Information on EC 1.1.1.312 - 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.312
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RECOMMENDED NAME
GeneOntology No.
2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP+ = 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
protocatechuate degradation I (meta-cleavage pathway)
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Tyrosine metabolism
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Benzoate degradation
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Aminobenzoate degradation
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SYSTEMATIC NAME
IUBMB Comments
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal:NADP+ 2-oxidoreductase
The enzyme does not act on unsubstituted aliphatic or aromatic aldehydes or glucose; NAD+ can replace NADP+, but with lower affinity. The enzyme was initially believed to act on 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and produce 4-carboxy-2-hydroxy-cis,cis-muconate [1]. However, later studies showed that the substrate is the hemiacetal form [3], and the product is 2-oxo-2H-pyran-4,6-dicarboxylate [2,4].
CAS REGISTRY NUMBER
COMMENTARY hide
67272-39-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain SYK-6; SYK-6
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NAD+
4-carboxy-2-hydroxy-cis,cis-muconate + NADH
show the reaction diagram
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH
show the reaction diagram
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+ + H2O
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH + 2 H+
show the reaction diagram
4-carboxy-2-hydroxymuconate semialdehyde + NADP+
2-pyrone-4,6-dicarboxylic acid + NADPH + H2O
show the reaction diagram
protocatechuate + NADP+ + H2O
2-pyrone-4,6-dicarboxylic acid + NADPH + H+
show the reaction diagram
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
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+ + H2O
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH + 2 H+
show the reaction diagram
additional information
?
-
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2-pyrone-4,6-dicarboxylic acid may be a metabolic intermediate in the bacterial metabolism of protocatechuic acid
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-pyrone-4,6-dicarboxylic acid
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non-competitive inhibition with respect to 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde
5,5'-dithiobis(2-nitrobenzoate)
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1 h at 0.1 mM inhibits 98% of enzyme activity
Blue dextran
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competitive inhibitor with respect to NADP+
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HgCl2
methoxy Reactive Blue 2
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inhibits the enzyme non-competitively with respect to 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and competitively with respect to NADP+
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Monoiodoacetic acid
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weaker inhibitor than p-chloromercuribenzoate or HgCl2
N-ethylmaleimide
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weaker inhibitor than p-chloromercuribenzoate or HgCl2
NADH
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competitive inhibition with respect to NAD+, non-competitive inhibition with respect to 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde
NADPH
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competitive inhibition with respect to NADP, non-competitive inhibition with respect to 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde
p-chloromercuribenzoate
Reactive blue 2
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inhibits the enzyme non-competitively with respect to 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and competitively with respect to NADP+
Reactive Blue 4
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inhibits the enzyme non-competitively with respect to 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and competitively with respect to NADP+
additional information
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not: various metal ions, metal chelating reagents, reducing reagents
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Lubrol
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the enzyme activity increases in a sigmoidal manner with increasing concentrations, minimum concentration necessary for the increase of enzyme activity is higher than 0.05 mM, effectively eliminates the dye inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 0.075
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde
0.252 - 0.284
NAD+
0.0061 - 0.314
NADP+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00006
Blue dextran
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-
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0.0002
methoxy Reactive Blue 2
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0.072
Reactive blue 2
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0.0045
Reactive Blue 4
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coenzyme NADP+, similar value with coenzyme NAD+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
360
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after purification from the cell extract of Escherichia coli
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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fermenter condition for production of 2-pyrone-4,6-dicarboxylic acid, PDC
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.3
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at pH 5.5 and 9.3: about 50% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
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highest stability
288243
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42
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10 min, pH 7.0, 50% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, for at least 4 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from the cell extract of Escherichia coli, using POROS polyethyleneimine anion-exchange chromatography, POROS quaternized PI anion-exchange chromatography and POROS phenylether hydrophobic-interaction chromatography
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recombinant enzyme expressed in Escherichia coli
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using gel filtration on Sephadex G-200
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase gene ligC expressed in Escherichia coli
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coexpression with protocatechuate 4,5-dioxygenase in Pseudomonas putida PpY1100; into the pKT230MC vector for expression in Pseudomonas putida PpY1100 and into pUC119 for DNA amplification in Escherichia coli DH5alpha
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
industry