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Literature summary for 1.3.3.5 extracted from

  • Khlupova, M.E.; Vasileva, I.S.; Shumakovich, G.P.; Morozova, O.V.; Chertkov, V.A.; Shestakova, A.K.; Kisin, A.V.; Yaropolov, A.I.
    Enzymatic polymerization of dihydroquercetin using bilirubin oxidase (2015), Biochemistry (Moscow), 80, 233-241 .
    View publication on PubMed
Search for more literature for 1.3.3.5

Application

Application Comment Organism
synthesis enzymatic oxidative polymerization of dihydroquercetin from Larix sibirica using bilirubin oxidase as a biocatalyst. As compared with the monomer, oligoDHQ demonstrates higher thermal stability and high antioxidant activity Albifimbria verrucaria

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+
-
 Albifimbria verrucaria

Organism

Organism UniProt Comment Textmining
Albifimbria verrucaria Q12737
-
-

Purification (Commentary)

Purification (Comment) Organism
the commercial preparation of bilirubin oxidase from Myrothecium verrucaria is additionally purified by anion exchange chromatography Albifimbria verrucaria

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Albifimbria verrucaria
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
-
 Albifimbria verrucaria ? + H2O
-
 ?
ferricyanide + O2
-
 Albifimbria verrucaria ? + H2O
-
 ?
additional information oxidative polymerization of dihydroquercetin from Larix sibirica using bilirubin oxidase as a biocatalyst. DHQ oligomers (oligoDHQ) with molecular mass of 2800 and polydispersity of 8.6 are obtained by enzymatic reaction under optimal conditions. The oligomers appear to be soluble in dimethylsulfoxide, dimethylformamide, and methanol. UVvisible spectra of oligoDHQ in dimethylsulfoxide indicate the presence of highly conjugated bonds. Irregular structure of a polymer formed via the enzymatic oxidation of DHQ followed by nonselective radical polymerization. As compared with the monomer, oligoDHQ demonstrates higher thermal stability and high antioxidant activity Albifimbria verrucaria ?
-
 ?

pH Range

pH Minimum pH Maximum Comment Organism
3 9.5 activity range, inactive above and below. In reaction with electron donor substrates, the enzyme exhibits the maximal activity at acidic pH values: pH 4.0 for 2,2'-azino-bis-[3-ethylbenzthiazoline-6-sulfonic acid] (ABTS) and pH 3.0 for potassium ferricyanide. Catalytic activity decreases on pH increase, and the enzyme becomes completely inactive at pH above 9.5. At neutral pH values, bilirubin oxidase retains about 50% maximal activity in oxidation of both substrates. In reaction with a hydrogen atom donor (catechol), the pH profile of the enzyme activity is shifted to alkaline values: enzymatic activity is not exhibited at pH below 6.0. This is probably related with the higher reactivity of the substrate as a phenolate anion Albifimbria verrucaria

General Information

General Information Comment Organism
physiological function the enzyme is a copper-containing oxidase that catalyzes oxidation of various organic compounds, including phenolic ones, by molecular oxygen, the latter is reduced to water via a fourelectron mechanism Albifimbria verrucaria