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Information on EC 4.2.1.80 - 2-oxopent-4-enoate hydratase and Organism(s) Escherichia coli and UniProt Accession P77608

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.80 2-oxopent-4-enoate hydratase
IUBMB Comments
The enzyme is involved in the catechol meta-cleavage pathway, a major mechanism for degradation of aromatic compounds. Also acts, more slowly, on cis-2-oxohex-4-enoate, but not on the trans-isomer. The enzyme was named when it was thought that the substrate is 2-oxopent-4-enoate. However, it was later found that the actual substrate is its tautomer (2Z)-2-hydroxypenta-2,4-dienoate. In some organisms the enzyme forms a complex with EC 4.1.1.77, 2-oxo-3-hexenedioate decarboxylase (previously named 4-oxalocrotonate decarboxylase).
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Escherichia coli
UNIPROT: P77608
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
2-oxopent-4-enoate hydratase, 2-hydroxypenta-2,4-dienoate hydratase, vinylpyruvate hydratase, 2-hydroxypentadienoic acid hydratase, 2-keto-4-pentenoate hydratase, 2-hydroxypent-2,4-dienoate hydratase, hpd hydratase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-hydroxypent-2,4-dienoate hydratase
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-
-
-
2-hydroxypentadienoic acid hydratase
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-
2-keto-4-pentenoate hydratase
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-
-
-
2-keto-4-pentenoate(vinylpyruvate)hydratase
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-
-
-
2-keto-4-pentenoic acid hydratase
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-
-
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OEH 2-keto-4-pentenoate hydratase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
4-hydroxy-2-oxopentanoate hydro-lyase (2-oxopent-4-enoate-forming)
The enzyme is involved in the catechol meta-cleavage pathway, a major mechanism for degradation of aromatic compounds. Also acts, more slowly, on cis-2-oxohex-4-enoate, but not on the trans-isomer. The enzyme was named when it was thought that the substrate is 2-oxopent-4-enoate. However, it was later found that the actual substrate is its tautomer (2Z)-2-hydroxypenta-2,4-dienoate. In some organisms the enzyme forms a complex with EC 4.1.1.77, 2-oxo-3-hexenedioate decarboxylase (previously named 4-oxalocrotonate decarboxylase).
CAS REGISTRY NUMBER
COMMENTARY hide
227181-25-1
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229017-66-7
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64427-80-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxypentadienoic acid
?
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
reqirement of divalent cations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sodium oxalate
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.041
2-hydroxypentadienoic acid
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pH 6
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0049
sodium oxalate
-
pH 6
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
538
-
MonoQ pool
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
gel filtration
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pollard, J.R.; Bugg, T.D.H.
Purification, characterization and reaction mechanism of monofunctional 2-hydroxypentadienoic acid hydratase from Escherichia coli
Eur. J. Biochem.
251
98-106
1998
Escherichia coli
Manually annotated by BRENDA team