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Information on EC 1.2.1.61 - 4-hydroxymuconic-semialdehyde dehydrogenase
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1.2.1.61 4-hydroxymuconic-semialdehyde dehydrogenaseIUBMB Comments
Involved in the 4-nitrophenol degradation pathway.
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The enzyme appears in viruses and cellular organisms
Synonyms
4-hydroxymuconic semialdehyde dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-HS dehydrogenase
4-hydroxymuconic semialdehyde dehydrogenase
hAPE
HqdC
PdcG
4-hydroxymuconic semialdehyde dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-hydroxymuconic semialdehyde + NAD+ + H2O = maleylacetate + NADH + H+
-
-
-
-
4-hydroxymuconic semialdehyde + NAD+ + H2O = maleylacetate + NADH + H+
catalytic mechanism involving residues Glu247 and Cys281
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
,
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxymuconic-semialdehyde:NAD+ oxidoreductase
Involved in the 4-nitrophenol degradation pathway.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH
-
conversion of hydroquinone to beta-ketoadipic acid via 4-hydroxymuconic semialdehyde and maleyl acetic acid
-
?
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
-
-
-
-
?
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
-
-
-
-
?
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
-
-
-
?
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
-
-
-
?
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
-
-
-
?
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + H+
-
-
-
-
?
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + H+
-
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH
-
conversion of hydroquinone to beta-ketoadipic acid via 4-hydroxymuconic semialdehyde and maleyl acetic acid
-
?
4-hydroxymuconic semialdehyde + NAD+ + H2O
maleylacetate + NADH + 2 H+
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
metabolism
-
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
-
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). G8Q9Q7_PSEO1
Pseudomonas ogarae (strain DSM 112162 / CECT 30235 / F113)
487
0
52021
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
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
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
-
18% activity after 30 min at pH 3.0, and 75% activity after 30 min at pH 10.0
719179
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
purified enzyme retains 65% activity after 20 min at 60°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pnpE, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
HapE shows 45% sequence identity with CymC, a p-cumic aldehyde dehydrogenase, from Pseudomonas putida
additional information
-
HapE shows 45% sequence identity with CymC, a p-cumic aldehyde dehydrogenase, from Pseudomonas putida
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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
brenda
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)
brenda
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)
brenda
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