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EC Tree
IUBMB Comments An iron protein. This enzyme catalyses a step in the pathway of phenylpropanoid compounds degradation.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
2,3-dihydroxy-beta-phenylpropionate 1,2-oxygenase, 2,3-dihydroxy-beta-phenylpropionate oxygenase, 2,3-dihydroxy-beta-phenylpropionic dioxygenase, 2,3-dihydroxyphenylpropionate 1,2-dioxygenase, 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase, MhpB,
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2,3-dihydroxy-beta-phenylpropionate 1,2-oxygenase
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2,3-dihydroxy-beta-phenylpropionate oxygenase
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2,3-dihydroxy-beta-phenylpropionic dioxygenase
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2,3-dihydroxyphenylpropionate 1,2-dioxygenase
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3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase
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(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate
(2)
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3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
(1)
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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.
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2,3-dihydroxycinnamic acid + O2
2-hydroxy-6-oxonona-2,4,7-trienoate
2,3-dihydroxyphenoxyacetic acid + O2
2-hydroxyhexa-2,4-dienoic acid-6-carboxymethylester
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?
2,3-dihydroxyphenylpropionic acid + O2
2-hydroxy-6-oxonona-dienoate
3-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
3-ethylcatechol + O2
2-hydroxy-6-oxoocta-2,4-dienoate
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
3-phenethylcatechol + O2
2-hydroxy-6-oxo-8-phenylocta-2,4-dienoate
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?
3-propylcatechol + O2
2-hydroxy-6-oxonona-2,4-dienoate
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?
catechol + O2
2-hydroxy-6-oxohexa-2,4-dienoate
meta-ring-cleavage
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?
methyl-(2,3-dihydroxyphenyl)propionate + O2
(2Z,4E)-2-hydroxy-9-methoxy-6,9-dioxonona-2,4-dienoic acid
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?
2,3-dihydroxycinnamic acid + O2
2-hydroxy-6-oxonona-2,4,7-trienoate
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?
2,3-dihydroxycinnamic acid + O2
2-hydroxy-6-oxonona-2,4,7-trienoate
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?
2,3-dihydroxyphenylpropionic acid + O2
2-hydroxy-6-oxonona-dienoate
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?
2,3-dihydroxyphenylpropionic acid + O2
2-hydroxy-6-oxonona-dienoate
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?
2,3-dihydroxyphenylpropionic acid + O2
2-hydroxy-6-oxonona-dienoate
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?
3-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
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?
3-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
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?
3-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
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?
3-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
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?
3-ethylcatechol + O2
2-hydroxy-6-oxoocta-2,4-dienoate
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?
3-ethylcatechol + O2
2-hydroxy-6-oxoocta-2,4-dienoate
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?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
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?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
meta-ring cleavage
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?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
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meta-ring cleavage
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?
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3-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
3-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
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?
3-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
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?
3-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
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?
3-(2,3-dihydroxyphenyl)propionate + O2
2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
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?
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Fe2+
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Fe2+
weakly bound, 1 mol per mol tetramer, by addition of Fe2+ re-activated apoenzyme
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2-(3,4-dihydroxyphenyl)-N-[(4-fluorophenyl)methyl]-N-hydroxyacetamide
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over 90% inhibition at 0.25 mM
N-benzyl-3-(3,4-dimethoxyphenyl)-N-hydroxypropanamide
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25% inhibition at 0.25 mM
diethyl dicarbonate
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DTNB
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p-hydroxymercuribenzoate
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p-hydroxymercuribenzoate
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0.014 - 0.036
2,3-dihydroxycinnamic acid
0.3
2,3-dihydroxyphenoxyacetic acid
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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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0.037
methyl-2,3-dihydroxyphenylpropionate
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0.014
2,3-dihydroxycinnamic acid
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0.036
2,3-dihydroxycinnamic acid
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0.0071
3-(2,3-dihydroxyphenyl)propionate
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0.026
3-(2,3-dihydroxyphenyl)propionate
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0.059
3-ethylcatechol
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0.09
3-methylcatechol
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0.13
3-methylcatechol
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29
3-(2,3-dihydroxyphenyl)propionate
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0.11
2-(3,4-dihydroxyphenyl)-N-[(4-fluorophenyl)methyl]-N-hydroxyacetamide
Rhodococcus jostii
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pH 7.5, 37°C
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4.3
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2,3-dihydroxyphenylproponic acid
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brenda
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brenda
gene mhpB
SwissProt
brenda
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brenda
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36000
4 * 36000, SDS-PAGE
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tetramer
4 * 36000, SDS-PAGE
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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
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
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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
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
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Geary, P.J.; Dagley, S.
The time sequence of interactions of a dioxygenase with its substrates
Biochim. Biophys. Acta
167
459-461
1968
Achromobacter sp.
brenda
Dagley, S.; Chapman, P.J.; Gibson, D.T.
The metabolism of beta-phenylpropionic acid by an Achromobacter
Biochem. J.
97
643-650
1965
Achromobacter sp.
brenda
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
brenda
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
brenda
Sainsbury, P.D.; Mineyeva, Y.; Mycroft, Z.; Bugg, T.D.
Chemical intervention in bacterial lignin degradation pathways development of selective inhibitors for intradiol and extradiol catechol dioxygenases
Bioorg. Chem.
60
102-109
2015
Rhodococcus jostii
brenda
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1.13.11.16 3-carboxyethylcatechol 2,3-dioxygenase
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