Information on EC 3.1.1.57 - 2-pyrone-4,6-dicarboxylate lactonase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.1.57
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RECOMMENDED NAME
GeneOntology No.
2-pyrone-4,6-dicarboxylate lactonase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-oxo-2H-pyran-4,6-dicarboxylate + H2O = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
show the reaction diagram
the product isomerizes to 4-oxalmesaconate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
gallate degradation II
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methylgallate degradation
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protocatechuate degradation I (meta-cleavage pathway)
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syringate degradation
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gallate degradation
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Benzoate degradation
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Aminobenzoate degradation
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
2-pyrone-4,6-dicarboxylate lactonohydrolase
The product is most likely the keto-form of 4-oxalomesaconate (as shown in the reaction) [1,2]. It can be converted to the enol-form, 4-hydroxybuta-1,3-diene-1,2,4-trioate, either spontaneously or by EC 5.3.2.8, 4-oxalomesaconate tautomerase [3].
CAS REGISTRY NUMBER
COMMENTARY hide
84177-55-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene pmdD
UniProt
Manually annotated by BRENDA team
gene pmdD
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-pyrone-4,6-dicarboxylate + H2O
4-carboxy-2-hydroxyhexa-2,4-dienedioate
show the reaction diagram
2-pyrone-4,6-dicarboxylate + H2O
4-oxalomesaconate
show the reaction diagram
2-pyrone-4,6-dicarboxylate + H2O
?
show the reaction diagram
additional information
?
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no hydrolysis of gamma-butyrolactone, gamma-valerolactone, epsilon-caprolactone, gamma-n-decalactone, D-glucorono-gamma-lactone, mevalonolactone, 2-pyrone-6-carboxylate, coumalic acid, isodehydracetic acid, 4-hydroxy-6-methyl-2-pyrone and 4-methoxy-6-methyl-2-H-pyran-2-one
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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
2-pyrone-4,6-dicarboxylate + H2O
4-carboxy-2-hydroxyhexa-2,4-dienedioate
show the reaction diagram
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highly specific, various other lactones does not serve as substrates
product isomerizes to 4-oxalmesaconate
r
2-pyrone-4,6-dicarboxylate + H2O
4-oxalomesaconate
show the reaction diagram
2-pyrone-4,6-dicarboxylate + H2O
?
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-hydroxyisophthalic acid
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Co(NO3)2
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inhibits hydrolysis reaction by 59.9%
Cu(NO3)2
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inhibits synthesis reaction
Mn(NO3)2
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inhibits hydrolysis reaction by 62.1%
N-ethylmaleimide
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p-chloromercuribenzoate
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pyridine-2,4-dicarboxylic acid
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Zn(NO3)2
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inhibits hydrolysis reaction
additional information
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monoiodoacetate had essentially no effect, Mg(NO3)2, Ni(NO3)2, Ca(NO3)2, Cr(NO3)3 and Fe(NO3)3 shows essentially no effect, KCN and various metal chelating reagents including EDTA, tiron, 1,10-phenanthroline, 2,2'-bipyridine, diethyldithiocarbonate and 8-hydroxyquinoline shows no significant effect
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.041 - 0.72
2-Pyrone-4,6-dicarboxylate
0.026
4-oxalmesaconate
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pH 6.5, 24°C
0.025
4-oxalomesaconate
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pH 6.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0013 - 342
2-Pyrone-4,6-dicarboxylate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016 - 7100
2-Pyrone-4,6-dicarboxylate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
5-hydroxyisophthalic acid
pH 8.25, 30°C
0.075
pyridine-2,4-dicarboxylic acid
pH 8.25, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49.6
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recombinant protein from Escherichia coli, 25°C
247
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purification of hydrolase activity
495
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purified recombinant protein from Escherichia coli, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
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2-pyrone-4,6-dicarboxylate synthesis
6.5
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reverse reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.49
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isolelectric focusing at 6°C, LKB 8101 column pH 3.5-10.0
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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gel filtration
31000
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gel filtration
33000
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1 * 33000, SDS-PAGE
34345
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1 * 34345, calculated from the deduced amino acid sequence, native mass by gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
aged enzyme preparation is fully reactivated by preincubation at 24°C for 10 min with an excess amount of dithiothreitol, cysteine or GSH
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 30% of the activity is lost on storage for 1 year
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-20°C, purified enzyme can be stored for at least 2 months without appreciable loss in activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+), gel filtration
recombinant protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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gene pmdD, DNA and amino acid sequence determination and analysis, the pmdUKEFDABC genes constitute an operon, the transcription start site of the pmd operon is mapped at 167 nucleotides upstream of the initiation codon of pmdU. Quantitative real-time RT-PCR expression analysis
His-tagged version expressed in Escherichia coli BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
pmd promoter activity is enhanced 20fold when the cells grow in presence of protocatechuate. Inducers of the pmd operon are protocatechuic acid and 2-pyrone-4,6-dicarboxylate, but 2-pyrone-4,6-dicarboxylate is the more effective inducer
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D248A
prototypical metal-coordinating residue in the amidohydrolase superfamily
D248N
prototypical metal-coordinating residue in the amidohydrolase superfamily
H180A
prototypical metal-coordinating residue in the amidohydrolase superfamily
H180C
prototypical metal-coordinating residue in the amidohydrolase superfamily
H31N
prototypical metal-coordinating residue in the amidohydrolase superfamily
H33N
prototypical metal-coordinating residue in the amidohydrolase superfamily
R124M
active site residue
R130M
active site residue
R183M
active site residue
R217M
active site residue
Y156F
active site residue
Y49F
active site residue
additional information