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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 1.13.11.48742251 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 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 1.13.11.48207896 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 1.13.11.48673207 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
Display the reaction diagram Show all sequences 1.13.11.48684175 Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rue61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily Acta Crystallogr. Sect. F 63 382-385 2007 Paenarthrobacter nitroguajacolicus 17565176
Display the reaction diagram Show all sequences 1.13.11.48684175 Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rue61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily Acta Crystallogr. Sect. F 63 382-385 2007 Paenarthrobacter nitroguajacolicus Rü61a 17565176
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