Information on EC 1.13.11.16 - 3-carboxyethylcatechol 2,3-dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.16
-
RECOMMENDED NAME
GeneOntology No.
3-carboxyethylcatechol 2,3-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate
show the reaction diagram
(2)
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-
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3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
show the reaction diagram
(1)
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
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-
redox reaction
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-
-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-phenylpropanoate and 3-(3-hydroxyphenyl)propanoate degradation to 2-oxopent-4-enoate
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cinnamate and 3-hydroxycinnamate degradation to 2-oxopent-4-enoate
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-
3-phenylpropionate degradation
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Phenylalanine metabolism
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase (decyclizing)
An iron protein. This enzyme catalyses a step in the pathway of phenylpropanoid compounds degradation.
CAS REGISTRY NUMBER
COMMENTARY hide
105503-63-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene mhpB
SwissProt
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
2,3-dihydroxycinnamic acid + O2
2-hydroxy-6-oxonona-2,4,7-trienoate
show the reaction diagram
2,3-dihydroxyphenoxyacetic acid + O2
2-hydroxyhexa-2,4-dienoic acid-6-carboxymethylester
show the reaction diagram
-
-
-
-
?
2,3-dihydroxyphenylpropionic acid + O2
2-hydroxy-6-oxonona-dienoate
show the reaction diagram
3-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
show the reaction diagram
3-ethylcatechol + O2
2-hydroxy-6-oxoocta-2,4-dienoate
show the reaction diagram
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
show the reaction diagram
3-phenethylcatechol + O2
2-hydroxy-6-oxo-8-phenylocta-2,4-dienoate
show the reaction diagram
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-
-
-
?
3-propylcatechol + O2
2-hydroxy-6-oxonona-2,4-dienoate
show the reaction diagram
-
-
-
-
?
catechol + O2
2-hydroxy-6-oxohexa-2,4-dienoate
show the reaction diagram
meta-ring-cleavage
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-
?
methyl-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-dienoic acid-9-methylester
show the reaction diagram
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-
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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
3-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diethyl dicarbonate
p-hydroxymercuribenzoate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014 - 0.036
2,3-dihydroxycinnamic acid
0.3
2,3-dihydroxyphenoxyacetic acid
-
-
0.0071 - 0.026
3-(2,3-dihydroxyphenyl)propionate
0.059 - 0.185
3-ethylcatechol
0.09 - 0.13
3-methylcatechol
0.094
3-phenethylcatechol
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-
0.154
3-propylcatechol
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0.72
catechol
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0.037
methyl-2,3-dihydroxyphenylpropionate
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29
3-(2,3-dihydroxyphenyl)propionate
Escherichia coli
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3.6
3-methylcatechol
Escherichia coli
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2
catechol
Escherichia coli
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
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2,3-dihydroxyphenylproponic acid
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9.5
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
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gel filtration
134000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 36000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity stable in crude extract, inactive apoenzyme stable, can be re-activated by treatment with Fe2+ and ascorbate, irreversible apoenzyme activity loss if stored in completely Fe2+-free buffer, re-activated holoenzyme unstable
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Show AA Sequence (719 entries)
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