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Literature summary extracted from

  • Kumar, M.; Zapata, A.; Ramirez, A.; Bowen, S.; Francisco, W.; Farmer, P.
    Nitrosyl hydride (HNO) replaces dioxygen in nitroxygenase activity of manganese quercetin dioxygenase (2011), Proc. Natl. Acad. Sci. USA, 108, 18926-18931.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.24 expression of Fe-QDO in Escherichia coli Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.24 additional information
-
 additional information kinetics, modeling, overview Bacillus subtilis
1.13.11.24 0.004
-
 quercetin pH 7.0, temperature not specified in the publication Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.24 Co2+ can partly substitute for Mn2+ Bacillus subtilis
1.13.11.24 Cu2+ can partly substitute for Mn2+ Bacillus subtilis
1.13.11.24 Fe2+ can partly substitute for Mn2+ Bacillus subtilis
1.13.11.24 HNO nitrosyl hydride replaces dioxygen in nitroxygenase activity of manganese quercetin dioxygenase resulting in the incorporation of both N and O atoms into the product. Turnover is demonstrated by consumption of quercetin and other related substrates under anaerobic conditions in the presence of HNO-releasing compounds and the enzyme. As with dioxygenase activity, a nonenzymatic base-catalyzed reaction of quercetin with HNO isobserved above pH 7, but no enhancement of this basal reactivity is found upon addition of divalent metal salts. Unique and regioselective N-containing products are characterized by MS analysis for both the enzymatic and nonenzymatic reactions Bacillus subtilis
1.13.11.24 Mn2+ preferred divalent metal ion Bacillus subtilis
1.13.11.24 additional information the enzyme from Bacillus subtilis is active with several divalent metal cofactors such as Fe, Mn, and Co, although Mn(II) is the preferred cofactor for this enzyme Bacillus subtilis
1.13.11.24 Ni2+ can partly substitute for Mn2+. Nickel is a poor cofactor. Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.24 quercetin + O2 Bacillus subtilis quercetin dioxygenase catalyzes the oxidation of the flavonol quercetin with dioxygen, cleaving the central heterocyclic ring and releasing CO 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.24 Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.24 quercetin + O2
-
 Bacillus subtilis 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?
1.13.11.24 quercetin + O2 quercetin dioxygenase catalyzes the oxidation of the flavonol quercetin with dioxygen, cleaving the central heterocyclic ring and releasing CO Bacillus subtilis 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.24 Co-QDO
-
 Bacillus subtilis
1.13.11.24 Fe-QDO
-
 Bacillus subtilis
1.13.11.24 manganese quercetin dioxygenase
-
 Bacillus subtilis
1.13.11.24 Mn-QDO
-
 Bacillus subtilis
1.13.11.24 QDO
-
 Bacillus subtilis
1.13.11.24 quercetin dioxygenase
-
 Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.24 7
-
 assay at Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.13.11.24 additional information
-
 nonenzymatic, basal reactivity of sodium trioxodinitrate/Na2N2O3 (Angeli's salt) as HNO donor with quercetin initiates above pH 7.0 Bacillus subtilis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.13.11.24 33000
-
 quercetin pH 7.0, temperature not specified in the publication Bacillus subtilis