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Information on EC 1.2.1.85 - 2-hydroxymuconate-6-semialdehyde dehydrogenase
for references in articles please use BRENDA:EC1.2.1.85
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EC Tree 1 Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.1 With NAD+ or NADP+ as acceptor
1.2.1.85 2-hydroxymuconate-6-semialdehyde dehydrogenase
IUBMB Comments
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 . Activity with NAD+ is more than 10-fold higher than with NADP+ . cf. EC 1.2.1.32, aminomuconate-semialdehyde dehydrogenase.
The enzyme appears in viruses and cellular organisms
- 1.2.1.85
- ethylene
-
2-hydroxymuconic
-
ankyrin
-
2,3-dioxygenase
- 4-oxalocrotonate
-
ubiquitin-mediated
-
ligases
- auxin
Reaction Schemes
showSynonyms
hms dehydrogenase, 2-hydroxymuconate-6-semialdehyde dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-hydroxymuconate semialdehyde dehydrogenase
2-hydroxymuconic semialdehyde dehydrogenase
5C-2HMS dehydrogenase
NAD+-dependent 2-hydroxy-muconic 6-semialdehyde dehydrogenase
NahI
praB
XylG
praB
-
-
-
-
XylG
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
2,3-dihydroxybenzoate degradation, 4-amino-3-hydroxybenzoate degradation, catechol degradation to 2-hydroxypentadienoate II, protocatechuate degradation III (para-cleavage pathway)
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
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+
-
Substrates: -
Products: -
Products: -
?
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+
-
Substrates: -
Products: -
Products: -
?
3-fluorobenzaldehyde + NAD+ + H2O
3-fluorobenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
4-methylbenzaldehyde + NAD+ + H2O
4-methylbenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
5-chloro-2-hydroxymuconic semialdehyde + NAD+ + H2O
5-chloro-2-hydroxymuconic acid + NADH + H+
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: 113% activity compared to 2-hydroxymuconate-6-semialdehyde
Products: -
Products: -
?
butyraldehyde + NAD+ + H2O
butanoate + NADH + H+
-
Substrates: 138% activity compared to 2-hydroxymuconate-6-semialdehyde
Products: -
Products: -
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
Substrates: 16.5% activity compared to 2-hydroxymuconate-6-semialdehyde
Products: -
Products: -
?
propionaldehyde + NAD+ + H2O
propanoate + NADH + H+
-
Substrates: 107% activity compared to 2-hydroxymuconate-6-semialdehyde
Products: -
Products: -
?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + H+
-
Substrates: 100% activity
Products: -
Products: -
?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + H+
-
Substrates: 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+
Products: -
Products: -
?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
5-chloro-2-hydroxymuconic semialdehyde + NAD+ + H2O
5-chloro-2-hydroxymuconic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
5-chloro-2-hydroxymuconic semialdehyde + NAD+ + H2O
5-chloro-2-hydroxymuconic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: 25% activity compared to 2-hydroxymuconate-6-semialdehyde
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: weak substrate
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme NahI is highly specific for its biological substrate, 2-hydroxymuconate semialdehyde, no activity with salicylaldehyde, another intermediate in the naphthalene-degradation pathway
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme NahI is highly specific for its biological substrate, 2-hydroxymuconate semialdehyde, no activity with salicylaldehyde, another intermediate in the naphthalene-degradation pathway
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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+
Substrates: -
Products: -
Products: -
?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0093
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate
-
in 100 mM Tris-HCl, pH 8.5, at 25Ā°C
0.33
NAD+
-
in the presence of benzaldehyde, 100 mM glycine-NaOH (pH 9.2), at 25Ā°C
additional information
additional information
Michaelis-Menten kinetics
-
0.0013
2-hydroxymuconate-6-semialdehyde
pH 8.5, 25Ā°C, recombinant enzyme
0.017
2-hydroxymuconate-6-semialdehyde
-
in 100 mM Tris-HCl, pH 8.5, at 25Ā°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.9
2-hydroxymuconate-6-semialdehyde
pH 8.5, 25Ā°C, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2100
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate
-
apparent value, in 100 mM Tris-HCl, pH 8.5, at 25Ā°C
1600
2-hydroxymuconate-6-semialdehyde
-
apparent value, in 100 mM Tris-HCl, pH 8.5, at 25Ā°C
22
3-Chlorobenzaldehyde
-
apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25Ā°C
330
3-Fluorobenzaldehyde
-
apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25Ā°C
8
3-Methoxybenzaldehyde
-
apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25Ā°C
36
3-methylbenzaldehyde
-
apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25Ā°C
20
3-Nitrobenzaldehyde
-
apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25Ā°C
10
4-methylbenzaldehyde
-
apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25Ā°C
32
benzaldehyde
-
apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25Ā°C
56
NAD+
-
apparent value, in the presence of benzaldehyde, 100 mM glycine-NaOH (pH 9.2), at 25Ā°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme from cell extract shows a specific activity of 0.0041 units/mg in 100 mM sodium phosphate, pH 7.5, at 24Ā°C. After 17fold purification, the enzyme shows a specific activity of 0.071 units/mg in 100 mM sodium phosphate, pH 7.5, at 24Ā°C, in 100 mM sodium phosphate, pH 7.5, at 24Ā°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
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
-
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
-
metabolism
-
the enzyme is involved in benzene or toluene degradation
-
physiological function
the enzyme is involved in the degradation of intermediate 2-hydroxymuconate 6-semialdehyde in the naphthalene-degradation pathway
physiological function
-
the enzyme is involved in the degradation of intermediate 2-hydroxymuconate 6-semialdehyde in the naphthalene-degradation pathway
-
Show AA Sequence and Transmembrane Helices (780 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
tetramer
x * 51712, recombinant detagged enzyme, mass spectrometry, x * 55000, recombinant N-terminally His-tagged enzyme, SDS-PAGE
tetramer
-
x * 51712, recombinant detagged enzyme, mass spectrometry, x * 55000, recombinant N-terminally His-tagged enzyme, SDS-PAGE
-
additional information
enzyme protein structure analysis by circular dichroism spectroscopy, and three-dimensional structure model, overview
additional information
-
enzyme protein structure analysis by circular dichroism spectroscopy, and three-dimensional structure model, overview
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme structure analysis by dynamic light scattering, small-angle X-ray scattering experiments and circular dichroism spectroscopy
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, TSKgel DEAE-5PW column chromatography, Affigel-Blue affinity chromatography, and TSKgel Phenyl-5PW column chromatography
-
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
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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., Bordetella sp. 10d
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.
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
-
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)
brenda
de Lima-Morales, D.; Chaves-Moreno, D.; Wos-Oxley, M.L.; Jauregui, R.; Vilchez-Vargas, R.; Pieper, D.H.
Degradation of benzene by Pseudomonas veronii 1YdBTEX2 and 1YB2 is catalyzed by enzymes encoded in distinct catabolism gene clusters
Appl. Environ. Microbiol.
82
167-173
2015
Pseudomonas veronii, Pseudomonas veronii 1YB2, Pseudomonas veronii 1YdBTEX2
brenda
EXTERNAL LINKS (specific for EC-Number 1.2.1.85)
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