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Literature summary for 1.14.13.130 extracted from

  • Becker, D.; Schräder, T.; Andreesen, J.R.
    Two-component flavin-dependent pyrrole-2-carboxylate monooxygenase from Rhodococcus sp. (1997), Eur. J. Biochem., 249, 739-747.
    View publication on PubMed

Inhibitors

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 [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

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 [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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Rhodococcus sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of reductase component and oxygenase component Rhodococcus sp.

Source Tissue

Source Tissue Comment 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] Comment Organism
1.82
-
pH 7.5, 30°C Rhodococcus sp.

Substrates and Products (Substrate)

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
Rhodococcus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Rhodococcus sp.

Cofactor

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

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.