BRENDA - Enzyme Database show
show all sequences of 1.14.13.130

Two-component flavin-dependent pyrrole-2-carboxylate monooxygenase from Rhodococcus sp.

Becker, D.; Schräder, T.; Andreesen, J.R.; Eur. J. Biochem. 249, 739-747 (1997)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
5,5'-dithiobis(2-nitrobenzoic acid)
0.1 mM, 5 min incubation, complete inactivation
Rhodococcus sp.
bathophenanthroline disulfonic acid
0.005 mM, 5 min incubation, 75% loss of activity
Rhodococcus sp.
Cu2+
1 mM, 5 min incubation, complete inactivation
Rhodococcus sp.
Zn2+
1 mM, 5 min incubation, complete inactivation
Rhodococcus sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.024
-
pyrrole-2-carboxylate
pH 7.5, 30°C
Rhodococcus sp.
0.061
-
O2
pH 7.5, 30°C
Rhodococcus sp.
0.094
-
NADH
pH 7.5, 30°C
Rhodococcus sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
2 mM, activity increases about 50%
Rhodococcus sp.
Mn2+
2 mM, activity increases about 50%
Rhodococcus sp.
additional information
no positive effect is observed if 0.02 mM Fe2+ is added to the reaction mixture
Rhodococcus sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
54000
-
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)
Rhodococcus sp.
150000
-
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)
Rhodococcus sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
pyrrole-2-carboxylate + NADH + H+ + O2
Rhodococcus sp.
the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodococcus sp.
-
-
-
Purification (Commentary)
Commentary
Organism
purification of reductase component and oxygenase component
Rhodococcus sp.
Source Tissue
Source Tissue
Commentary
Organism
Textmining
culture condition:pyrrole-2-carboxylate-grown cell
-
Rhodococcus sp.
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.82
-
pH 7.5, 30°C
Rhodococcus sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
708366
Rhodococcus sp.
?
-
-
-
-
pyrrole-2-carboxylate + NADH + H+ + O2
no activity with NADPH
708366
Rhodococcus sp.
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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
-
-
?
pyrrole-2-carboxylate + NADH + H+ + O2
the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
708366
Rhodococcus sp.
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
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)
Rhodococcus sp.
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
-
Rhodococcus sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Rhodococcus sp.
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
flavoprotein, no activity with FMN. Half-maximum velocity is obtained at FAD concentration of 0.015 mM
Rhodococcus sp.
NADH
no activity with NADPH
Rhodococcus sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
flavoprotein, no activity with FMN. Half-maximum velocity is obtained at FAD concentration of 0.015 mM
Rhodococcus sp.
NADH
no activity with NADPH
Rhodococcus sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
5,5'-dithiobis(2-nitrobenzoic acid)
0.1 mM, 5 min incubation, complete inactivation
Rhodococcus sp.
bathophenanthroline disulfonic acid
0.005 mM, 5 min incubation, 75% loss of activity
Rhodococcus sp.
Cu2+
1 mM, 5 min incubation, complete inactivation
Rhodococcus sp.
Zn2+
1 mM, 5 min incubation, complete inactivation
Rhodococcus sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.024
-
pyrrole-2-carboxylate
pH 7.5, 30°C
Rhodococcus sp.
0.061
-
O2
pH 7.5, 30°C
Rhodococcus sp.
0.094
-
NADH
pH 7.5, 30°C
Rhodococcus sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
2 mM, activity increases about 50%
Rhodococcus sp.
Mn2+
2 mM, activity increases about 50%
Rhodococcus sp.
additional information
no positive effect is observed if 0.02 mM Fe2+ is added to the reaction mixture
Rhodococcus sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
54000
-
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)
Rhodococcus sp.
150000
-
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)
Rhodococcus sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
pyrrole-2-carboxylate + NADH + H+ + O2
Rhodococcus sp.
the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
purification of reductase component and oxygenase component
Rhodococcus sp.
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
culture condition:pyrrole-2-carboxylate-grown cell
-
Rhodococcus sp.
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.82
-
pH 7.5, 30°C
Rhodococcus sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
708366
Rhodococcus sp.
?
-
-
-
-
pyrrole-2-carboxylate + NADH + H+ + O2
no activity with NADPH
708366
Rhodococcus sp.
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
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
-
-
?
pyrrole-2-carboxylate + NADH + H+ + O2
the enzyme initiates the degradation of pyrrole-2-carboxylate. Growth on pyrrole-2-carboxylate as the sole source of carbon, nitrogen and energy
708366
Rhodococcus sp.
5-hydroxypyrrole-2-carboxylate + NAD+ + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
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)
Rhodococcus sp.
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
-
Rhodococcus sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Rhodococcus sp.
General Information
General Information
Commentary
Organism
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
Rhodococcus sp.
General Information (protein specific)
General Information
Commentary
Organism
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
Rhodococcus sp.
Other publictions for EC 1.14.13.130
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
708366
Becker
Two-component flavin-dependent ...
Rhodococcus sp.
Eur. J. Biochem.
249
739-747
1997
-
-
-
-
-
-
4
3
-
3
2
1
-
3
-
-
1
-
-
1
1
-
3
1
1
-
-
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
4
-
3
-
3
2
1
-
-
-
1
-
1
1
-
3
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
707605
Hormann
Purification and characterizat ...
Arthrobacter sp., Arthrobacter sp. Py1
Biol. Chem. Hoppe-Seyler
375
211-218
1994
-
-
-
-
-
1
4
-
-
-
2
2
-
2
-
-
1
-
-
1
-
1
4
1
-
-
-
-
1
1
-
2
-
1
-
-
-
-
2
-
-
1
-
4
-
-
-
-
2
2
-
-
-
1
-
1
-
1
4
1
-
-
-
-
1
1
-
1
1
1
1
1
-
-