Information on EC 1.2.1.61 - 4-hydroxymuconic-semialdehyde dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.61
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RECOMMENDED NAME
GeneOntology No.
4-hydroxymuconic-semialdehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-hydroxymuconic semialdehyde + NAD+ + H2O = maleylacetate + NADH + 2 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-hydroxyacetophenone degradation
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4-nitrophenol degradation I
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Chlorocyclohexane and chlorobenzene degradation
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxymuconic-semialdehyde:NAD+ oxidoreductase
Involved in the 4-nitrophenol degradation pathway.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
isolated from methyl parathion polluted activated sludge
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Manually annotated by BRENDA team
isolated from methyl parathion polluted activated sludge
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
the pnpE-encoded enzyme gamma-hydroxymuconic semialdehyde dehydrogenase catalyzes the reduction of 4-hydroxymuconic semialdehyde to maleylacetate in Pseudomonas sp. strain WBC-3, playing a key role in the catabolism of toxic para-nitrophenol to Krebs cycle intermediates
additional information
highly conserved residues C281 and E247 are identified to be critical for its catalytic activity, and flexible docking studies of the enzyme-substrate system predict the interactions between PnpE and its substrate 4-hydroxymuconic semialdehyde, flexible docking of substrate to PnpE, molecular docking analysis, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH
show the reaction diagram
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conversion of hydroquinone to beta-ketoadipic acid via 4-hydroxymuconic semialdehyde and maleyl acetic acid
-
?
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
show the reaction diagram
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + H+
show the reaction diagram
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
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH
show the reaction diagram
-
conversion of hydroquinone to beta-ketoadipic acid via 4-hydroxymuconic semialdehyde and maleyl acetic acid
-
?
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
show the reaction diagram
C1I208
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
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5 mM chloride salt, 123.3% activity compared to untreated control
Cd2+
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5 mM sulfate salt, 58.9% activity compared to untreated control
Co2+
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5 mM chloride salt, 147.1% activity compared to untreated control
Cu2+
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5 mM chloride salt, 110.2% activity compared to untreated control
Fe2+
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5 mM chloride salt, 39.5% activity compared to untreated control
Fe3+
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5 mM chloride salt, 187.4% activity compared to untreated control
K+
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5 mM chloride salt, 95.7% activity compared to untreated control
Mg2+
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5 mM chloride salt, 138.1% activity compared to untreated control
Mn2+
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5 mM chloride salt, 186.1% activity compared to untreated control
Na+
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5 mM chloride salt, 88.2% activity compared to untreated control
Ni2+
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5 mM chloride salt, 183.9% activity compared to untreated control
Zn2+
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5 mM chloride salt, 145.9% activity compared to untreated control
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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5 mM, 83.2% activity compared to untreated control
SDS
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5 mM, 81.6% activity compared to untreated control
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0006
uninduced cells, pH 7.0, temperature not specified in the publication
0.0025
hydroquinone-induced cells, pH 7.0, temperature not specified in the publication
0.0031
nonylphenol-induced cells, pH 7.0, temperature not specified in the publication
0.44
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purified recombinant His6-PdcG enzyme, pH 8.0 at 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
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recombinant His6-PdcG by SDS-PAGE
53500
calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the monomer of PnpE has the typical structural organization betaalphabeta of the ALDH family, with 17 beta-strands and 14 alpha-helices, the secondary structures belong to three domains: a substrate binding domain, a cofactor binding domain, and an oligomerization domain mediating protein dimerization. The substrate binding domain consists of a central six-stranded beta-sheet and six alpha-helices, while the cofactor binding domain contains a nine-stranded beta-sheet and seven alpha-helices, structure, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme PnpE in apo-form or in complex with NAD+, sitting drop vapor diffusion technique, 10 mg/ml apo-enzyme from 20% w/v PEG 3350, and 0.2 M KNO3 at 20°C, 10 mg/ml NAD+-complexed enzyme from 0.1 M bicine, pH 8.5, 20% PEG 10000, and 1 mM NAD+, X-ray diffraction structure determination and analysis at 2.7-3.1 A resolution, molecular replacement method using bovine mitochondrial aldehyde dehydrogenase, PDB ID 1A4Z, as the search model
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 10
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18% activity after 30 min at pH 3.0, and 75% activity after 30 min at pH 10.0
719179
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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purified enzyme retains 65% activity after 20 min at 60°C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His6-PdcG by Ni2+-NTA affinity chromatography
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, followed by gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene pnpE, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
HqdC expression in Escherichia coli BL21-DE3 cells
PdcG with His6 tag inserted into expression vectors pET30a and expressed in Escherichia coli BL21 (DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
by 0.5 mM hydroquinone and by 0.5 mM nonylphenol
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C281A
site-directed mutagenesis
E247K
site-directed mutagenesis
F150A
site-directed mutagenesis
F154A
site-directed mutagenesis
F447A
site-directed mutagenesis
H275E
site-directed mutagenesis
I282D
site-directed mutagenesis
N149A
site-directed mutagenesis
W157A
site-directed mutagenesis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information