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Information on EC 1.2.1.85 - 2-hydroxymuconate-6-semialdehyde dehydrogenase for references in articles please use BRENDA:EC1.2.1.85Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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2-hydroxymuconate-6-semialdehyde dehydrogenase
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2-hydroxymuconate-6-semialdehyde + NAD+ + H2O = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
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2,3-dihydroxybenzoate degradation
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4-amino-3-hydroxybenzoate degradation
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catechol degradation to 2-hydroxypentadienoate II
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protocatechuate degradation III (para-cleavage pathway)
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Microbial metabolism in diverse environments
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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.
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2-hydroxymuconate semialdehyde dehydrogenase
2-hydroxymuconic semialdehyde dehydrogenase
NAD+-dependent 2-hydroxy-muconic 6-semialdehyde dehydrogenase
2-hydroxymuconate semialdehyde dehydrogenase
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2-hydroxymuconate semialdehyde dehydrogenase
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2-hydroxymuconic semialdehyde dehydrogenase
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2-hydroxymuconic semialdehyde dehydrogenase
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5C-2HMS dehydrogenase
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5C-2HMS dehydrogenase
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HMS dehydrogenase
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NAD+-dependent 2-hydroxy-muconic 6-semialdehyde dehydrogenase
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NAD+-dependent 2-hydroxy-muconic 6-semialdehyde dehydrogenase
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NahI
; gene name
praB
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XylG
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UniProt
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UniProt
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evolution
the naphthalene catabolic genes (nah) of NAH7 are organized into two operons. The nah operon (nahAaAbAcAdBFCED) encodes the upper pathway enzymes involved in the conversion of naphthalene to salicylate. On the other hand, the sal operon (nahGTHINLOMKJ) codes for the lower pathway enzymes involved in the conversion of salicylate to pyruvate and acetaldehyde. The lower pathway starts with the oxidation of salicylate to catechol by salicylate hydroxylase (NahG), which is extradiol-cleaved by catechol-2,3-dioxygenase (NahH) and further transformed to pyruvate and acetyl-CoA by the remaining meta-cleavage pathway gene products, NahI, NahJ, NahK, NahN, NahL, NahM, and NahO. Enzyme NahI is further classified into the ALDH8 family together with different 2-hydroxymuconate semialdehyde dehydrogenases
evolution
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the naphthalene catabolic genes (nah) of NAH7 are organized into two operons. The nah operon (nahAaAbAcAdBFCED) encodes the upper pathway enzymes involved in the conversion of naphthalene to salicylate. On the other hand, the sal operon (nahGTHINLOMKJ) codes for the lower pathway enzymes involved in the conversion of salicylate to pyruvate and acetaldehyde. The lower pathway starts with the oxidation of salicylate to catechol by salicylate hydroxylase (NahG), which is extradiol-cleaved by catechol-2,3-dioxygenase (NahH) and further transformed to pyruvate and acetyl-CoA by the remaining meta-cleavage pathway gene products, NahI, NahJ, NahK, NahN, NahL, NahM, and NahO. Enzyme NahI is further classified into the ALDH8 family together with different 2-hydroxymuconate semialdehyde dehydrogenases
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physiological function
the enzyme is involved in the degradation of intermediate 2-hydroxymuconate 6-semialdehyde in the naphthalene-degradation pathway
physiological function
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the enzyme is involved in the degradation of intermediate 2-hydroxymuconate 6-semialdehyde in the naphthalene-degradation pathway
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2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate + NAD+ + H2O
(2E,4Z)-2-hydroxy-5-methylhexa-2,4-diendioate + NADH + H+
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?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + H+
3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH + H+
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3-fluorobenzaldehyde + NAD+ + H2O
3-fluorobenzoate + NADH + H+
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3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + H+
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3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH + H+
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3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
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4-methylbenzaldehyde + NAD+ + H2O
4-methylbenzoate + NADH + H+
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5-chloro-2-hydroxymuconic semialdehyde + NAD+ + H2O
5-chloro-2-hydroxymuconic acid + NADH + H+
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
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113% activity compared to 2-hydroxymuconate-6-semialdehyde
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
butyraldehyde + NAD+ + H2O
butanoate + NADH + H+
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138% activity compared to 2-hydroxymuconate-6-semialdehyde
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formaldehyde + NAD+ + H2O
formate + NADH + H+
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16.5% activity compared to 2-hydroxymuconate-6-semialdehyde
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propionaldehyde + NAD+ + H2O
propanoate + NADH + H+
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107% activity compared to 2-hydroxymuconate-6-semialdehyde
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additional information
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2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
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2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
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2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + H+
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100% activity
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2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + H+
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the activity of crude enzyme for 2-hydroxymuconate-6-semialdehyde in the presence of NAD+ is about 11 times higher than that achieved with NADP+
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2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + H+
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the activity of crude enzyme for 2-hydroxymuconate-6-semialdehyde in the presence of NAD+ is about 11 times higher than that achieved with NADP+
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2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + H+
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5-chloro-2-hydroxymuconic semialdehyde + NAD+ + H2O
5-chloro-2-hydroxymuconic acid + NADH + H+
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5-chloro-2-hydroxymuconic semialdehyde + NAD+ + H2O
5-chloro-2-hydroxymuconic acid + NADH + H+
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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25% activity compared to 2-hydroxymuconate-6-semialdehyde
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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weak substrate
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additional information
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enzyme NahI is highly specific for its biological substrate, 2-hydroxymuconate semialdehyde, no activity with salicylaldehyde, another intermediate in the naphthalene-degradation pathway
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additional information
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enzyme NahI is highly specific for its biological substrate, 2-hydroxymuconate semialdehyde, no activity with salicylaldehyde, another intermediate in the naphthalene-degradation pathway
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2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
Q1XGK8
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2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
Q1XGK8
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NAD+
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highly specific for NAD+
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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
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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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0.0013
2-hydroxymuconate-6-semialdehyde
pH 8.5, 25°C, recombinant enzyme
0.017
2-hydroxymuconate-6-semialdehyde
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in 100 mM Tris-HCl, pH 8.5, at 25°C
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0.9
2-hydroxymuconate-6-semialdehyde
pH 8.5, 25°C, recombinant enzyme
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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
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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
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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
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brenda
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brenda
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brenda
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brenda
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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
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x * 53188, calculated from amino acid sequence; x * 58000, SDS-PAGE
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x * 53188, calculated from amino acid sequence; x * 58000, SDS-PAGE
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tetramer
x * 51712, recombinant detagged enzyme, mass spectrometry, x * 55000, recombinant N-terminally His-tagged enzyme, SDS-PAGE
tetramer
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x * 51712, recombinant detagged enzyme, mass spectrometry, x * 55000, recombinant N-terminally His-tagged enzyme, SDS-PAGE
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additional information
enzyme protein structure analysis by circular dichroism spectroscopy, and three-dimensional structure model, overview
additional information
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enzyme protein structure analysis by circular dichroism spectroscopy, and three-dimensional structure model, overview
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enzyme structure analysis by dynamic light scattering, small-angle X-ray scattering experiments and circular dichroism spectroscopy
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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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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
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XYLG_PSEPU
486
51761
Swiss-Prot
DMPC_PSEUF
486
51683
Swiss-Prot
A0A1J5R271_9ZZZZ
79
8761
TrEMBL
W7W721_9BURK
311
32835
TrEMBL
A0A1W6KB31_9ALTE
486
52132
TrEMBL
A0A0B5F5U3_9BURK
484
51906
TrEMBL
A0A238D8Y5_THIDL
503
53821
TrEMBL
A0A0M2HAC1_9MICO
519
56107
TrEMBL
A0A2H5ZSJ6_9BACT
78
8462
TrEMBL
A0A2S5CVW8_LYSSH
491
54182
TrEMBL
A0A143QN76_9NOCA
510
55257
TrEMBL
A0A1D3JYJ0_9PSED
486
52906
TrEMBL
A0A0F0LNU0_9MICO
512
55427
TrEMBL
A0A117EC48_STRSC
486
52052
TrEMBL
A0A2P9FAN0_9ACTN
486
51766
TrEMBL
W2UHE3_9GAMM
485
52195
TrEMBL
A0A2H5ZUP2_9BACT
485
53164
TrEMBL
A0A2H6AUK7_9BACT
487
53739
TrEMBL
A0A1D3K921_9PSED
486
51724
TrEMBL
A0A1Y0YL83_BACLI
494
54200
TrEMBL
A0A1J5QWH2_9ZZZZ
80
8860
TrEMBL
A0A2S6R213_9PROT
487
51627
TrEMBL
A0A1N7SGG1_9BURK
484
51734
TrEMBL
W7W6Q4_9BURK
311
32835
TrEMBL
W7WC76_9BURK
484
51193
TrEMBL
W7WUM3_9BURK
484
51193
TrEMBL
A0A021XHC1_9RHIZ
484
51641
TrEMBL
A0A1B1JX52_RHOOP
492
52899
TrEMBL
A0A2W8N4P5_9BURK
503
53434
TrEMBL
A0A1V5IWH1_9BACT
162
17478
TrEMBL
A0A2H5WBN6_9BACT
51
5437
TrEMBL
A0A0K6J6Q2_BACCE
489
54078
TrEMBL
A0A0L6CY22_9RHOB
460
49107
TrEMBL
W5YQG9_9ALTE
486
51913
TrEMBL
W7WNN9_9BURK
224
23971
TrEMBL
A0A0P1FTX3_THAGE
460
49237
TrEMBL
A0A238JAU7_9RHOB
460
49437
TrEMBL
A0A098BU08_9NOCA
492
52473
TrEMBL
A0A238U9K2_9FLAO
479
52635
TrEMBL
A0A0N0I4C1_9BACI
345
37659
TrEMBL
W7WQ67_9BURK
493
52227
TrEMBL
A0A238DV35_9BURK
503
53837
TrEMBL
A0A2N9BKP4_STRCX
487
52082
TrEMBL
A0A1X6ZI18_9RHOB
459
49212
TrEMBL
A0A100JTL1_STRSC
487
52032
TrEMBL
W7W4H3_9BURK
486
52461
TrEMBL
A0A0M2H6E5_9MICO
523
56116
TrEMBL
A0A0U4WI66_9BACL
492
54364
TrEMBL
A0A2K9ZCI2_RHILE
505
54046
TrEMBL
A0A0H4NWU2_9BACI
480
52800
TrEMBL
A0A1J5RRC6_9ZZZZ
503
53866
TrEMBL
A0A1E2ZID5_9GAMM
491
53197
TrEMBL
Q1XGK8_PSEPU
486
51517
TrEMBL
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Inoue, J.; Shaw, J.P.; Rekik, M.; Harayama, S.
Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida
J. Bacteriol.
177
1196-1201
1995
Pseudomonas putida, Pseudomonas putida KT 2240
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Orii, C.; Takenaka, S.; Murakami, S.; Aoki, K.
Metabolism of 4-amino-3-hydroxybenzoic acid by Bordetella sp. strain 10d: a different modified meta-cleavage pathway for 2-aminophenols
Biosci. Biotechnol. Biochem.
70
2653-2661
2006
Bordetella sp. 10d, Bordetella sp.
brenda
Kasai, D.; Fujinami, T.; Abe, T.; Mase, K.; Katayama, Y.; Fukuda, M.; Masai, E.
Uncovering the protocatechuate 2,3-cleavage pathway genes
J. Bacteriol.
191
6758-6768
2009
Paenibacillus sp., Paenibacillus sp. JJ-1b
brenda
Park, S.; Lee, D.; Kim, Y.; Lee, K.; Kim, C.
Cloning and nucleotide sequence analysis of xylG gene encoding 5C-2HMS dehydrogenase from Pseudomonas sp. S-47
Korean J. Appl. Microbiol. Bioeng.
30
8-14
2002
Pseudomonas sp., Pseudomonas sp. S-47
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brenda
de Araujo, S.; Neves, C.M.L.; Guimaraes, S.L.; Whitman, C.P.; Johnson Jr., W.H.; Aparicio, R.; Nagem, R.A.P.
Structural and kinetic characterization of recombinant 2-hydroxymuconate semialdehyde dehydrogenase from Pseudomonas putida G7
Arch. Biochem. Biophys.
579
8-17
2015
Pseudomonas putida (Q1XGK8), Pseudomonas putida G7 (Q1XGK8)
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