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Information on EC 4.1.1.68 - 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase and Organism(s) Escherichia coli and UniProt Accession P37352

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.68 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
IUBMB Comments
Requires Mg2+ [2,3]. Part of the 4-hydroxyphenylacetate degradation pathway in Escherichia coli.
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This record set is specific for:
Escherichia coli
UNIPROT: P37352
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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Synonyms
5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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isomerization
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decarboxylation
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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.
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
SUBSTRATE
PRODUCT                       
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
2-Oxohept-3-enedioate + CO2
show the reaction diagram
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-
?
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 SUBSTRATE
NATURAL PRODUCT
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
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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enzyme is part of the 4-hydroxyphenylacetate meta-cleavage pathway
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HPCE_ECOLX
427
0
46878
Swiss-Prot
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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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
crystallization experiments
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Garrido-Pertierra, A.; Cooper, R.A.
Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli
Eur. J. Biochem.
117
581-584
1981
Escherichia coli
Manually annotated by BRENDA team
Roper, D.I.; Cooper, R.A.
Purification, nucleotide sequence and some properties of a bifunctional isomerase/decarboxylase from the homoprotocatechuate degradative pathway of Escherichia coli C
Eur. J. Biochem.
217
575-580
1993
Escherichia coli, Escherichia coli C
Manually annotated by BRENDA team
Jervis, T.J.; Roper, D.I.; Glover, I.D.
Crystallization and preliminary X-ray analysis of a bifunctional enzyme: HHDD isomerase/OPET decarboxylase from Escherichia coli
Acta Crystallogr. Sect. D
52
1036-1038
1996
Escherichia coli
Manually annotated by BRENDA team
Tame, J.R.; Namba, K.; Dodson, E.J.; Roper, D.I.
The crystal structure of HpcE, a bifunctional decarboxylase/isomerase with a multifunctional fold
Biochemistry
41
2982-2989
2002
Escherichia coli (P37352)
Manually annotated by BRENDA team