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

for references in articles please use BRENDA:EC4.1.1.68
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The expected taxonomic range for this enzyme is: Escherichia coli

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EC NUMBER
COMMENTARY hide
4.1.1.68
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RECOMMENDED NAME
GeneOntology No.
5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2Z,4Z)-2-hydroxyhepta-2,4-dienedioate = (4Z)-2-oxohept-4-enedioate
show the reaction diagram
(1b)
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(3E,5R)-5-carboxy-2-oxohept-3-enedioate = (2Z,4Z)-2-hydroxyhepta-2,4-dienedioate + CO2
show the reaction diagram
(1a)
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(3E,5R)-5-carboxy-2-oxohept-3-enedioate = (4Z)-2-oxohept-4-enedioate + CO2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
isomerization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-hydroxyphenylacetate degradation
Tyrosine metabolism
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
5-oxopent-3-ene-1,2,5-tricarboxylate carboxy-lyase (2-oxohept-3-enedioate-forming)
Requires Mg2+ [2,3]. Part of the 4-hydroxyphenylacetate degradation pathway in Escherichia coli.
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CAS REGISTRY NUMBER
COMMENTARY hide
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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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enzyme is part of the 4-hydroxyphenylacetate meta-cleavage pathway
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
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
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032
5-oxopent-3-ene-1,2,5-tricarboxylate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
P37352
Escherichia coli;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
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gel filtration
42100
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sedimentation equilibrium centrifugation
44514
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1 * 44514, calculation from nucleotide sequence
50000
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1 * 50000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
crystallization experiments
monomer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for at least 2 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by ammonium sulfate precipitation and gel filtration, additional purification is achieved using DEAE-Sephacel chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Show AA Sequence (574 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 4.1.1.68)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)