Information on EC 4.1.1.68 - 5-Oxopent-3-ene-1,2,5-tricarboxylate decarboxylase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY
4.1.1.68
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RECOMMENDED NAME
GeneOntology No.
5-Oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
5-oxopent-3-ene-1,2,5-tricarboxylate = 2-oxohept-3-enedioate + CO2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
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-
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decarboxylation
P37352
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isomerization
P37352
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PATHWAY
KEGG Link
MetaCyc Link
4-hydroxyphenylacetate degradation
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Microbial metabolism in diverse environments
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Tyrosine metabolism
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SYSTEMATIC NAME
IUBMB Comments
5-oxopent-3-ene-1,2,5-tricarboxylate carboxy-lyase (2-oxohept-3-enedioate-forming)
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-Hydroxyhepta-2,4-diene-1,7-dioate isomerase/5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
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5-Oxopenta-3-ene-1,2,5-tricarboxylate decarboxylase
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Decarboxylase, 5-oxopenta-3-ene-1,2,5-tricarboxylate
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HHDD isomerase/OPET decarboxylase
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OPET decarboxylase
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CAS REGISTRY NUMBER
COMMENTARY
148619-60-7
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151404-80-7
bifunctional enzyme ec4.1.1.68/ec5.3.3.10: isomerase, 2-hydroxyhepta-2,4-diene-1,7-dioate (Escherichia coli clone pFR835 gene hpcE reduced) / 2-hydroxyhepta-2,4-diene-1,7-dioate isomerase/5-oxopent-2-ene-1,2,5-tricarboxylate decarboxylase (Escherichia coli C clone pDR835 gene hpcE) /decarboxylase, 5-oxopenta-3-ene-1,2,5-tricarboxylate (Escherichia coli clone pDR835 gene hpcE reduced)
173015-33-3
bifunctional enzyme ec4.1.1.68/ec5.3.3.10: isomerase, 2-hydroxyhepta-2,4-diene-1,7-dioate (Escherichia coli clone pHCB3 gene hpaG) /decarboxylase, 5-oxopenta-3-ene-1,2,5-tricarboxylate (Escherichia coli clone pHCB3 gene hpaG) /GenBank Z37980-derived protein
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
bifunctional enzyme with activity of EC 5.3.3.10 and EC 4.1.1.68
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Manually annotated by BRENDA team
bifunctional enzyme with activity of EC 5.3.3.10 and EC 4.1.1.68; strain C
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Manually annotated by BRENDA team
strain C
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
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enzyme is part of the 4-hydroxyphenylacetate meta-cleavage pathway
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-carboxy-2-oxohept-3-enedioate + H+
2-hydroxyhepta-2,4-dienedioate + CO2
show the reaction diagram
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enzyme is part of the 4-hydroxyphenylacetate meta-cleavage pathway
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?
5-Oxopent-3-ene-1,2,5-tricarboxylate
2-Oxohept-3-enedioate + CO2
show the reaction diagram
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-
-
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5-Oxopent-3-ene-1,2,5-tricarboxylate
2-Oxohept-3-enedioate + CO2
show the reaction diagram
-
-
-
-
5-Oxopent-3-ene-1,2,5-tricarboxylate
2-Oxohept-3-enedioate + CO2
show the reaction diagram
P37352
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-
?
5-Oxopent-3-ene-1,2,5-tricarboxylate
2-Oxohept-3-enedioate + CO2
show the reaction diagram
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-
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5-Oxopent-3-ene-1,2,5-tricarboxylate
?
show the reaction diagram
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enzyme is involved in the homoprotocatechuate degradative pathway
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-Oxopent-3-ene-1,2,5-tricarboxylate
?
show the reaction diagram
-
enzyme is involved in the homoprotocatechuate degradative pathway
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METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.032
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5-oxopent-3-ene-1,2,5-tricarboxylate
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SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
27000
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gel filtration
42100
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sedimentation equilibrium centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
P37352
crystallization experiments
monomer
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1 * 44514, calculation from nucleotide sequence; 1 * 50000, SDS-PAGE
monomer
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1 * 44514, calculation from nucleotide sequence; 1 * 50000, SDS-PAGE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method
P37352
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4°C, stable for at least 2 months
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by ammonium sulfate precipitation and gel filtration, additional purification is achieved using DEAE-Sephacel chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE