Inhibitors | Comment | 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 Maximum [mM] | Substrate | Comment | 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 | Comment | 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 Maximum [Da] | Comment | 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus sp. | - |
- |
- |
Purification (Comment) | Organism |
---|---|
purification of reductase component and oxygenase component | Rhodococcus sp. |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
culture condition:pyrrole-2-carboxylate-grown cell | - |
Rhodococcus sp. | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.82 | - |
pH 7.5, 30°C | Rhodococcus sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | Rhodococcus sp. | ? | - |
? | |
pyrrole-2-carboxylate + NADH + H+ + O2 | no activity with NADPH | 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 | Rhodococcus sp. | 5-hydroxypyrrole-2-carboxylate + NAD+ + H2O | - |
? |
Subunits | Comment | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | - |
- |
Rhodococcus sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
- |
Rhodococcus sp. |
Cofactor | Comment | 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. |
General Information | Comment | 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. |