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Information on EC 1.2.1.60 - 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase
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1.2.1.60 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenaseIUBMB Comments
Involved in the tyrosine degradation pathway in Arthrobacter sp.
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Word Map
- 1.2.1.60
- cadmium
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vacuolar
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tonoplast-localized
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indica
- atpase
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japonica
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xylem
- 4-hydroxyphenylacetate
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root-to-shoot
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meta-cleavage
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase, 5-carboxymethyl-2-hydroxymuconate semialdehyde:NAD+ oxidoreductase, 5-carboxymethyl-2-hydroxymuconic semialdehyde dehydrogenase, carboxymethylhydroxymuconic semialdehyde dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase
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5-carboxymethyl-2-hydroxymuconate semialdehyde:NAD+ oxidoreductase
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5-carboxymethyl-2-hydroxymuconic semialdehyde dehydrogenase
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carboxymethylhydroxymuconic semialdehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+ = 5-carboxymethyl-2-hydroxymuconate + NADH + 2 H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
5-carboxymethyl-2-hydroxymuconic-semialdehyde:NAD+ oxidoreductase
Involved in the tyrosine degradation pathway in Arthrobacter sp.
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CAS REGISTRY NUMBER
COMMENTARY
63241-20-3
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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
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NADP+
5-carboxymethyl-2-hydroxymuconate + NADPH
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
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involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
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?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
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involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
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?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
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-
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
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involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
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?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
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involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
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?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
Escherichia coli B / ATCC 11303
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involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
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?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
Escherichia coli B / ATCC 11303
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involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
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-
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
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-
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
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-
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NADP+
5-carboxymethyl-2-hydroxymuconate + NADPH
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11% of the activity compared to the reduction with NAD+
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?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NADP+
5-carboxymethyl-2-hydroxymuconate + NADPH
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1,5% of the activity compared to reduction with NAD+
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?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NADP+
5-carboxymethyl-2-hydroxymuconate + NADPH
Escherichia coli B / ATCC 11303
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1,5% of the activity compared to reduction with NAD+
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?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NADP+
5-carboxymethyl-2-hydroxymuconate + NADPH
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1,5% of the activity compared to reduction with NAD+
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?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NADP+
5-carboxymethyl-2-hydroxymuconate + NADPH
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18% of the activity compared to reduction with NAD+
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?
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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
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
-
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
Escherichia coli B / ATCC 11303
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
Escherichia coli B / ATCC 11303
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
-
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
-
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
-
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
5-carboxymethyl-2-hydroxymuconate semialdehyde + H2O + NAD+
5-carboxymethyl-2-hydroxymuconate + NADH
-
involved in the meta-cleavage pathway of 4-hydroxyphenylacetate
-
?
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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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
7.8
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less active in Tris-HCl buffer than in phosphate or glycine/NaOH buffers
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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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strict dependency for induction of enzyme synthesis of the meta-cleavage pathway by 4-hydroxyphenylacetate
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strict dependency for induction of enzyme synthesis of the meta-cleavage pathway by 4-hydroxyphenylacetate
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Show AA Sequence and Transmembrane Helices (500 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
heating at 50°C for 3 min and immediate chilling on ice abolishes enzyme activity in crude cell extracts
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity, chromatography techniques
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Blakley, E.R.
The catabolism of L-tyrosine by an Arthrobacter sp.
Can. J. Microbiol.
23
1128-1139
1977
Arthrobacter globiformis, Arthrobacter globiformis PRL W15
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Fawcett, T.; Garrido-Pertierra, A.; Cooper, R.A.
5-Carboxymethyl-2-hydroxymuconic semialdehyde dehydrogenases of Escherichia coli C and Klebsiella pneumoniae M5a1 show very high N-terminal sequence homology
FEMS Microbiol. Lett.
57
307-312
1989
Escherichia coli, Klebsiella pneumoniae, Klebsiella pneumoniae M5a1, Escherichia coli C
brenda
Alonso, J.M.; Garrido-Pertierra, A.
Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate catabolic pathway of Pseudomonas putida
Biochem. Cell Biol.
64
1288-1293
1986
Pseudomonas putida
-
brenda
Alonso, J.M.; Garrido-Pertierra, A.
Kinetic properties of 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase from Escherichia coli
Biochimie
68
731-737
1986
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Alonso, J.M.; Garrido-Pertierra, A.
Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli
Biochim. Biophys. Acta
719
165-167
1982
Escherichia coli
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Cooper, R.A.; Skinner, M.A.
Catabolism of 3- and 4-hydroxyphenylacetate by the 3,4-dihydroxyphenylacetate pathway in Escherichia coli
J. Bacteriol.
143
302-306
1980
Escherichia coli, Escherichia coli B / ATCC 11303, Escherichia coli C
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Barbour, M.G.; Bayly, R.C.
Control of meta-cleavage degradation of 4-hydroxyphenylacetate in Pseudomonas putida
J. Bacteriol.
147
844-850
1981
Pseudomonas putida, Pseudomonas putida NCIB 9865
brenda
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