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  • Reaction
  • The optimum pH for an enzymatic reaction may shift by as much as 3 pH units upon immobilization.24 This shift is a result of both the charge of the support material and the chemical modification of the enzyme. (clicktocurecancer.info)
  • If you click on the box you will change to the appropriate reaction scheme or enzyme specification. (qmul.ac.uk)
  • An example of the reaction carried out by catechol 1,2-dioxygenase is the formation of cis,cis-muconic acid from catechol, shown below. (wikipedia.org)
  • 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)
  • For example, in the α-ketoglutarate-dependent enzymes, one atom of dioxygen is incorporated into two substrates, with one always being α-ketoglutarate, and this reaction is brought about by a mononuclear iron center. (wikipedia.org)
  • The two enzymes can be distinguished based on their reaction products and cofactors. (wikipedia.org)
  • section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. (uniprot.org)
  • This allows use of the over-expressed enzyme from a crude bacterial extract in a PCR reaction at a fraction of the cost of highly purified commercial enzyme. (igem.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)
  • aromatic compounds
  • 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)
  • Dorn E, Knackmuss H-J (1978) Chemical structure and biodegradability of halogenated aromatic compounds: two catechol 1,2-dioxygenases from a 3-chlorobenzoate grown pseudomonad. (springer.com)
  • These bacteria subsequently employ 1,2-CTD in the last step of the degradation of aromatic compounds to aliphatic products. (wikipedia.org)
  • NADH
  • 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)
  • phenol
  • Catechin /ˈkætɪtʃɪn/ is a flavan-3-ol, a type of natural phenol and antioxidant. (wikipedia.org)
  • Catechol is produced industrially by the hydroxylation of phenol using hydrogen peroxide. (wikipedia.org)
  • hydroxyl
  • 1,2-CTD uses Fe3+ as a cofactor to cleave the carbon-carbon bond between the phenolic hydroxyl groups of catechol, thus yielding muconic acid as its product. (wikipedia.org)
  • In contrast, 2,3-CTD utilizes Fe2+ as a cofactor to cleave the carbon-carbon bond adjacent to the phenolic hydroxyl groups of catechol, thus yielding 2-hydroxymuconaldehye as its product. (wikipedia.org)
  • The second catechol hydroxyl group on carbon 3 (C3) is coordinated to Fe3+ after its deprotonation by the Tyr200 ligand. (wikipedia.org)
  • Catechin possesses two benzene rings (called the A- and B-rings) and a dihydropyran heterocycle (the C-ring) with a hydroxyl group on carbon 3. (wikipedia.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)
  • Those enzymes mediate the O-methylation on a specific hydroxyl group, like on 4' (example in Catharanthus roseus) or 3' (example in rice) positions. (wikipedia.org)
  • catalytic
  • Particle size is also an important consideration: smaller particles have been observed to yield catalytic properties more closely approximating those obtained with soluble enzymes. (clicktocurecancer.info)
  • The most widely observed cofactor involved in dioxygenation reactions is iron, but the catalytic scheme employed by these iron-containing enzymes is highly diverse. (wikipedia.org)
  • The enzyme resembles a boomerang in shape, and can therefore be clearly divided into three domains: two catalytic domains residing at each end of the "boomerang" and a linker domain at the center. (wikipedia.org)
  • The catalytic mechanism of catechol 1,2-dioxygenase was elucidated using a combination of O18 labeling experiments and crystallography. (wikipedia.org)
  • caffeate
  • The transformation to ferulic acid is catalyzed by the enzyme caffeate O-methyltransferase. (wikipedia.org)
  • Dihydroxyphenylalanine ammonia-lyase was presumed to use 3,4-dihydroxy-L-phenylalanine (L-DOPA) to produce trans-caffeate and NH3. (wikipedia.org)
  • Caffeate O-methyltransferase is an enzyme responsible for the transformation of caffeic acid into ferulic acid. (wikipedia.org)
  • Caffeate 3,4-dioxygenase is an enzyme that uses caffeic acid and oxygen to produce 3-(2-carboxyethenyl)-cis,cis-muconate. (wikipedia.org)
  • oxidation
  • For instance, carbon-carbon bond cleavage, fatty acid hydroperoxidation, carbon-sulfur bond cleavage, and thiol oxidation are all reactions catalyzed by mononuclear iron dioxygenases. (wikipedia.org)
  • Chemical oxidation of caffeic acid in acidic conditions using sodium periodate leads to the formation of dimers with a furan structure (isomers of 2,5-(3′,4′-dihydroxyphenyl)tetrahydrofuran 3,4-dicarboxylic acid). (wikipedia.org)
  • Nitrogen
  • strain JS42 is able to utilize 2-nitrotoluene (2NT) as its sole carbon, nitrogen, and energy source. (nih.gov)
  • bacteria
  • 3. The composition of claim 1 wherein the host organism comprises bacteria of the Bacillus or Clostridia genera. (patents.com)
  • Catechols such as DHSA are produced through the metabolism of cholesterol by bacteria such as Mycobacterium tuberculosis. (wikipedia.org)
  • oxygenation
  • 1. Hayaishi, O. Direct oxygenation by O 2 , oxygenases. (qmul.ac.uk)
  • Despite this common oxygenation event, the mononuclear iron dioxygenases are diverse in how dioxygen activation is used to promote certain chemical reactions. (wikipedia.org)
  • strain
  • The genes coding for these enzymes are located on pVI150, an IncP-2 degradative mega plasmid of this strain. (diva-portal.org)
  • strain JS42 to 2-nitrotoluene. (nih.gov)
  • The 16S rDNA analysis revealed 99% nucleotide similarity to that of the type strain of R.rhodochrous (Fig. 2) ( 10 ). (kenyon.edu)
  • carbon-sulf
  • Glyoxalase I is classified as a carbon-sulfur lyase although, strictly speaking, the enzyme does not form or break a carbon-sulfur bond. (wikipedia.org)
  • chymotrypsin
  • Figure 4.4 illustrates the dramatic shifts that occur in the pH optimum of chymotrypsin, a proteolytic enzyme, following covalent immobilizations onto a polyornithine (positive) carrier and an ethylene-maleic anhydride copolymer (negative). (clicktocurecancer.info)
  • substrates
  • For example, in the α-ketoglutarate-dependent enzymes, one atom of dioxygen is incorporated into two substrates, with one always being α-ketoglutarate, and this reaction is brought about by a mononuclear iron center. (wikipedia.org)
  • O-methylated flavonoids formation implies the presence of specific O-methyltransferase (OMT) enzymes which accept a variety of substrates. (wikipedia.org)
  • 3-O-caffeoylshikimic acid (dactylifric acid) and its isomers, are enzymic browning substrates found in dates (Phoenix dactylifera fruits). (wikipedia.org)
  • Enzymology
  • In: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1293 (2). (iisc.ernet.in)
  • 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)
  • Oxidoreductases
  • This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. (wikipedia.org)
  • reaction
  • Fenton's reaction enzymes (iron homeostasis, reduction, hydrogen peroxide generation) were significantly expressed among all the datasets under lignocellulolytic conditions. (ijbs.com)
  • The two enzymes can be distinguished based on their reaction products and cofactors. (wikipedia.org)
  • An example of the reaction carried out by catechol 1,2-dioxygenase is the formation of cis,cis-muconic acid from catechol, shown below. (wikipedia.org)
  • genes
  • 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)
  • The genes coding for the conversion of carbazole to catechol are flanked by IS6100 elements in Sphingomonas sp. (wikipedia.org)
  • cleave
  • 1,2-CTD uses Fe3+ as a cofactor to cleave the carbon-carbon bond between the phenolic hydroxyl groups of catechol, thus yielding muconic acid as its product. (wikipedia.org)
  • In contrast, 2,3-CTD utilizes Fe2+ as a cofactor to cleave the carbon-carbon bond adjacent to the phenolic hydroxyl groups of catechol, thus yielding 2-hydroxymuconaldehye as its product. (wikipedia.org)
  • gene
  • Examples of recent gene duplication events in signaling as well as dioxygenase clusters are present, indicating selective gene family expansion as a relatively recent event in D. aromatica 's evolutionary history. (biomedcentral.com)
  • The human gene for this enzyme is called GLO1. (wikipedia.org)
  • effector
  • A number of proteins indicate interactions with an as yet unknown host, as indicated by the presence of predicted cell host remodeling enzymes, effector enzymes, hemolysin-like proteins, adhesins, NO reductase, and both type III and type VI secretory complexes. (biomedcentral.com)
  • The first is that the binding of the terminal phospholipids alters the conformation of the active sites, implying that the tunnel acts as an effector, only allowing the enzyme to be active in certain areas of the cell. (wikipedia.org)
  • synthase
  • One molecule of 4-coumaroyl-CoA is added to three molecules of malonyl-CoA to form tetrahydroxychalcone using 7,2′-dihydroxy-4′-methoxyisoflavanol synthase. (wikipedia.org)
  • employ
  • These enzyme do not use ACPSs, but instead employ coenzyme A esters and have a single active site to perform the necessary series of reactions, e.g. chain extension, condensation, and cyclization. (wikipedia.org)
  • skeleton
  • Catecholamines are biochemically significant hormones/neurotransmitters that are phenethylamines in which the phenyl group has a catechol skeleton structure. (wikipedia.org)
  • Flavan-3-ols (sometimes referred to as flavanols) are derivatives of flavans that use the 2-phenyl-3,4-dihydro-2H-chromen-3-ol skeleton. (wikipedia.org)
  • widely
  • Catechol is the conjugate acid of a chelating agent used widely in coordination chemistry. (wikipedia.org)
  • Catechol moieties are also found widely within the natural world. (wikipedia.org)
  • In recent years, 2-D electrophoresis has been widely accepted as a standard procedure to separate complex protein mixtures in proteome studies (Proteomics). (wikipedia.org)
  • hydrogen peroxide
  • Catechol is produced industrially by the hydroxylation of phenol using hydrogen peroxide. (wikipedia.org)
  • C6H5OH + H2O2 → C6H4(OH)2 + H2O Previously, it was produced by hydroxylation of salicylaldehyde using hydrogen peroxide, as well as the hydrolysis of 2-substituted phenols, especially 2-chlorophenol, with hot aqueous solutions containing alkali metal hydroxides. (wikipedia.org)
  • humans
  • The bioavailability of quercetin in humans is low and highly variable (0-50%), and it is rapidly cleared with an elimination half-life of 1-2 hours after ingesting quercetin foods or supplements. (wikipedia.org)
  • acid
  • Its methyl ether derivative, guaiacol, converts to catechol via hydrolysis of the CH3-O bond as promoted by hydriodic acid. (wikipedia.org)
  • The enzyme is inactivated by adding an acid, such as lemon juice. (wikipedia.org)
  • Dioxygenation and spontaneous deamination of 2-aminobenzene sulphonic acid in Alcaligenes sp. (wikipedia.org)
  • Metabolism of 4-amino-3-hydroxybenzoic acid by Bordetella sp. (wikipedia.org)
  • The transformation to ferulic acid is catalyzed by the enzyme caffeate O-methyltransferase. (wikipedia.org)
  • Caffeate O-methyltransferase is an enzyme responsible for the transformation of caffeic acid into ferulic acid. (wikipedia.org)
  • Caffeate 3,4-dioxygenase is an enzyme that uses caffeic acid and oxygen to produce 3-(2-carboxyethenyl)-cis,cis-muconate. (wikipedia.org)
  • Chemical oxidation of caffeic acid in acidic conditions using sodium periodate leads to the formation of dimers with a furan structure (isomers of 2,5-(3′,4′-dihydroxyphenyl)tetrahydrofuran 3,4-dicarboxylic acid). (wikipedia.org)
  • atoms
  • Rather, the enzyme shifts two hydrogen atoms from one carbon atom of the methylglyoxal to the adjacent carbon atom. (wikipedia.org)
  • Alcaligenes
  • in the degradative pathways of 2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic acids in Alcaligenes sp. (wikipedia.org)
  • carbon
  • Collectively these fungi are major inhabitants of forest biomass thus, playing a major role in carbon cycling and recycling of nutrients [ 1 , 2 ]. (ijbs.com)
  • Glyoxalase I is classified as a carbon-sulfur lyase although, strictly speaking, the enzyme does not form or break a carbon-sulfur bond. (wikipedia.org)
  • iron
  • Iron-containing dioxygenases can be subdivided into three classes on the basis of how iron is incorporated into the active site: those employing a mononuclear iron center, those containing a Rieske [2Fe-2S] cluster, and those utilizing a heme prosthetic group. (wikipedia.org)
  • Most mononculear iron dioxygenases are members of the cupin superfamily in which the overall domain structure is described as a six-stranded β-barrel fold (or jelly roll motif). (wikipedia.org)
  • At the center this barrel structure is a metal ion, most commonly ferrous iron, whose coordination environment is frequently provided by residues in two partially conserved structural motifs: G(X)5HXH(X)3-4E(X)6G and G(X)5-7PXG(X)2H(X)3N. (wikipedia.org)
  • Two important groups of mononuclear, non-heme iron dioxygenases are catechol dioxygenases and 2-oxoglutarate (2OG)-dependent dioxygenases. (wikipedia.org)
  • In the 2OG-dependent dioxygenases, ferrous iron (Fe(II)) is also coordinated by a (His)2(Glu/Asp)1 "facial triad" motif. (wikipedia.org)
  • The active site of catechol dioxygenases most frequently contains iron, but manganese-containing forms are also known. (wikipedia.org)
  • A novel non-heme iron-containing dioxygenase. (wikipedia.org)