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  • aromatic
  • Six species of free-living nitrogen fixing bacteria, Azomonas agilis, Azospirillum brasilense, Azospirillum lipoferum, Azotobacter chroococcum, Azotobacter vinelandii , and Beijerinckia mobilis , were surveyed for their ability to grow and fix N 2 using aromatic compounds as sole carbon and energy source. (springer.com)
  • oxidation
  • XylE is inefficient on its own, especially in vitro , due to instability caused by oxygen sensitivity, and oxidation of the active site iron molecule during it's functional cycle rendering the enzyme inactive 8 . (igem.org)
  • The ability to quench singlet oxygen seems to be in relation with the chemical structure of catechin, with the presence of the catechol moiety on ring B and the presence of a hydroxyl group activating the double bond on ring C. Electrochemical experiments show that (+)-catechin oxidation mechanism proceeds in sequential steps, related with the catechol and resorcinol groups and the oxidation is pH-dependent. (wikipedia.org)
  • The oxidation of the catechol 3',4'-dihydroxyl electron-donating groups occurs first, at very low positive potentials, and is a reversible reaction. (wikipedia.org)
  • lipoxygenase
  • Arachidonate 5-lipoxygenase , also known as ALOX5 , 5-lipoxygenase , 5-LOX , or 5-LO , is a non- heme iron-containing enzyme (EC 1.13.11.34) that in humans is encoded by the ALOX5 gene . (wikipedia.org)
  • Arachidonate 5-lipoxygenase is a member of the lipoxygenase family of enzymes. (wikipedia.org)
  • inhibit
  • Exposure to toxics such as mercury have been found to inhibit enzymes needed to digest wheat gluten and milk casein, resulting in symptoms of autism, ADHD, diabetes, etc. after chronic exposure to gluten or casein. (amalgam.org)
  • These drugs, entacapone and tolcapone, are predicted to bind to the enzyme InhA and directly inhibit substrate binding. (pubmedcentralcanada.ca)
  • gene
  • Structurally, the enzyme is a domain-swapped dimer in many species, although the two subunits have merged into a monomer in yeast, through gene duplication. (wikipedia.org)
  • The human gene for this enzyme is called GLO1. (wikipedia.org)
  • acids
  • The byproducts are stored in the form of tailings ponds where the water contains (1) toxic organic compounds such as naphthenic acids and catechol, (2) heavy metals, and (3) fine clay sediment 1 . (igem.org)
  • hydrogen
  • Rather, the enzyme shifts two hydrogen atoms from one carbon atom of the methylglyoxal to the adjacent carbon atom. (wikipedia.org)
  • Fenton's reaction enzymes (iron homeostasis, reduction, hydrogen peroxide generation) were significantly expressed among all the datasets under lignocellulolytic conditions. (ijbs.com)
  • catalyzes
  • In enzymology, a lactoylglutathione lyase (EC 4.4.1.5) (also known as glyoxalase I) is an enzyme that catalyzes the isomerization of hemithioacetal adducts, which are formed in a spontaneous reaction between a glutathionyl group and aldehydes such as methylglyoxal. (wikipedia.org)
  • detoxification
  • The principal physiological function of glyoxalase I is the detoxification of methylglyoxal, a reactive 2-oxoaldehyde that is cytostatic at low concentrations and cytotoxic at millimolar concentrations. (wikipedia.org)
  • toxic
  • In 2010, the Lethbridge iGEM team confirmed that xylE when introduce to E. coli hydrolyzes catechol to 2-HMS demonstrating and that this critical step can successfully be performed to convert toxic chemicals to metabolic intermediates 7 . (igem.org)
  • employs
  • Due to the evolutionary loss of genes coding for various lignocellulolytic enzymes (including several cellulases), P. placenta employs hemicellulolytic glycoside hydrolases and Fenton's reactions for the rapid depolymerization of plant cell wall components. (ijbs.com)