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• W2059269003 startingPage "859" @default.
• W2059269003 abstract "Two Escherichia coli transformants with catechol 1,2-dioxygenase activity were selected from a gene library of the benzamide-assimilating bacterium Arthrobacter species strain BA-5-17, which produces four catechol 1,2-dioxygenase isozymes. A DNA fragment isolated from one transformant contained a complete open reading frame (ORF). The deduced amino acid sequence of the ORF shared high identity with hydroxyquinol 1,2-dioxygenase. An enzyme expressed by the ORF was purified to homogeneity and characterized. When hydroxyquinol was used as a substrate, the purified enzyme showed 6.8-fold activity of that for catechol. On the basis of the sequence identity and substrate specificity of the enzyme, we concluded that the ORF encoded hydroxyquinol 1,2-dioxygenase. When catechol was used as a substrate, cis, cis-muconic acid and 2-hydroxymuconic 6-semialdehyde, which were products by the intradiol and extradiol ring cleavage activities, respectively, were produced. These results showed that the hydroxyquinol 1,2-dioxygenase reported here was a novel dioxygenase that catalyzed both the intradiol and extradiol cleavage of catechol." @default.
• W2059269003 created "2016-06-24" @default.
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• W2059269003 date "1999-01-01" @default.
• W2059269003 modified "2023-10-16" @default.
• W2059269003 title "Cloning of a Gene Encoding Hydroxyquinol 1,2-Dioxygenase that Catalyzes Both Intradiol and Extradiol Ring Cleavage of Catechol" @default.
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• W2059269003 doi "https://doi.org/10.1271/bbb.63.859" @default.
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