Information on EC 1.14.13.130 - pyrrole-2-carboxylate monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.130
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RECOMMENDED NAME
GeneOntology No.
pyrrole-2-carboxylate monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
pyrrole-2-carboxylate + NADH + H+ + O2 = 5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
pyrrole-2-carboxylate,NADH:oxygen oxidoreductase (5-hydroxylating)
A flavoprotein (FAD). The enzyme initiates the degradation of pyrrole-2-carboxylate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Py1
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Manually annotated by BRENDA team
strain Py1
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
show the reaction diagram
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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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
pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.094
NADH
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pH 7.5, 30°C
0.061
O2
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pH 7.5, 30°C
0.024
pyrrole-2-carboxylate
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pH 7.5, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.82
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pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 9.5
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pH 7.2: 65% of maximal activity, pH 9.5: 68% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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)
160000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
FAD and dithioerythritol stabilize enzyme activity during purification
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several months, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FAD and dithioerythritol stabilize enzyme activity during purification
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purification of reductase component and oxygenase component
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activity is induced by wrowth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy