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Literature summary for 1.13.11.24 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)

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ can partly substitute for Mn2+ Bacillus subtilis
Cu2+ can partly substitute for Mn2+ Bacillus subtilis
Fe2+ can partly substitute for Mn2+ Bacillus subtilis
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
Mn2+ preferred divalent metal ion Bacillus subtilis
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
Ni2+ can partly substitute for Mn2+. Nickel is a poor cofactor. Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
quercetin + O2
-
Bacillus subtilis 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
?
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

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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]

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