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Literature summary extracted from

  • Wieser, M.; Fujii, N.; Yoshida, T.; Nagasawa T.
    Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910 (1998), Eur. J. Biochem., 257, 495-499.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.1.93 2-mercaptoethanol reducing agents in optimal concentrations of 20 mM or above are a prerequisite for high CO2 fixation turnovers, with dithiothreitol enhancing the carboxylation 16.2fold compared with a control without reducing agent, followed by ascorbate (15.5fold), Na2S2O5 (13.6fold) and 2-mercaptoethanol (7.2fold) Priestia megaterium
4.1.1.93 ascorbate reducing agents in optimal concentrations of 20 mM or above are a prerequisite for high CO2 fixation turnovers, with dithiothreitol enhancing the carboxylation 16.2fold compared with a control without reducing agent, followed by ascorbate (15.5fold), Na2S2O5 (13.6fold) and 2-mercaptoethanol (7.2fold) Priestia megaterium

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.93 Pyrrole substrate inhibition of carboxylation above 300 mM Priestia megaterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.93 61
-
Pyrrole pH 5.5, 20°C Priestia megaterium
4.1.1.93 560
-
HCO3- pH 5.5, 20°C Priestia megaterium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.93 Na2S2O5 reducing agents in optimal concentrations of 20 mM or above are a prerequisite for high CO2 fixation turnovers, with dithiothreitol enhancing the carboxylation 16.2fold compared with a control without reducing agent, followed by ascorbate (15.5fold), Na2S2O5 (13.6fold) and 2-mercaptoethanol (7.2fold) Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.93 Priestia megaterium
-
-
-
4.1.1.93 Priestia megaterium PYR2910
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.1.93 pyrrole-2-carboxylate + H2O = pyrrole + HCO3- the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide Priestia megaterium
4.1.1.93 pyrrole-2-carboxylate = pyrrole + CO2 the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.93 additional information no carboxylation of thiophene, furan, indole, 1-methylpyrrole, 1-(2-cyanethyl)pyrrole, pyrrolidine, pyrazine, pyridine, pyridine-4-carboxamide, imidazole, n-butylimidazole, 1,2,3-triazole, 1,2,4-triazole, 1,3,5-triazine and thiazole Priestia megaterium ?
-
?
4.1.1.93 additional information no carboxylation of thiophene, furan, indole, 1-methylpyrrole, 1-(2-cyanethyl)pyrrole, pyrrolidine, pyrazine, pyridine, pyridine-4-carboxamide, imidazole, n-butylimidazole, 1,2,3-triazole, 1,2,4-triazole, 1,3,5-triazine and thiazole Priestia megaterium PYR2910 ?
-
?
4.1.1.93 pyrrole + HCO3- the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide Priestia megaterium pyrrole-2-carboxylate + H2O
-
?
4.1.1.93 pyrrole + HCO3- the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide Priestia megaterium PYR2910 pyrrole-2-carboxylate + H2O
-
?
4.1.1.93 pyrrole-2-carboxylate the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide Priestia megaterium pyrrole + CO2
-
?
4.1.1.93 pyrrole-2-carboxylate the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide Priestia megaterium PYR2910 pyrrole + CO2
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.93 20
-
assay at, carboxylase reaction Priestia megaterium
4.1.1.93 30
-
assay at, decarboxylase reaction Priestia megaterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.93 5.5
-
assay at, carboxylase reaction Priestia megaterium
4.1.1.93 7
-
assay at, decarboxylase reaction Priestia megaterium

General Information

EC Number General Information Comment Organism
4.1.1.93 physiological function despite a strong reverse reaction, it is assumed that reversible pyrrole-2-carboxylate decarboxylase takes part in the catabolism of pyrrole-2-carboxylate due to a slow decrease of the decarboxylation product pyrrole under resting cells conditions and the non-physiologically high Km-value for HCO23, which is substantially above the concentrations of HCO23 that probably occur in vivo Priestia megaterium