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The enzyme appears in viruses and cellular organisms
Synonyms 4-hydroxymuconic semialdehyde dehydrogenase, more
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4-hydroxymuconic semialdehyde dehydrogenase
gamma-hydroxymuconic semialdehyde dehydrogenase
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NAD dependent gamma-hydroxymuconic semialdehyde dehydrogenase
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4-HS dehydrogenase
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4-hydroxymuconic semialdehyde dehydrogenase
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4-hydroxymuconic semialdehyde dehydrogenase
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4-hydroxymuconic semialdehyde dehydrogenase
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4-hydroxymuconic semialdehyde dehydrogenase
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4-hydroxymuconic semialdehyde dehydrogenase
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4-hydroxymuconic semialdehyde dehydrogenase
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4-hydroxymuconic semialdehyde dehydrogenase
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hAPE
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HqdC
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PdcG
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4-hydroxymuconic semialdehyde + NAD+ + H2O = maleylacetate + NADH + H+
4-hydroxymuconic semialdehyde + NAD+ + H2O = maleylacetate + NADH + H+
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4-hydroxymuconic semialdehyde + NAD+ + H2O = maleylacetate + NADH + H+
catalytic mechanism involving residues Glu247 and Cys281
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MetaCyc
4-hydroxyacetophenone degradation, 4-nitrophenol degradation I
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4-hydroxymuconic-semialdehyde:NAD+ oxidoreductase
Involved in the 4-nitrophenol degradation pathway.
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4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH
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Substrates: conversion of hydroquinone to beta-ketoadipic acid via 4-hydroxymuconic semialdehyde and maleyl acetic acid Products: -
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4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + H+
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
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Substrates: - Products: -
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4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
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Substrates: - Products: -
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4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
Substrates: - Products: -
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4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
Substrates: - Products: -
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4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
Substrates: - Products: -
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4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + H+
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Substrates: - Products: -
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4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + H+
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Substrates: - Products: -
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4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH
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Substrates: conversion of hydroquinone to beta-ketoadipic acid via 4-hydroxymuconic semialdehyde and maleyl acetic acid Products: -
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4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
Substrates: - Products: -
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NAD+
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NAD+
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can not be replaced by NADP+, NADH or NADPH
NAD+
NAD+ is situated in a cleft of PnpE. The cofactor binding site is composed of two pockets. The adenosine and the first ribose group of NAD bind in one pocket and the nicotinamide ring in the other. Six amino acids, C281, E247, Q210, W148, I146 and K172, interact with the cofactor
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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
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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
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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
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8
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isolated from methyl parathion polluted activated sludge
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isolated from methyl parathion polluted activated sludge
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UniProt
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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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
metabolism
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enzyme is part of the degradation pathway of 4-nitrophenol which is a priority environmental pollutant
metabolism
HqdC gene is part of a gene cluster associated with hydroquinone degradation into 3-oxoadipate
metabolism
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enzyme is part of the degradation pathway of 4-nitrophenol which is a priority environmental pollutant
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metabolism
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HqdC gene is part of a gene cluster associated with hydroquinone degradation into 3-oxoadipate
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F8TW85_9SPHN
498
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53482
TrEMBL
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G8Q9Q7_PSEO1
Pseudomonas ogarae (strain DSM 112162 / CECT 30235 / F113)
487
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52021
TrEMBL
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Q8KLV3_PSEST
87
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9337
TrEMBL
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B1GRL7_PSEFL
487
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52400
TrEMBL
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C1I208_PSEWB
Pseudomonas sp. (strain WBC-3)
487
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52339
TrEMBL
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52000
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recombinant His6-PdcG by SDS-PAGE
53500
calculated from sequence
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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
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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
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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
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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
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additional information
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purified enzyme retains 65% activity after 20 min at 60°C
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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
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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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by 0.5 mM hydroquinone and by 0.5 mM nonylphenol
by 0.5 mM hydroquinone and by 0.5 mM nonylphenol
by 0.5 mM hydroquinone and by 0.5 mM nonylphenol
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additional information
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HapE shows 45% sequence identity with CymC, a p-cumic aldehyde dehydrogenase, from Pseudomonas putida
additional information
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HapE shows 45% sequence identity with CymC, a p-cumic aldehyde dehydrogenase, from Pseudomonas putida
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Spain, J.C.; Gibson, D.T.
Pathway for biodegradation of p-nitrophenol in a Moraxella sp.
Appl. Environ. Microbiol.
57
812-819
1991
Moraxella sp.
brenda
Moonen, M.J.; Kamerbeek, N.M.; Westphal, A.H.; Boeren, S.A.; Janssen, D.B.; Fraaije, M.W.; van Berkel, W.J.
Elucidation of the 4-hydroxyacetophenone catabolic pathway in Pseudomonas fluorescens ACB
J. Bacteriol.
190
5190-5198
2008
Pseudomonas fluorescens, Pseudomonas fluorescens ACB
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Zhang, S.; Sun, W.; Xu, L.; Zheng, X.; Chu, X.; Tian, J.; Wu, N.; Fan, Y.
Identification of the para-nitrophenol catabolic pathway, and characterization of three enzymes involved in the hydroquinone pathway, in Pseudomonas sp. 1-7
BMC Microbiol.
12
27
2012
Pseudomonas sp., Pseudomonas sp. 1-7
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Kolvenbach, B.A.; Dobrowinski, H.; Fousek, J.; Vlcek, C.; Schaeffer, A.; Gabriel, F.L.; Kohler, H.P.; Corvini, P.F.
An unexpected gene cluster for downstream degradation of alkylphenols in Sphingomonas sp. strain TTNP3
Appl. Microbiol. Biotechnol.
93
1315-1324
2012
Sphingomonas sp. (F8TW85), Sphingomonas sp., Sphingomonas sp. TTNP3 (F8TW85)
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Su, J.; Zhang, C.; Zhang, J.J.; Wei, T.; Zhu, D.; Zhou, N.-Y.; Gu, Lc.
Crystal structure of the gamma-hydroxymuconic semialdehyde dehydrogenase from Pseudomonas sp. strain WBC-3, a key enzyme involved in para-Nitrophenol degradation
BMC Struct. Biol.
13
30
2013
Pseudomonas sp. WBC-3 (C1I208)
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