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Information on EC 1.13.11.16 - 3-carboxyethylcatechol 2,3-dioxygenase and Organism(s) Escherichia coli and UniProt Accession P0ABR9

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IUBMB Comments
An iron protein. This enzyme catalyses a step in the pathway of phenylpropanoid compounds degradation.
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This record set is specific for:
Escherichia coli
UNIPROT: P0ABR9
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
2,3-dihydroxyphenylpropionate 1,2-dioxygenase, 3-carboxyethylcatechol 2,3-dioxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2,3-dihydroxy-beta-phenylpropionate 1,2-oxygenase
-
-
-
-
2,3-dihydroxy-beta-phenylpropionate oxygenase
-
-
-
-
2,3-dihydroxy-beta-phenylpropionic dioxygenase
-
-
-
-
3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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
-
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
-
-
-
?
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
-
-
?
methyl-(2,3-dihydroxyphenyl)propionate + O2
(2Z,4E)-2-hydroxy-9-methoxy-6,9-dioxonona-2,4-dienoic acid
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
Fe2+
weakly bound, 1 mol per mol tetramer, by addition of Fe2+ re-activated apoenzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diethyl dicarbonate
-
p-hydroxymercuribenzoate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.036
2,3-dihydroxycinnamic acid
-
0.3
2,3-dihydroxyphenoxyacetic acid
-
0.026
3-(2,3-dihydroxyphenyl)propionate
-
0.185
3-ethylcatechol
-
0.09
3-methylcatechol
-
0.094
3-phenethylcatechol
-
0.154
3-propylcatechol
-
0.72
catechol
-
0.037
methyl-2,3-dihydroxyphenylpropionate
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29
3-(2,3-dihydroxyphenyl)propionate
-
3.6
3-methylcatechol
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene mhpB
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
134000
gel filtration
36000
4 * 36000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bugg, T.D.
Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli
Biochim. Biophys. Acta
1202
258-264
1993
Escherichia coli (P0ABR9), Escherichia coli
Manually annotated by BRENDA team
Spence, E.L.; Kawamukai, M.; Sanvoisin, J.; Braven, H.; Bugg, T.D.
Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases
J. Bacteriol.
178
5249-5256
1996
Cupriavidus necator, Escherichia coli (P0ABR9), Escherichia coli
Manually annotated by BRENDA team