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Information on EC 1.13.11.3 - protocatechuate 3,4-dioxygenase
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1.13.11.3 protocatechuate 3,4-dioxygenaseIUBMB Comments
Requires Fe3+. The enzyme, which participates in the degradation of aromatic compounds, catalyses the intradiol addition of both oxygen atoms from molecular oxygen, resulting in ortho-cleavage of the aromatic ring. The type of cleavage leads to mineralization via the intermediate 3-oxoadipate.
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Word Map
- 1.13.11.3
-
catecholate
-
1,2-dioxygenase
-
intradiol
- p-hydroxybenzoate
- 3,4-dihydroxybenzoate
-
beta-ketoadipate
- gentisate
-
ring-cleavage
- beta-carboxy-cis,cis-muconate
- enol-lactone
- fuscum
-
lipscomb
-
orville
- hydroxyquinol
- 3,5-di-tert-butylcatechol
- 4-methylcatechols
- analysis
- environmental protection
- degradation
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3,4-PCD
EC 1.13.1.3
-
-
formerly
-
EC 1.99.2.3
-
-
formerly
-
oxygenase, protocatechuate 3,4-di-
-
-
-
-
P3,4DO
P34O
PcaG
PcaH
PcaHG
protocatechuate 3,4-dioxygenase
protocatechuate oxygenase
-
-
-
-
protocatechuic 3,4-dioxygenase
-
-
-
-
protocatechuic 3,4-oxygenase
-
-
-
-
protocatechuic acid oxidase
-
-
-
-
additional information
additional information
-
Experiments with mutants where the pcaG genes contain variations in repeat sequences capable of producing a selectable phenotype following a specific deletion give following results: As a lower limit a sequence repition of 8 bp or greater in length is required for deletion frequencies to rise significantly above 1.5 x 10-8. Deletions occurr with a frequency of 7.2 x 10-8 in strains containing repetitions of 12 bp in length separated by 30 bp
additional information
-
Experiments with mutants where the pcaG genes contain variations in repeat sequences capable of producing a selectable phenotype following a specific deletion give following results: As a lower limit a sequence repition of 8 bp or greater in length is required for deletion frequencies to rise significantly above 1.5 x 10-8. Deletions occurr with a frequency of 7.2 x 10-8 in strains containing repetitions of 12 bp in length separated by 30 bp
-
additional information
-
the genetic locus ncg12314-ncg12315 encodes a putative protocatechuate 3,4-dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate
proposed mechanism based on Mössbauer, EPR and inhibition kinetic data
-
3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate
proposed reaction mechanism
-
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 <
-
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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3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
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reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
protocatechuate:oxygen 3,4-oxidoreductase (decyclizing)
Requires Fe3+. The enzyme, which participates in the degradation of aromatic compounds, catalyses the intradiol addition of both oxygen atoms from molecular oxygen, resulting in ortho-cleavage of the aromatic ring. The type of cleavage leads to mineralization via the intermediate 3-oxoadipate.
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CAS REGISTRY NUMBER
COMMENTARY
9029-47-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenylalanine + O2
?
Nocardia erythropolis
-
at 10.7% the rate of protocatechuic acid oxidation
-
-
?
3-(3,4-dihydroxyphenyl)propionate + O2
?
-
protocatechuate 3,4-dioxygenase II
-
-
?
5-fluoro-protocatechuic acid + O2
5-fluoro-3-carboxy-cis,cis-muconate
-
at 2.1% the rate of protocatechuic acid oxidation
-
?
6-chloro-protocatechuate + O2
6-chloro-3-carboxy-cis,cis-muconate
-
at 4.3% the rate of protocatechuic acid oxidation
-
?
2,3-dihydroxybenzoate + O2
?
I0DHJ0; I0DHJ1
23.6% of the activity with protocatechuate for the free enzyme, 149.3% for the calcium alginate-immobilized enzyme, and 119.8% for the glyoxyl agarose-immobilized enzyme
-
-
?
2,4-dihydroxybenzoate + O2
?
I0DHJ0; I0DHJ1
43.5% of the activity with protocatechuate for the free enzyme, 96.5% for the calcium alginate-immobilized enzyme, and 65.6% for the glyoxyl agarose-immobilized enzyme
-
-
?
2,5-dihydroxybenzoate + O2
?
I0DHJ0; I0DHJ1
33.5% of the activity with protocatechuate for the free enzyme, 158.6% for the calcium alginate-immobilized enzyme, and 72.1% for the glyoxyl agarose-immobilized enzyme
-
-
?
2,6-dihydroxybenzoate + O2
?
I0DHJ0; I0DHJ1
30.5% of the activity with protocatechuate for the free enzyme, 90.4% for the calcium alginate-immobilized enzyme, and 36.2% for the glyoxyl agarose-immobilized enzyme
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
absolute requirement for vicinal hydroxyl groups in the 3- and 4-position
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ir
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 2-chloro-protocatechuate
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 5-bromo-protocatechuate
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 5-chloro-protocatechuate
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
methylene blue cannot replace O2 as electron acceptor
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ir
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
Nocardia erythropolis
-
enzyme is active on a wide range of o-dihydroxyphenyl compounds
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
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very low activity with: 3,4-dihydroxyphenylacetic acid
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?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
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very low activity with 3,4-dihydroxymandelic acid
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?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
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very low activity with 4'-methylcatechol
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?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
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very low activity with: 3,4-dihydroxyphenylacetic acid
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?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
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very low activity with 3,4-dihydroxymandelic acid
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?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
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very low activity with 4'-methylcatechol
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?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
no other substrate found
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ir
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
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no other substrate found
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ir
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
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i.e. protocatechuate
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-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
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-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
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specific for protocatechuate
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
no other substrate found
-
?
3,4-dihydroxybenzoate + O2
?
-
spectroscopic and electronic structure study of the enzyme-substrate complex
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-
?
3,4-dihydroxybenzoate + O2
?
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spectroscopic and electronic structure study of the enzyme-substrate complex
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-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
I0DHJ0; I0DHJ1
29.5% of the activity with protocatechuate for the free enzyme, 95.0% for the calcium alginate-immobilized enzyme, and 41.1% for the glyoxyl agarose-immobilized enzyme
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
I0DHJ0; I0DHJ1
29.54% ctivity compared to 3,4-dihydroxybenzoate
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
I0DHJ0; I0DHJ1
29.54% ctivity compared to 3,4-dihydroxybenzoate
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
I0DHJ0; I0DHJ1
29.5% of the activity with protocatechuate for the free enzyme, 95.0% for the calcium alginate-immobilized enzyme, and 41.1% for the glyoxyl agarose-immobilized enzyme
-
-
?
3,4-dihydroxymandelic acid + O2
?
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protocatechuate 3,4-dioxygenase II
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-
?
3,4-dihydroxymandelic acid + O2
?
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protocatechuate 3,4-dioxygenase II
-
-
?
3,4-dihydroxymandelic acid + O2
?
Nocardia erythropolis
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at 5.4% the rate of protocatechuic acid oxidation
-
-
?
3,4-dihydroxyphenylacetate + O2
?
-
W153V protocatechuate 3,4-dioxygenase I mutant enzyme: 13% activity compared to protocatechuate, wild-type protocatechuate 3,4-dioxygenase I: 2% activity compared to protocatechuate
-
-
-
3,5-dihydroxybenzoate + O2
?
I0DHJ0; I0DHJ1
44.3% of the activity with protocatechuate for the free enzyme, 113.3% for the calcium alginate-immobilized enzyme, and 42.9% for the glyoxyl agarose-immobilized enzyme
-
-
?
3-methylcatechol + O2
2-methylmuconate
-
at 5% the rate of protocatechuic acid oxidation
-
?
3-methylcatechol + O2
2-methylmuconate
Nocardia erythropolis
-
at 14.4% the rate of protocatechuic acid oxidation
-
?
3-methylcatechol + O2
2-methylmuconate
-
at 0.4% the rate of protocatechuic acid oxidation
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
at very low rates
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
at very low rates
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
at very low rates
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
at very low rates
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
Nocardia erythropolis
-
at 3.1% the rate of protocatechuic acid oxidation
-
?
4-sulfocatechol + O2
3-sulfomuconate
-
catalyzed by protocatechuate 3,4-dioxgenase type II only
-
?
4-sulfocatechol + O2
3-sulfomuconate
-
catalyzed by protocatechuate 3,4-dioxgenase type II only
-
?
4-sulfocatechol + O2
3-sulfomuconate
-
catalyzed by protocatechuate 3,4-dioxgenase type II only
-
?
caffeic acid + O2
?
I0DHJ0; I0DHJ1
34.2% of the activity with protocatechuate for the free enzyme, 150% for the calcium alginate-immobilized enzyme, and 97% for the glyoxyl agarose-immobilized enzyme
-
-
?
caffeic acid + O2
?
I0DHJ0; I0DHJ1
34.2% of the activity with protocatechuate for the free enzyme, 150% for the calcium alginate-immobilized enzyme, and 97% for the glyoxyl agarose-immobilized enzyme
-
-
?
catechol + O2
cis,cis-muconate
-
reaction of EC 1.13.11.1
-
-
?
catechol + O2
cis,cis-muconate
-
reaction of EC 1.13.11.1
-
-
?
catechol + O2
muconate
-
at 3% the rate of protocatechuic acid oxidation
-
?
catechol + O2
muconate
Nocardia erythropolis
-
at 33.8% the rate of protocatechuic acid oxidation
-
?
catechol + O2
muconate
-
at 0.4% the rate of protocatechuic acid oxidation
-
?
catechol + O2
muconate
-
at 0.4% the rate of protocatechuic acid oxidation
-
?
pyrogallol + O2
?
-
at 10% the rate of protocatechuic acid oxidation
-
-
?
pyrogallol + O2
?
Nocardia erythropolis
-
at 36% the rate of protocatechuic acid oxidation
-
-
?
pyrogallol + O2
?
-
at 0.4% the rate of protocatechuic acid oxidation
-
-
?
pyrogallol + O2
?
-
at 0.4% the rate of protocatechuic acid oxidation
-
-
?
trans-3,4-dihydroxycinnamate + O2
?
-
W153V protocatechuate 3,4-dioxygenase I mutant enzyme: 35% activity compared to protocatechuate, wild-type protocatechuate 3,4-dioxygenase I: 2% activity compared to protocatechuate
-
-
-
additional information
?
-
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
-
additional information
?
-
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
-
additional information
?
-
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
-
additional information
?
-
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
-
additional information
?
-
-
enzyme involved in last ring fission in naphtalene degradation, intermediates confirm proceeding through protocatechuic acid via ortho-claevage pathway
-
-
-
additional information
?
-
-
the enzyme is active on a wide range of phenyl compounds, in contrast to the high specificity of similar enzymes from other sources
-
-
-
additional information
?
-
-
the enzyme is active on a wide range of phenyl compounds, in contrast to the high specificity of similar enzymes from other sources
-
-
-
additional information
?
-
-
strain KB2 degrades 13 mM 3,4-dihydroxybenzoate, 10 mM benzoic acid and 12 mM phenol within 24 h of incubation
-
-
-
additional information
?
-
I0DHJ0; I0DHJ1
protocatechuate 3,4-dioxygenase from KB2 strain shows activity against various dihydroxybenzoic acids, but highest activity with primary substrate protocatechuate. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate, overview
-
-
-
additional information
?
-
-
protocatechuate 3,4-dioxygenase from KB2 strain shows activity against various dihydroxybenzoic acids, but highest activity with primary substrate protocatechuate. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate, overview
-
-
-
additional information
?
-
-
strain KB2 degrades 13 mM 3,4-dihydroxybenzoate, 10 mM benzoic acid and 12 mM phenol within 24 h of incubation
-
-
-
additional information
?
-
I0DHJ0; I0DHJ1
protocatechuate 3,4-dioxygenase from KB2 strain shows activity against various dihydroxybenzoic acids, but highest activity with primary substrate protocatechuate. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate, overview
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
A0A193DXA9 and A0A193DXP2
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
Q0SH27 AND Q0SH26
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
I0DHJ0 AND I0DHJ1
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
I0DHJ0 AND I0DHJ1
100% activity
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
I0DHJ0 AND I0DHJ1
100% activity
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
I0DHJ0 AND I0DHJ1
-
-
-
?
additional information
?
-
A8I4B3
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
-
additional information
?
-
A8I4B7
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
-
additional information
?
-
A8I4B3
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
-
additional information
?
-
A8I4B7
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
-
additional information
?
-
-
enzyme involved in last ring fission in naphtalene degradation, intermediates confirm proceeding through protocatechuic acid via ortho-claevage pathway
-
-
-
additional information
?
-
-
the enzyme is active on a wide range of phenyl compounds, in contrast to the high specificity of similar enzymes from other sources
-
-
-
additional information
?
-
-
the enzyme is active on a wide range of phenyl compounds, in contrast to the high specificity of similar enzymes from other sources
-
-
-
additional information
?
-
-
strain KB2 degrades 13 mM 3,4-dihydroxybenzoate, 10 mM benzoic acid and 12 mM phenol within 24 h of incubation
-
-
-
additional information
?
-
-
strain KB2 degrades 13 mM 3,4-dihydroxybenzoate, 10 mM benzoic acid and 12 mM phenol within 24 h of incubation
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2,2'-dipyridyl
I0DHJ0; I0DHJ1
activates the enzyme immobilized on calcium alginate, but inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose, at 0.3 mM
Cu2+
-
increases enzyme activity for both cell-free and immobilized extracts by 8% and 44%, respectively
EDTA
I0DHJ0; I0DHJ1
activates the enzyme immobilized on calcium alginate, but inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose, at 0.3 mM
Fe
Fe3+
additional information
Fe
-
external addition of FeSO4 is absolutely essential, other metal ions cannot replace Fe2+
Fe3+
-
increases enzyme activity for both cell-free and immobilized extracts by 16% and 99%, respectively
Fe3+
-
presence of a alphabetaFe3+ protomer in a variety of stoichiometries
additional information
I0DHJ0; I0DHJ1
protective effect of immobilization on calcium alginate on enzyme activity is observed in the presence of Cd2+, Al3+, and Fe3+ while in the presence of Mn2+ and Zn2+ the inhibitory effect of metals on enzyme activity increases
additional information
-
protective effect of immobilization on calcium alginate on enzyme activity is observed in the presence of Cd2+, Al3+, and Fe3+ while in the presence of Mn2+ and Zn2+ the inhibitory effect of metals on enzyme activity increases
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-3-(3,4-dimethoxyphenyl)-N-hydroxyprop-2-enamide
over 90% inhibition at 0.2 mM
(2E)-N-hydroxy-3-(4-methoxyphenyl)prop-2-enamide
over 90% inhibition at 0.2 mM
1,10-phenanthroline
-
0.005 mM, approx. 50% inhibition after 30 min, complete inhibition after 60 min, complete restoration of inactivated enzyme by addition of excess ferric EDTA complex
2-(2H-1,3-benzodioxol-5-yl)-N-[(4-fluorophenyl)methyl]-N-hydroxyacetamide
60% inhibition at 0.2 mM
3-(3,4-dimethoxyphenyl)-N-hydroxy-N-octylpropanamide
57% inhibition at 0.2 mM
3-(3,4-dimethoxyphenyl)-N-hydroxypropanamide
60% inhibition at 0.2 mM
2,2'-dipyridyl
I0DHJ0; I0DHJ1
activates the enzyme immobilized on calcium alginate, but inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose, at 0.3 mM
2-Hydroxyisonicotinic acid N-oxide
-
0.000025 mM, 50% inactivation after 10 min, most potent inhibitor
butanol
I0DHJ0; I0DHJ1
inhibits the activity of the enzyme immobilized on glyoxyl agarose by 23.5% at 0.3 mM
EDTA
I0DHJ0; I0DHJ1
activates the enzyme immobilized on calcium alginate, but inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose, at 0.3 mM
ethanol
I0DHJ0; I0DHJ1
inhibits the activity of the enzyme immobilized on glyoxyl agarose by 50% at 0.3 mM
methanol
I0DHJ0; I0DHJ1
inhibits the activity of the enzyme immobilized on calcium alginate by 28% at 0.3 mM
Propanol
I0DHJ0; I0DHJ1
inhibits the activity of the enzyme immobilized on glyoxyl agarose by 23% at 0.3 mM
additional information
-
not inhibited by iodoacetamide, 5,5'-dithiobis(2-nitrobenzoate), mercaptoethanol, dithiothreitol, glutathione, o-phenanthroline and H2O2
-
additional information
-
not inhibited by arsenate, iodoacetate, semicarbazide, N-phenylmaleimide, fluoride or cyanide
-
additional information
poor inhibition by N-hydroxy-3-(4-methoxyphenyl)propanamide at 0.2 mM
-
additional information
-
poor inhibition by N-hydroxy-3-(4-methoxyphenyl)propanamide at 0.2 mM
-
additional information
I0DHJ0; I0DHJ1
protective effect of immobilization on calcium alginate on enzyme activity is observed in the presence of Cd2+, Al3+, and Fe3+ while in the presence of Mn2+ and Zn2+ the inhibitory effect of metals on enzyme activity increases
-
additional information
-
protective effect of immobilization on calcium alginate on enzyme activity is observed in the presence of Cd2+, Al3+, and Fe3+ while in the presence of Mn2+ and Zn2+ the inhibitory effect of metals on enzyme activity increases
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
butanol
I0DHJ0; I0DHJ1
activates the free enzyme and enzyme immobilized on calcium alginate by 20% and 9% at 0.3 mM, respectively
ethanol
I0DHJ0; I0DHJ1
activates the free enzyme and enzyme immobilized on calcium alginate by 42% and 56% at 0.3 mM, respectively
additional information
I0DHJ0; I0DHJ1
propanol has no effect on the activity of enzyme immobilized on calcium alginate at 0.3 mM
-
additional information
-
propanol has no effect on the activity of enzyme immobilized on calcium alginate at 0.3 mM
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06534
3,4-dihydroxybenzoate
free enzyme, at pH 7.4 and 37°C
0.095
3,4-dihydroxybenzoate
-
multi-walled carbon nanotube-immobilized enzyme, at pH 10.0 and 60°C
0.15929
3,4-dihydroxybenzoate
Fe3O4 nanoparticles-immobilized enzyme, at pH 7.4 and 37°C
additional information
additional information
-
measurement of Km at different pH values
-
additional information
additional information
-
rates (s-1) and dissocation constants (microM) for protocatechuate: Y408H: k+2 = 2.8, k-2 = 1.9, k+2 + k-2 = 4.7, K1 = 2600, Kd = 1100, Y408F: k+2 = 0.39, k-2 = 0.46, k+2 + k-2 = 0.85, K1 = 84, Kd = 45, Y408C: k+2 + k-2 = 0.67; substrate dissociation constant for protocatechuate: wild type = 2.5 microM, Y408H = 39 micro M, Y408C = 57 microM
-
additional information
additional information
-
the enzyme exhibits Michaelis-Menten kinetics for all substrates tested
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.3
3,4-dihydroxybenzoate
-
multi-walled carbon nanotube-immobilized enzyme, at pH 10.0 and 60°C
10.25
3,4-dihydroxybenzoate
free enzyme, at pH 7.4 and 37°C
15.97
3,4-dihydroxybenzoate
Fe3O4 nanoparticles-immobilized enzyme, at pH 7.4 and 37°C
0.007
protocatechuate
-
for the mutant enzyme Y408H, at 25°C in 50 mM Tris and 2 mM beta-mercaptoethanol, pH 8.5 under saturating protocatechuate and O2 conditions
0.01
protocatechuate
-
for the mutant enzyme Y408E, at 25°C in 50 mM Tris and 2 mM beta-mercaptoethanol, pH 8.5 under saturating protocatechuate and O2 conditions
0.011
protocatechuate
-
for the mutant enzyme Y408F, at 25°C in 50 mM Tris and 2 mM beta-mercaptoethanol, pH 8.5 under saturating protocatechuate and O2 conditions
0.13
protocatechuate
-
for the mutant enzyme Y408C, at 25°C in 50 mM Tris and 2 mM beta-mercaptoethanol, pH 8.5 under saturating protocatechuate and O2 conditions
100
protocatechuate
-
for the wild-type enzyme, at 25°C in 50 mM Tris and 2 mM beta-mercaptoethanol, pH 8.5 under saturating protocatechuate and O2 conditions
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
45.1
3,4-dihydroxybenzoate
-
multi-walled carbon nanotube-immobilized enzyme, at pH 10.0 and 60°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0068
2-Hydroxyisonicotinic acid N-oxide
-
apparent Ki, irreversible binding
3.9
2-Hydroxypyridine N-oxide
-
apparent Ki, inhibition is not freely reversible
additional information
additional information
-
rates (s-1) and dissociation constants (microM) for 4-hysroxybenzoate: wild type: k+2 = 42, k-2 = 14, k+2 + k-2 = 56, K1 = 700, Kd = 170, Y408H: k+2 + k-2 = 2.3, Y408C: k+2 + k-2 = 0.7, Y408F: k+2 + k-2 = 0.9; substrate dissociation constant for 3-hydroxybenzoate: wild type = 3500 microM, Y408H = 180 microM, Y408E = 210 microM, Y408C = 2500 microM, Y408F = 1800 microM; substrate dissociation constant for 4-hydroxybenzoate: wild type = 300 microM, Y408H = 6.3 microM, Y408C = 51 microM, Y408F = 12 microM
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
(2E)-3-(3,4-dimethoxyphenyl)-N-hydroxyprop-2-enamide
Rhodococcus jostii
Q0SH27 AND Q0SH26
pH 7.5, 37°C
0.015
(2E)-N-hydroxy-3-(4-methoxyphenyl)prop-2-enamide
Rhodococcus jostii
Q0SH27 AND Q0SH26
pH 7.5, 37°C
0.16
3-(3,4-dimethoxyphenyl)-N-hydroxypropanamide
Rhodococcus jostii
Q0SH27 AND Q0SH26
pH 7.5, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.113
-
activity in E. coli cell extracts expressing the recombinant enzyme
2.98
-
inductor 3,4-dihydroxybenzoic acid, cell-free extract from Stenotrophomonas maltophilia
5.2
-
type II protocatechuate 3,4-dioxygenase, oxidation of 4-sulfocatechol
6.37
-
inductor 4-hydroxybenzoic acid, cell-free extract from Stenotrophomonas maltophilia
8.7
-
inductor vanillic acid, cell-free extract from Stenotrophomonas maltophilia
16.7
-
type II protocatechuate 3,4-dioxygenase, oxidation of 4-sulfocatechol
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
9.2
8.5
-
maximum activity for the wild type enzyme and the mutants enymes Y408C, Y408F, Y408E and Y408H
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
the enzyme shows more than 50% activity between pH 5.5 and 8.5
6 - 9
-
pH 6.0: about 40% of maximal activity, pH 9.0: about 65% of maximal activity
7 - 11
I0DHJ0; I0DHJ1
the enzyme shows more than 50% activity between pH 7.0 and 11.0 and loses 98.3% of its original enzymatic activity at pH 4.0 and about 95.4% at pH 12.0
additional information
-
activity increases steadily up to pH 9.0, above pH 9.0 the enzyme begins to undergo spontaneous oxidation
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
37
40
45 - 50
55
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
the enzyme shows more than 50% activity between 20 and 70°C
50 - 70
-
50°C: about 55% of maximal activity, 70°C: about 60% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme is induced in cells grown on protocatechuic acid or analogues
-
-
brenda
Pseudomonas mendocina P2d, an array of colors are formed when Pseudomonas mendocia P2d cells grow in sodium or tyrosine, which is ascribed to the presence of multiple enzyms: catechol-1,2-doxygenase, catechol-2,3-dioxygenase, protocatechuate-3,4-dioxygenase, and tyrosinase
-
-
brenda
isolates GAI-16, S25com04 and IC4, enzyme activity is induced by growth on p-hydroxybenzoate
-
-
brenda
protocatechuate 3,4-dioxygenase alpha subunit
SwissProt
brenda
protocatechuate 3,4-dioxygenase beta subunit
SwissProt
brenda
protocatechuate 3,4-dioxygenase alpha subunit
SwissProt
brenda
protocatechuate 3,4-dioxygenase beta subunit
SwissProt
brenda
cells cultivated with protocatechuate, p-cresol, vanillate and 4-hydroybenzoate as sole carbon and energy surce for growth, exhibite protocatechuate 3,4-dioxygenase activities
-
-
brenda
thermophilic isolate G27 from high-temperature oilfield in Lithuania
-
-
brenda
American Type Culture Collection (ATCC) 23975, previously classified as Pseudomonas aeruginosa
-
-
brenda
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
-
-
brenda
previously classified as Pseudomonas aeruginosa strain ATCC 23975
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
monocyclic hydrocarbons, 4-hydroxybenzoic acid, protocatechuic acid and vanillic acid
brenda
-
monocyclic hydrocarbons, 4-hydroxybenzoic acid, protocatechuic acid and vanillic acid
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
localized in 100000 g supernatant, completely absent in mitochondrial, microsomal and chloroplast fraction
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
additional information
metabolism
-
protocatechuate 3,4-dioxygenase is the key enzyme of protocatechuate breakdown
metabolism
-
PCA 3,4-dioxygenase is essential for vanillate, 4-hydroxybenzoate, and protocatechuate assimilation
metabolism
-
the enzyme is involved in the degradation of the environmental pollutant 3-chlorobenzoate
metabolism
-
protocatechuate 3,4-dioxygenase is the key enzyme of protocatechuate breakdown
-
metabolism
-
protocatechuate 3,4-dioxygenase is the key enzyme of protocatechuate breakdown
-
metabolism
-
the enzyme is involved in the degradation of the environmental pollutant 3-chlorobenzoate
-
additional information
I0DHJ0; I0DHJ1
enzyme immobilized on calcium alginate gel binds to the carrier by electrostatic interaction while glyoxyl agarose is linked with the enzyme by covalent bonds. Since positively charged amino acids are localized at the entrance of crevasse, the electrostatic interaction plays the key role in modulation of enzyme activity. Significant increase of enzyme activity after its immobilization in calcium alginate is probably caused by strong electrostatic interactions between positively charged amino acid residues of the enzyme and negatively charged groups of alginate. High activity of immobilized protocatechuate 3,4-dioxygenase towards 2,3-dihydroxybenzoate, 2,5-dihydroxybenzoate, and 3,5-dihydroxybenzoate can be connected with modification of its catalytic mechanism as only 2,3-dihydroxybenzoate is in configuration typical for protocatechuate 3,4-dioxygenase's substrate
additional information
-
enzyme immobilized on calcium alginate gel binds to the carrier by electrostatic interaction while glyoxyl agarose is linked with the enzyme by covalent bonds. Since positively charged amino acids are localized at the entrance of crevasse, the electrostatic interaction plays the key role in modulation of enzyme activity. Significant increase of enzyme activity after its immobilization in calcium alginate is probably caused by strong electrostatic interactions between positively charged amino acid residues of the enzyme and negatively charged groups of alginate. High activity of immobilized protocatechuate 3,4-dioxygenase towards 2,3-dihydroxybenzoate, 2,5-dihydroxybenzoate, and 3,5-dihydroxybenzoate can be connected with modification of its catalytic mechanism as only 2,3-dihydroxybenzoate is in configuration typical for protocatechuate 3,4-dioxygenase's substrate
additional information
-
enzyme immobilized on calcium alginate gel binds to the carrier by electrostatic interaction while glyoxyl agarose is linked with the enzyme by covalent bonds. Since positively charged amino acids are localized at the entrance of crevasse, the electrostatic interaction plays the key role in modulation of enzyme activity. Significant increase of enzyme activity after its immobilization in calcium alginate is probably caused by strong electrostatic interactions between positively charged amino acid residues of the enzyme and negatively charged groups of alginate. High activity of immobilized protocatechuate 3,4-dioxygenase towards 2,3-dihydroxybenzoate, 2,5-dihydroxybenzoate, and 3,5-dihydroxybenzoate can be connected with modification of its catalytic mechanism as only 2,3-dihydroxybenzoate is in configuration typical for protocatechuate 3,4-dioxygenase's substrate
-
Show AA Sequence and Transmembrane Helices (3369 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21900
-
x * 21900 + x * 26700, deduced from nucleotide sequences of putative alpha and beta subunits
22280
-
alpha,beta, 2 * 22280 + 2 * 26630, holoenzyme probably contains 6 alpha2,beta2 tetramers, amino acid sequence
23000
26500
26630
-
alpha,beta, 2 * 22280 + 2 * 26630, holoenzyme probably contains 6 alpha2,beta2 tetramers, amino acid sequence
26700
-
x * 21900 + x * 26700, deduced from nucleotide sequences of putative alpha and beta subunits
29000
34300
-
trimer of dimers, (alphabeta)3, 3 * 29000, alpha subunit, + 3 * 34300, beta-subunit, SDS-PAGE
150000
480000
29000
-
trimer of dimers, (alphabeta)3, 3 * 29000, alpha subunit, + 3 * 34300, beta-subunit, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
heterodimer
hexamer
octamer
tetramer
-
alpha,beta, 2 * 22280 + 2 * 26630, holoenzyme probably contains 6 alpha2,beta2 tetramers, amino acid sequence
additional information
?
-
x * 21900 + x * 26700, deduced from nucleotide sequences of putative alpha and beta subunits
decamer