactors: Identification of amino acid residues involved in substrate binding and catalysis, and testing for rate-limiting steps in the reaction of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase Curr. Microbiol. 51 344-352 2005 Paenarthrobacter nitroguajacolicus R-61a 16187153
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