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Enzyme Nomenclature
Information on EC 1.14.13.130 - pyrrole-2-carboxylate monooxygenase
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1.14.13.130 pyrrole-2-carboxylate monooxygenaseIUBMB Comments
A flavoprotein (FAD). The enzyme initiates the degradation of pyrrole-2-carboxylate.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
pyrrole-2-carboxylate + NADH + H+ + O2 = 5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
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
-
-
?
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
-
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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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
-
the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
-
-
?
pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
-
the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
-
-
?
pyrrole-2-carboxylate + NADH + H+ + O2
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
-
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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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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flavoprotein, no activity with FMN. Half-maximum velocity is obtained at FAD concentration of 0.015 mM
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bathophenanthroline disulfonic acid
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0.005 mM, 5 min incubation, 75% 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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
-
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
-
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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)
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)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
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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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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.
brenda
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