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Information on EC 3.1.1.24 - 3-oxoadipate enol-lactonase and Organism(s) Paraburkholderia xenovorans and UniProt Accession Q13KT2

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.24 3-oxoadipate enol-lactonase
IUBMB Comments
The enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase.
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This record set is specific for:
Paraburkholderia xenovorans
UNIPROT: Q13KT2
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Word Map
The taxonomic range for the selected organisms is: Paraburkholderia xenovorans
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
enol-lactone hydrolase, beta-ketoadipate enol-lactone hydrolase, 3-oxoadipate enol-lactone hydrolase, elh i, elh ii, 3-oxoadipate enol-lactonase, 3-oxoadipate-enol-lactonase, 4-methyl-3-oxoadipate enol-lactone hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-oxoadipate-enol-lactonase
-
enol-lactone hydrolase
-
carboxymethylbutenolide lactonase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
4-carboxymethylbut-3-en-4-olide enol-lactonohydrolase
The enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-04-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-oxoadipate enol-lactone + H2O
3-oxoadipate
show the reaction diagram
-
-
-
?
3-oxoadipate-enol-lactone + H2O
3-oxoadipate
show the reaction diagram
also known as beta-ketoadipate-enol-lactone
-
-
?
4-hydroxy-3-pentenoic acid gamma-lactone + H2O
4-oxopentanoic acid
show the reaction diagram
-
i.e. levulinic acid
-
?
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
3-oxoadipate enol-lactone + H2O
3-oxoadipate
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57600
calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with levulinic acid
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity column chromatography and Superdex75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bains, J.; Kaufman, L.; Farnell, B.; Boulanger, M.J.
A product analog bound form of 3-oxoadipate-enol-lactonase (PcaD) reveals a multifunctional role for the divergent cap domain
J. Mol. Biol.
406
649-658
2011
Paraburkholderia xenovorans (Q13KT2)
Manually annotated by BRENDA team
Knapik, A.A.; Petkowski, J.J.; Otwinowski, Z.; Cymborowski, M.T.; Cooper, D.R.; Majorek, K.A.; Chruszcz, M.; Krajewska, W.M.; Minor, W.
A multi-faceted analysis of RutD reveals a novel family of alpha/beta hydrolases
Proteins
80
2359-2368
2012
Paraburkholderia xenovorans (Q13KT2)
Manually annotated by BRENDA team