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Information on EC 1.14.13.130 - pyrrole-2-carboxylate monooxygenase for references in articles please use BRENDA:EC1.14.13.130
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IUBMB Comments A flavoprotein (FAD). The enzyme initiates the degradation of pyrrole-2-carboxylate.
The enzyme appears in viruses and cellular organisms
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pyrrole-2-carboxylate + NADH + H+ + O2 = 5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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pyrrole-2-carboxylate,NADH:oxygen oxidoreductase (5-hydroxylating)
A flavoprotein (FAD). The enzyme initiates the degradation of pyrrole-2-carboxylate.
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pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
additional information
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no enzymatic activity is detected with the analogous aromatic heterocyclic compounds furan-2-carboxylate and furan-3-carboxylate, and thiophene-2-carboxylate and thiophene-3-carboxylate (0.25 mM). Pyrrole, proline, indole, and indole-2-carboxylate (each 0.25 mM) do not serve as a substrate or effector of NADH oxidation for pyrrole-2-carboxylate monooxygenase. Chlorinated phenols and 4-hydroxyphenylacetate, which are substrates for the structurally related two-component flavin aromatic monooxygenases isolated from different sources, do not affect NADH oxidation or oxygen consumption catalyzed by pyrrole-2-carboxylate monooxygenase
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pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
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pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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no activity with NADPH. Narrow substrate specificity. Besides pyrrole-2-carboxylate, only pyrrole, pyrrole-2-aldehyde, and indole-2-carboxylate stimulate the oxygen consumption at a very low rate
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pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
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pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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no activity with NADPH. Narrow substrate specificity. Besides pyrrole-2-carboxylate, only pyrrole, pyrrole-2-aldehyde, and indole-2-carboxylate stimulate the oxygen consumption at a very low rate
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pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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no activity with NADPH
the product is unstable. A conversion of 5-hydroxypyrrole-2-carboxylate to 2-oxoglutarate seems to be possible by spontaneous and/or enzyme catayzed hydrolytic reactions
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pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
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pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
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pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
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pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
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FAD
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flavoprotein. Contains 2.7-3.6 mol of FAD per mol of enzyme
FAD
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flavoprotein, no activity with FMN. Half-maximum velocity is obtained at FAD concentration of 0.015 mM
NADH
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no activity with NADPH
NADH
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no activity with NADPH
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Co2+
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2 mM, activity increases about 50%
Mn2+
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2 mM, activity increases about 50%
additional information
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no positive effect is observed if 0.02 mM Fe2+ is added to the reaction mixture
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5,5'-dithiobis(2-nitrobenzoic acid)
bathophenanthroline disulfonic acid
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0.005 mM, 5 min incubation, 75% loss of activity
Cu+
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0.001-0.01 mM, 93% loss of activity
Cu2+
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1 mM, 5 min incubation, complete inactivation
Hg2+
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0.01-0.1 mM, 96% loss of activity
Zn2+
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1 mM, 5 min incubation, complete inactivation
additional information
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no inhibition by 1 mM EDTA or 1 mM arsenite
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5,5'-dithiobis(2-nitrobenzoic acid)
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0.5 mM, 87% loss of activity
5,5'-dithiobis(2-nitrobenzoic acid)
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0.1 mM, 5 min incubation, complete inactivation
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0.094
NADH
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pH 7.5, 30°C
0.024
pyrrole-2-carboxylate
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pH 7.5, 30°C
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7.2 - 9.5
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pH 7.2: 65% of maximal activity, pH 9.5: 68% of maximal activity
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physiological function
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the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
physiological function
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the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
physiological function
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the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
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P2CO_ARTSY
30
0
3325
Swiss-Prot
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54000
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the enzyme consists of two protein components, the reductase component and the oxygenase component. The reductase is a monomer (18700 Da, mass spectrometry) and the oxygenase is a trimer (3 * 54000, mass spectrometry, gel filtration)
60000
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x * 60000, SDS-PAGE
150000
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oxygenase component, gel filtration. The enzyme consists of two protein components, the reductase component and the oxygenase component. The reductase is a monomer (18700 Da, mass spectrometry) and the oxygenase is a trimer (3 * 54000, mass spectrometry, gel filtration)
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x * 60000, SDS-PAGE
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x * 60000, SDS-PAGE
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the enzyme consists of two protein components, the reductase component and the oxygenase component. The reductase is a monomer (18700 Da, mass spectrometry) and the oxygenase is a trimer (3 * 54000, mass spectrometry, gel filtration)
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FAD and dithioerythritol stabilize enzyme activity during purification
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-20°C, several months, stable
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FAD and dithioerythritol stabilize enzyme activity during purification
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purification of reductase component and oxygenase component
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activity is induced by wrowth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
activity is induced by wrowth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
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activity is induced by wrowth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
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Hormann, K; Andreesen, J.R.
Purification and characterization of a pyrrole-2-carboxylate oxygenase from Arthrobacter strain Py
Biol. Chem. Hoppe-Seyler
375
211-218
1994
Arthrobacter sp., Arthrobacter sp. Py1
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Becker, D.; Schräder, T.; Andreesen, J.R.
Two-component flavin-dependent pyrrole-2-carboxylate monooxygenase from Rhodococcus sp.
Eur. J. Biochem.
249
739-747
1997
Rhodococcus sp.
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Enzyme Nomenclature
1.14.13.130 pyrrole-2-carboxylate monooxygenase
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