Information on EC 1.13.11.8 - protocatechuate 4,5-dioxygenase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
1.13.11.8
-
RECOMMENDED NAME
GeneOntology No.
protocatechuate 4,5-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protocatechuate + O2 = 4-carboxy-2-hydroxymuconate semialdehyde
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
extradiol cleavage
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
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reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3,4-dichlorobenzoate degradation
-
-
3-chlorobenzoate degradation II (via protocatechuate)
-
-
Aminobenzoate degradation
-
-
Benzoate degradation
-
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Microbial metabolism in diverse environments
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-
Polycyclic aromatic hydrocarbon degradation
-
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protocatechuate degradation I (meta-cleavage pathway)
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-
SYSTEMATIC NAME
IUBMB Comments
protocatechuate:oxygen 4,5-oxidoreductase (decyclizing)
Requires Fe2+.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-56-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a phthalate-degrading bacterium, gene pmdB encodes for the beta-subunit of PCA 4,5-dioxygenase, and harboring of another PCA 4,5-dioxygenase gene, pmdAIIBII
-
-
Manually annotated by BRENDA team
a phthalate-degrading bacterium, gene pmdB encodes for the beta-subunit of PCA 4,5-dioxygenase, and harboring of another PCA 4,5-dioxygenase gene, pmdAIIBII
-
-
Manually annotated by BRENDA team
strain Pt-L5, ATCC 49249
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-
Manually annotated by BRENDA team
no activity in Stenotrophomonas maltophilia
-
-
-
Manually annotated by BRENDA team
no activity in Stenotrophomonas maltophilia KB2
-
-
-
Manually annotated by BRENDA team
biovar viceae, strain USDA 2370, grown on 4-hydroxybenzoate-containing medium
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenyl sulfonate + O2
2-hydroxy-6-oxo-4-sulfohexa-2,4-dienoate
show the reaction diagram
3-O-methylgallate + O2
4-carboxy-2-hydroxy-6-methoxy-6-oxohexa-2,4-dienoate + 2-pyrone-4,6-dicarboxylate
show the reaction diagram
5-methoxygallic acid + O2
?
show the reaction diagram
-
-
-
-
?
5-methylprotocatechuate + O2
4-carboxy-2-hydroxy-3-methylmuconate semialdehyde
show the reaction diagram
gallate + O2
?
show the reaction diagram
gallic acid + O2
2-pyrone-4,6-dicarboxylic acid + H2O
show the reaction diagram
-
-
major product formed
-
?
gallic acid + O2
?
show the reaction diagram
-
-
-
-
?
protocatechuate + O2
4-carboxy-2-hydroxymuconate semialdehyde
show the reaction diagram
sulfonylcatechol + O2
?
show the reaction diagram
additional information
?
-
-
no activity on 3-O-methylgallate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
gallic acid + O2
2-pyrone-4,6-dicarboxylic acid + H2O
show the reaction diagram
-
-
major product formed
-
?
protocatechuate + O2
4-carboxy-2-hydroxymuconate semialdehyde
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Amino-4-hydroxybenzoic acid
-
-
3-Chloro-4-hydroxybenzoic acid
-
-
3-Fluoro-4-hydroxybenzoic acid
-
-
3-Hydroxy-4-aminobenzoic acid
-
-
3-hydroxybenzoate
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-
3-Iodo-4-hydroxybenzoic acid
-
-
3-methoxy-4-hydroxybenzoic acid
-
-
3-Nitro-4-hydroxybenzoic acid
-
-
4-hydroxybenzoate
-
-
4-nitrocatechol
-
competitive inhibitor
iodoacetamide
-
competitive inhibitor
p-chloromercuribenzoic acid
-
excellent competitive inhibitor
Protocatechualdehyde
-
competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.125
5-methoxygallic acid
-
-
0.0735
gallic acid
-
-
0.02 - 0.08
protocatechuate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
350
protocatechuate
Comamonas testosteroni
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.3
3-hydroxybenzoate
-
-
1
4-hydroxybenzoate
-
-
0.56
4-nitrocatechol
-
-
0.96
Protocatechualdehyde
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
purified enzyme, pH 7.0, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
assay at
9.5 - 9.8
-
CAPS
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 35
-
approx. 85% of maximal activity at 5°C, approx. 20% of maximal activity at 35°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
-
gel filtration
120000
-
gel filtration
142000
-
gel filtration
180000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 17000, + 1 * 34000, SDS-PAGE
homodimer
-
2 * 62000, SDS-PAGE
octamer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
under strictly anaerobic conditions
-
under aerobic conditions
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis can be performed only at temperatures at or below 4°C
-
rapid loss of activity during purification due to the oxidation of an active-site ferrous iron group
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
rapidly inactivated by oxidizing agents such as H2O2 or ferricyanide, partial reactivation by ascorbate
-
439357
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196°C, in liquid nitrogen, without significant loss of activity for several years
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, Q-Sepharose
-
heat treatment, DEAE-Sepharose, superdex 200, Resource Q
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
gene organization of the PCA45 pathway genes in strain E6, overview. Identification of the pmd promoter region, the transcription start site of the pmd operon is a thymine 167 nt upstream of the pmdU start codon, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced by protocatechuate
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