Information on EC 4.2.1.80 - 2-oxopent-4-enoate hydratase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.1.80
-
RECOMMENDED NAME
GeneOntology No.
2-oxopent-4-enoate hydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-hydroxy-2-oxopentanoate = 2-oxopent-4-enoate + H2O
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-oxopentenoate degradation
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4-chloronitrobenzene degradation
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Benzoate degradation
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Dioxin degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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Phenylalanine metabolism
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Xylene degradation
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3-phenylpropionate degradation
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gallate degradation
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phenol degradation
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxy-2-oxopentanoate hydro-lyase (2-oxopent-4-enoate-forming)
Also acts, more slowly, on cis-2-oxohex-4-enoate, but not on the trans-isomer.
CAS REGISTRY NUMBER
COMMENTARY hide
227181-25-1
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229017-66-7
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64427-80-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 10d
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Manually annotated by BRENDA team
strain 10d
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
strain F199, gene plasmid pNL1-encoded
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Manually annotated by BRENDA team
strain F199, gene plasmid pNL1-encoded
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-
Manually annotated by BRENDA team
DJ-12
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Manually annotated by BRENDA team
strain DJ77, phnH-gene encoded
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxyhexa-2,4-dienoate + H2O
2-keto-4-hydroxyhexanoate
show the reaction diagram
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-
-
-
?
2-hydroxypent-2,4-dienoate
2-keto-4-hydroxypentanoate
show the reaction diagram
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reaction in the catabolic pathway of numerous aromatic compounds, including polychlorinated biphenyls
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-
?
2-hydroxypent-2,4-dienoate + H2O
2-keto-4-hydroxypentanoate
show the reaction diagram
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-
-
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?
2-hydroxypentadienoic acid
?
show the reaction diagram
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-
-
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?
2-keto-cis-4-hexenoic acid
?
show the reaction diagram
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50% the rate of 4-hydroxy-2-oxopentanoate, higher activity towards cis than towards trans-isomer
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-
?
4-hydroxy-2-oxopentanoate
2-oxopent-4-enoate + H2O
show the reaction diagram
5-chloro-2-hydroxypent-2,4-dienoate
5-chloro-2-keto-4-hydroxypentanoate
show the reaction diagram
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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-hydroxypent-2,4-dienoate
2-keto-4-hydroxypentanoate
show the reaction diagram
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reaction in the catabolic pathway of numerous aromatic compounds, including polychlorinated biphenyls
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
Co2+
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divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
Zn2+
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divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sodium oxalate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0408
2-hydroxyhexa-2,4-dienoate
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activated by Mg2+
0.0317 - 0.0386
2-hydroxypent-2,4-dienoate
0.041
2-hydroxypentadienoic acid
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pH 6
0.03
4-hydroxy-2-oxopentanoate
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pH 7, native enzyme
0.0459
5-chloro-2-hydroxypent-2,4-dienoate
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activated by Mg2+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
60.5
2-hydroxyhexa-2,4-dienoate
Paraburkholderia xenovorans
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activated by Mg2+
215 - 361
2-hydroxypent-2,4-dienoate
7.7
5-chloro-2-hydroxypent-2,4-dienoate
Paraburkholderia xenovorans
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activated by Mg2+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0049
sodium oxalate
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pH 6
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.33 - 0.54
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cell-free extracts from succinate-grown cells, strain-dependent
4
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recombinant enzyme
5.2
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cell-free extracts from DL-allylglycerine grown cells
45
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native enzyme
538
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MonoQ pool
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 7.5
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
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8 * 27000, SDS-PAGE
27400
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calculated from nucleotide sequence
28040
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calculated from nucleotide sequence
30000
5 * 35000, fusion protein, SDS-PAGE. 5 * 30000, purified protein, SDS-PAGE
35000
5 * 35000, fusion protein, SDS-PAGE. 5 * 30000, purified protein, SDS-PAGE
151000
gel filtration-multiangle laser light scattering
221000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
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8 * 27000, SDS-PAGE
pentamer
5 * 35000, fusion protein, SDS-PAGE. 5 * 30000, purified protein, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
MhpD with and without Mg2+, by hanging-drop vapour-diffusion method, to 2.8 A resolution. Space group of the crystals is H3 with unit cell parameters a = 207.35 A, b = 207.35 A, c = 545.47 A, alpha = 90°, beta = 90°, and gamma = 120°. Assembles to form a 20-nm-diameter particle comprising 60 protein subunits, arranged with 532 symmetry when crystallised at low pH in the presence of phosphate or sulphate ions. Particles form rapidly and are stable in solution during gel filtration at low pH. They are probably formed through trimers of pentamers, which are stabilised by the interaction of two phosphate ions with residues of the N-terminal domains of subunits at the 3fold axis. Once the particles are formed at high concentrations of phosphate (or sulphate), they remain stable in solution at 20fold lower concentrations of the anion. Guest molecules can be trapped within the hollow protein shell during assembly. The C-termini of the subunits are freely accessible on the surface of the protein cage
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by centrifugation and gel filtration
copurified with 4-oxalocrotonate decarboxylase
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ligated into a modified pET22b expression vector encoding a His6 tag and expressed in Escherichia coli BL21(DE3) cells
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