Information on EC 1.2.1.85 - 2-hydroxymuconate-6-semialdehyde dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.85
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RECOMMENDED NAME
GeneOntology No.
2-hydroxymuconate-6-semialdehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2,3-dihydroxybenzoate degradation
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4-amino-3-hydroxybenzoate degradation
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catechol degradation to 2-oxopent-4-enoate II
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protocatechuate degradation III (para-cleavage pathway)
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phenol degradation
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Benzoate degradation
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Xylene degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
2-hydroxymuconate-6-semialdehyde:NAD+ oxidoreductase
This substrate for this enzyme is formed by meta ring cleavage of catechol (EC 1.13.11.2, catechol 2,3-dioxygenase), and is an intermediate in the bacterial degradation of several aromatic compounds. Has lower activity with benzaldehyde [1]. Activity with NAD+ is more than 10-fold higher than with NADP+ [3]. cf. EC 1.2.1.32, aminomuconate-semialdehyde dehydrogenase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate + NAD+ + H2O
(2E,4Z)-2-hydroxy-5-methylhexa-2,4-diendioate + NADH + H+
show the reaction diagram
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?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
show the reaction diagram
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + H+
show the reaction diagram
3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH + H+
show the reaction diagram
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?
3-fluorobenzaldehyde + NAD+ + H2O
3-fluorobenzoate + NADH + H+
show the reaction diagram
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?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + H+
show the reaction diagram
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?
3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH + H+
show the reaction diagram
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?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
show the reaction diagram
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?
4-methylbenzaldehyde + NAD+ + H2O
4-methylbenzoate + NADH + H+
show the reaction diagram
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?
5-chloro-2-hydroxymuconic semialdehyde + NAD+ + H2O
5-chloro-2-hydroxymuconic acid + NADH + H+
show the reaction diagram
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
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113% activity compared to 2-hydroxymuconate-6-semialdehyde
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?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
butyraldehyde + NAD+ + H2O
butanoate + NADH + H+
show the reaction diagram
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138% activity compared to 2-hydroxymuconate-6-semialdehyde
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formaldehyde + NAD+ + H2O
formate + NADH + H+
show the reaction diagram
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16.5% activity compared to 2-hydroxymuconate-6-semialdehyde
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propionaldehyde + NAD+ + H2O
propanoate + NADH + H+
show the reaction diagram
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107% activity compared to 2-hydroxymuconate-6-semialdehyde
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?
additional information
?
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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-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
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complete inhibition at 1 mM
Hg2+
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complete inhibition at 1 mM
iodoacetic acid
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69% residual activity at 1 mM
N-ethylmaleimide
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18% residual activity at 1 mM
p-chloromercuribenzoate
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41% residual activity at 1 mM
Zn2+
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26% residual activity at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0093
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate
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in 100 mM Tris-HCl, pH 8.5, at 25°C
0.0013 - 0.017
2-hydroxymuconate-6-semialdehyde
1.3
3-Chlorobenzaldehyde
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in 100 mM glycine-NaOH (pH 9.2), at 25°C
0.17
3-Fluorobenzaldehyde
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in 100 mM glycine-NaOH (pH 9.2), at 25°C
0.94
3-Methoxybenzaldehyde
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in 100 mM glycine-NaOH (pH 9.2), at 25°C
0.63
3-methylbenzaldehyde
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in 100 mM glycine-NaOH (pH 9.2), at 25°C
0.81
3-Nitrobenzaldehyde
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in 100 mM glycine-NaOH (pH 9.2), at 25°C
0.53
4-methylbenzaldehyde
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in 100 mM glycine-NaOH (pH 9.2), at 25°C
0.46
benzaldehyde
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in 100 mM glycine-NaOH (pH 9.2), at 25°C
0.33
NAD+
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in the presence of benzaldehyde, 100 mM glycine-NaOH (pH 9.2), at 25°C
additional information
additional information
Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9
2-hydroxymuconate-6-semialdehyde
pH 8.5, 25°C, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2100
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate
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apparent value, in 100 mM Tris-HCl, pH 8.5, at 25°C
1600
2-hydroxymuconate-6-semialdehyde
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apparent value, in 100 mM Tris-HCl, pH 8.5, at 25°C
22
3-Chlorobenzaldehyde
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apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25°C
330
3-Fluorobenzaldehyde
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apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25°C
8
3-Methoxybenzaldehyde
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apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25°C
36
3-methylbenzaldehyde
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apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25°C
20
3-Nitrobenzaldehyde
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apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25°C
10
4-methylbenzaldehyde
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apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25°C
32
benzaldehyde
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apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25°C
56
NAD+
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apparent value, in the presence of benzaldehyde, 100 mM glycine-NaOH (pH 9.2), at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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enzyme from cell extract shows a specific activity of 0.0041 units/mg in 100 mM sodium phosphate, pH 7.5, at 24°C. After 17fold purification, the enzyme shows a specific activity of 0.071 units/mg in 100 mM sodium phosphate, pH 7.5, at 24°C, in 100 mM sodium phosphate, pH 7.5, at 24°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.3
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pH optimum for the oxidation of 2-hydroxymuconic semialdehyde
9.6
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pH optimum for the oxidation of benzaldehyde
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53188
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x * 53188, calculated from amino acid sequence
58000
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x * 58000, SDS-PAGE
184000
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme structure analysis by dynamic light scattering, small-angle X-ray scattering experiments and circular dichroism spectroscopy
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, TSKgel DEAE-5PW column chromatography, Affigel-Blue affinity chromatography, and TSKgel Phenyl-5PW column chromatography
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recombinant soluble N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, tag cleavage by TEV protease, and another nickel affinity chromatography step, followed by gel filtration and ultrafiltration
streptomycin sulfate precipitation, ammonium sulfate precipitation, DE52 cellulose column chromatography, DEAE-cellulofine column chromatography, and DEAE-Toyopearl column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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gene nahI, the naphthalene catabolic genes (nah) of NAH7 are organized into two operons on a 83 kilobase plasmid, recombinant expression of soluble N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha