• The isofunctional enzymes of catechol 1,2-dioxygenase from species of Acinetobacter, Pseudomonas, Nocardia, Alcaligenes and Corynebacterium oxidize 3-methylcatechol according to both the intradiol and extradiol cleavage patterns. (wikipedia.org)
  • However, the enzyme preparations from Brevibacterium and Arthrobacter have only the intradiol cleavage activity. (wikipedia.org)
  • Extradiol Cleavage of 3-Methylcatechol by Catechol 1,2-Dioxygenase from Various Microorganisms. (wikipedia.org)
  • In the convergent mode, structurally diverse aromatic compounds are converted to one of a few aromatic ring cleavage substrates such as catechol, gent sate, protocatechuate and their derivatives [ 5 ]. (biomedcentral.com)
  • In this divergent mode, a metal-dependent dioxygenase channels these dihydroxylated intermediates into one of the two possible pathways: the meta -cleavage pathway or the ortho -cleavage pathway [ 7 - 9 ] (Fig. 1 ). (biomedcentral.com)
  • Oxygenases belong to the oxidoreductive group of enzymes (E.C. Class 1), which oxidize the substrates by transferring oxygen from molecular oxygen (O 2 ) and utilize FAD/NADH/NADPH as the co-substrate. (biomedcentral.com)
  • The enzyme 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate dehydrogenase uses 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate and NAD+ to produce 3-methylcatechol, NADH and CO2. (wikipedia.org)
  • A number of bacteria that can degrade a variety of aromatic compounds have been identified and the pathways involved in the degradation have been extensively characterized [ 3 , 4 ]. (biomedcentral.com)
  • Many of these compounds have been reported to be toxic to the living organisms [ 3 ]. (biomedcentral.com)
  • The 2,3-dihydrobenzofuran derivative, 7-acetyl-4,6-dimethoxy-2-isopropenyl-2,3-dihydrobenzofuran, had an ED 50 value of 1.3 μg (5.4×10 -9 mol)/cm 2 against the common cutworm. (go.jp)