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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The enzyme appears in viruses and cellular organisms

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EC NUMBER
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1.14.13.130
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RECOMMENDED NAME
GeneOntology No.
pyrrole-2-carboxylate monooxygenase
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REACTION
REACTION DIAGRAM
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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.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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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
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COFACTOR
ORGANISM
UNIPROT
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LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
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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
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INHIBITORS
ORGANISM
UNIPROT
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.82
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pH 7.5, 30°C
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
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LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
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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
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SUBUNITS
ORGANISM
UNIPROT
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LITERATURE
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.130)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)