1.13.11.15: 3,4-dihydroxyphenylacetate 2,3-dioxygenase
This is an abbreviated version!
For detailed information about 3,4-dihydroxyphenylacetate 2,3-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.15
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1.13.11.15
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extradiol
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catecholate
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4-nitrocatechol
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fuscum
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brevibacterium
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globiformis
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manganese-dependent
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ring-cleaving
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extradiol-cleaving
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second-sphere
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monoanionic
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hydroperoxo
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4-hydroxyphenylacetate
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superoxo
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alkylperoxo
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feiii-superoxo
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manganeseii
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ortho-dihydroxylated
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side-on
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crystallo
- 1.13.11.15
-
extradiol
-
catecholate
- 4-nitrocatechol
- fuscum
-
brevibacterium
- globiformis
-
manganese-dependent
-
ring-cleaving
-
extradiol-cleaving
-
second-sphere
-
monoanionic
-
hydroperoxo
- 4-hydroxyphenylacetate
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superoxo
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alkylperoxo
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feiii-superoxo
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manganeseii
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ortho-dihydroxylated
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side-on
-
crystallo
Reaction
Synonyms
2,3-HPCD, 3,4-dihydroxyphenylacetic acid 2,3-dioxygenase, Bf 2,3-HPCD, DHPAO, Fe-HPCD, Fe-MndD, FeHPCD, homoprotocatechuate 2,3 dioxygenase, homoprotocatechuate 2,3-dioxygenase, homoprotocatechuate dioxygenase, HPADO, HPC 2,3-dioxygenase, HPC dioxygenase, HPCA 2,3-dioxygenase, HPCD, Mn(II)-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase, Mn-HPCD, Mn-MndD, MndD, MnHPCD, oxygenase, homoprotocatechuate 2,3-di-, PaDHPAO
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1.13.11.15 3,4-dihydroxyphenylacetate 2,3-dioxygenaseAdvanced search results
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results (General Information
General Information on EC 1.13.11.15 - 3,4-dihydroxyphenylacetate 2,3-dioxygenase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
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In mutant Y257F, steps of the catalytic cycle are slowed by as much as 100fold by the mutation compared to the wild-type enzyme due to failure of mutant Y257F to facilitate the observed distortion of the bound 3,4-dihydroxyphenylacetate that is proposed to promote transfer of one electron to O2, Steady-state and transient kinetic analyses
metabolism
the catalytic reaction with substrate 4-nitrocatechol is comprised of four steps: (1) A dioxygen attacks the aromatic ring to produce an alkylperoxo species. (2) O-O bond cleavage and the formation of an epoxide species occur. (3) A seven-membered O-heterocyclic compound is generated by the extinction of the epoxy structure. (4) The seven-membered ring undergoes ring opening to form the final product (C2-C3 cleavage product). The effective free energy barrier of the catalytic reaction of the system is 26.2 kcal/mol
additional information
evolution
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the enzyme PaDHPAO likely belongs to the mononuclear non-heme metal-containing 2-His-1-carboxylate facial triad enzyme superfamily
evolution
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the enzyme PaDHPAO likely belongs to the mononuclear non-heme metal-containing 2-His-1-carboxylate facial triad enzyme superfamily
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additional information
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proposed mechanism for homoprotocatechuate binding to homoprotocatechuate 2,3-dioxygenase, substrate binding structure and thermodynamics, isothermal titration calorimetry analysis, overview
additional information
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reaction mechanism and intermediate formation, Mössbauer spectral analysis of wild-type and Y257F mutant enzymes, detailed overview. Residue His200 is positioned to interact with both the substrate C4-OH substituent and the bound oxygen. It plays many roles including that of an acid-base catalyst to promote the Criegee rearrangement chemistry
additional information
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the enzyme requires Fe2+ for catalysis, but Mn2+ can be substituted (MnHPCD) with essentially no change in the steady-state kinetic parameters, spectral analysis, overview
