Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Fetzner, S.
    Ring-cleaving dioxygenases with a cupin fold (2012), Appl. Environ. Microbiol., 78, 2505-2514.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.24 expression in Escherichia coli Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.13.11.24 extracellular
-
 Aspergillus japonicus
-
-
1.13.11.24 extracellular
-
 Penicillium olsonii
-
-

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 Co2+ can partly substitute for Ni2+ Streptomyces sp.
1.13.11.24 Cu2+ can partly substitute for Mn2+ Bacillus subtilis
1.13.11.24 Cu2+ required, the copper ion is mainly coordinated by three His residues and a water molecule in a distorted tetrahedral geometry. In a minor form, the metal is penta-coordinated by three His, a glutamate, and an aquo ligand in a trigonal bipyramidal geometry. The major role of the activesite metal ion could be to correctly position the substrate and to stabilize transition states and intermediates rather than to mediate electron transfer Aspergillus japonicus
1.13.11.24 Cu2+ required, the major role of the activesite metal ion could be to correctly position the substrate and to stabilize transition states and intermediates rather than to mediate electron transfer Penicillium olsonii
1.13.11.24 Fe2+ can partly substitute for Mn2+ Bacillus subtilis
1.13.11.24 Fe2+ can partly substitute for Ni2+ Streptomyces sp.
1.13.11.24 Mn2+ can partly substitute for Ni2+ Streptomyces sp.
1.13.11.24 Mn2+ preferred divalent metal ion Bacillus subtilis
1.13.11.24 additional information fungal quercetinases appear to exclusively utilize a Cu2+ ion for catalysis Aspergillus japonicus
1.13.11.24 additional information fungal quercetinases appear to exclusively utilize a Cu2+ ion for catalysis Penicillium olsonii
1.13.11.24 additional information the bacterial enzyme is capable of using different divalent metal ions for catalysis, with preference Mn2+, Co2+, Fe2+, Ni2+, Cu2+in descending order, suggesting that the redox properties of the metal are relatively unimportant for the catalytic reaction. The major role of the active site metal ion could be to correctly position the substrate and to stabilize transition states and intermediates rather than to mediate electron transfer. The recombinant enzyme is able to exchange its active-site metal ion while retaining catalytic activity Bacillus subtilis
1.13.11.24 additional information the bacterial enzyme is capable of using different divalent metal ions for catalysis, with preference Ni2+, Co2+, Mn2+, Fe2+ in descending order, suggesting that the redox properties of the metal are relatively unimportant for the catalytic reaction. The major role of the active site metal ion could be to correctly position the substrate and to stabilize transition states and intermediates rather than to mediate electron transfer Streptomyces sp.
1.13.11.24 Ni2+ can partly substitute for Mn2+. Nickel is a poor cofactor. Bacillus subtilis
1.13.11.24 Ni2+ preferred divalent metal ion Streptomyces sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.24 additional information Bacillus subtilis the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol ?
-
 ?
1.13.11.24 additional information Streptomyces sp. the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol ?
-
 ?
1.13.11.24 additional information Aspergillus japonicus the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol ?
-
 ?
1.13.11.24 additional information Penicillium olsonii the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol ?
-
 ?
1.13.11.24 additional information Streptomyces sp. FLA / DSM 41951 the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol ?
-
 ?
1.13.11.24 quercetin + O2 Bacillus subtilis
-
 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?
1.13.11.24 quercetin + O2 Streptomyces sp.
-
 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?
1.13.11.24 quercetin + O2 Aspergillus japonicus
-
 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?
1.13.11.24 quercetin + O2 Penicillium olsonii
-
 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?
1.13.11.24 quercetin + O2 Streptomyces sp. FLA / DSM 41951
-
 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.24 Aspergillus japonicus
-
-
-
1.13.11.24 Bacillus subtilis
-
-
-
1.13.11.24 Penicillium olsonii
-
-
-
1.13.11.24 Streptomyces sp.
-
-
-
1.13.11.24 Streptomyces sp. FLA / DSM 41951
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.24 additional information the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol Bacillus subtilis ?
-
 ?
1.13.11.24 additional information the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol Streptomyces sp. ?
-
 ?
1.13.11.24 additional information the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol Aspergillus japonicus ?
-
 ?
1.13.11.24 additional information the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol Penicillium olsonii ?
-
 ?
1.13.11.24 additional information the enzyme opens up two C-C bonds of the heterocyclic ring of quercetin, a widespread plant flavonol Streptomyces sp. FLA / DSM 41951 ?
-
 ?
1.13.11.24 quercetin + O2
-
 Bacillus subtilis 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?
1.13.11.24 quercetin + O2
-
 Streptomyces sp. 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?
1.13.11.24 quercetin + O2
-
 Aspergillus japonicus 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?
1.13.11.24 quercetin + O2
-
 Penicillium olsonii 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?
1.13.11.24 quercetin + O2
-
 Streptomyces sp. FLA / DSM 41951 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.11.24 homodimer bicupin domain structure Bacillus subtilis
1.13.11.24 homodimer bicupin domain structure Aspergillus japonicus
1.13.11.24 homodimer bicupin domain structure Penicillium olsonii
1.13.11.24 homodimer monocupin domain structure Streptomyces sp.

Synonyms

EC Number Synonyms Comment Organism
1.13.11.24 flavonol 2,4-dioxygenase
-
 Bacillus subtilis
1.13.11.24 flavonol 2,4-dioxygenase
-
 Streptomyces sp.
1.13.11.24 flavonol 2,4-dioxygenase
-
 Aspergillus japonicus
1.13.11.24 flavonol 2,4-dioxygenase
-
 Penicillium olsonii
1.13.11.24 quercetinase
-
 Bacillus subtilis
1.13.11.24 quercetinase
-
 Streptomyces sp.
1.13.11.24 quercetinase
-
 Aspergillus japonicus
1.13.11.24 quercetinase
-
 Penicillium olsonii
1.13.11.24 type III extradiol dioxygenase
-
 Bacillus subtilis
1.13.11.24 type III extradiol dioxygenase
-
 Streptomyces sp.
1.13.11.24 type III extradiol dioxygenase
-
 Aspergillus japonicus
1.13.11.24 type III extradiol dioxygenase
-
 Penicillium olsonii

General Information

EC Number General Information Comment Organism
1.13.11.24 evolution the ring-cleaving dioxygenase belongs to the cupin superfamily, characterized by a six-stranded beta-barrel fold and conserved amino acid motifs that provide the 3His or 2- or 3His-1Glu ligand environment of a divalent metal ion. The cupin domain comprises two conserved amino acid motifs with the consensus sequences G(X)5HXH(X)3-4E(X)6G (motif 1) and G(X)5-7PXG(X)2H(X)3N Bacillus subtilis
1.13.11.24 evolution the ring-cleaving dioxygenase belongs to the cupin superfamily, characterized by a six-stranded beta-barrel fold and conserved amino acid motifs that provide the 3His or 2- or 3His-1Glu ligand environment of a divalent metal ion. The cupin domain comprises two conserved amino acid motifs with the consensus sequences G(X)5HXH(X)3-4E(X)6G (motif 1) and G(X)5-7PXG(X)2H(X)3N Streptomyces sp.
1.13.11.24 evolution the ring-cleaving dioxygenase belongs to the cupin superfamily, characterized by a six-stranded beta-barrel fold and conserved amino acid motifs that provide the 3His or 2- or 3His-1Glu ligand environment of a divalent metal ion. The cupin domain comprises two conserved amino acid motifs with the consensus sequences G(X)5HXH(X)3-4E(X)6G (motif 1) and G(X)5-7PXG(X)2H(X)3N Aspergillus japonicus
1.13.11.24 evolution the ring-cleaving dioxygenase belongs to the cupin superfamily, characterized by a six-stranded beta-barrel fold and conserved amino acid motifs that provide the 3His or 2- or 3His-1Glu ligand environment of a divalent metal ion. The cupin domain comprises two conserved amino acid motifs with the consensus sequences G(X)5HXH(X)3-4E(X)6G (motif 1) and G(X)5-7PXG(X)2H(X)3N Penicillium olsonii
1.13.11.24 additional information enzyme-bound quercetin shields the FeII cofactor from interactions with the O2 mimic nitric oxide, tentatively suggesting that the reaction catalyzed by Bacillus (Fe-)quercetinase may proceed without direct interaction of dioxygen and metal ion, overview Bacillus subtilis
1.13.11.24 additional information the mechanism which involves initial electron transfer from the divalent metal to O2, as proposed for the extradiol dioxygenases, requires that a MIII-superoxo state is thermodynamically accessible, overview Streptomyces sp.