1.13.11.3: protocatechuate 3,4-dioxygenase
This is an abbreviated version!
For detailed information about protocatechuate 3,4-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.3
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1.13.11.3
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catecholate
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1,2-dioxygenase
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intradiol
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4-hydroxybenzoate
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3,4-dihydroxybenzoate
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beta-ketoadipate
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ring-cleavage
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gentisate
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beta-carboxy-cis,cis-muconate
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enol-lactone
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hydroxyquinol
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orville
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lipscomb
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fuscum
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cis-muconate
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4-methylcatechols
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3,5-di-tert-butylcatechol
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analysis
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environmental protection
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degradation
- 1.13.11.3
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catecholate
-
1,2-dioxygenase
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intradiol
- 4-hydroxybenzoate
- 3,4-dihydroxybenzoate
-
beta-ketoadipate
-
ring-cleavage
- gentisate
- beta-carboxy-cis,cis-muconate
-
enol-lactone
- hydroxyquinol
-
orville
-
lipscomb
- fuscum
-
cis-muconate
- 4-methylcatechols
- 3,5-di-tert-butylcatechol
- analysis
- environmental protection
- degradation
Reaction
Synonyms
3,4-PCase, 3,4-PCD, 3,4-PCDase, 3,4-POD, EC 1.13.1.3, EC 1.99.2.3, More, oxygenase, protocatechuate 3,4-di-, P3,4DO, P3,4O enzyme, P34O, PCA 3,4-dioxygenase, PcaG, PcaH, PcaHG, PCD, protocatchetuate 3,4-dioxygenase, protocatechuate 3,4-dioxygenase, protocatechuate oxygenase, protocatechuic 3,4-dioxygenase, protocatechuic 3,4-oxygenase, protocatechuic acid oxidase
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Reaction
Reaction on EC 1.13.11.3 - protocatechuate 3,4-dioxygenase
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proposed reaction mechanism
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3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate
proposed mechanism based on Mössbauer, EPR and inhibition kinetic data
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3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate
examining a distorted trigonal-bipyramidal geometry observed for the non-heme iron center in protocatechuate 3,4-dioxygenase by utilizing a sterically hindered iron salen complex gives following results: the extent of a structural change of the iron center from a preferred square-pyramidal to a distorted trigonal-bipyramidal geometry varies with the external ligand that is bound in the order Cl <
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3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate
the computational (hybrid density functional method B3LYP) results of the catalytic cycle of the intradiol dioxygenases suggest: (1)binging of the substrate as a dianion (2) binding of dioxygen to the metal aided by an electron transfer from the substrate to O2 (3) formation of a bridging peroxo intermediate and its conformational change, which opens the coordination site trans to His462, (4) binding of a neutral XOH ligand (H2O or Tyr447) at the open site, (5) proton transfer from XOH to the neighboring peroxo ligand yielding the hydroperoxo intermediate, (6) a Criegee rearrangment leading to the anhydride intermediate (the criegee mechanism requires an in-plane oriantation of the involved two oxygen and two carbon atoms. Under some conditions homolytic O-O bond cleavage might compete with the Criegee rearangment.) and (7) hydrolysis of the anhydride to the final acyclic product.
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