The enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide. The enzyme is activated by carboxylic acids.
Specify your search results
The expected taxonomic range for this enzyme is: Priestia megaterium
the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide
the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide
the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide
the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
pyrrole-2-carboxylate carboxy-lyase
The enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide. The enzyme is activated by carboxylic acids.
the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide
the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide
the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide
the enzyme catalyses both the carboxylation and decarboxylation reactions. However, while bicarbonate is the preferred substrate for the carboxylation reaction, decarboxylation produces carbon dioxide
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)
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)
if a carboxylic acid, such as acetate, is omitted from the reaction using the pure enzyme, no enzyme activity is found. As soon as a carboxylic acid is added, the decarboxylation starts immediately. The enzyme activity is increased with the number of carbon atoms, rising from formate to butyrate. Above four carbon atoms, the activity decreases. Pimelate, butyrate and propionate are the strongest activators
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)
if a carboxylic acid, such as acetate, is omitted from the reaction using the pure enzyme, no enzyme activity is found. As soon as a carboxylic acid is added, the decarboxylation starts immediately. The enzyme activity is increased with the number of carbon atoms, rising from formate to butyrate. Above four carbon atoms, the activity decreases. Pimelate, butyrate and propionate are the strongest activators
if a carboxylic acid, such as acetate, is omitted from the reaction using the pure enzyme, no enzyme activity is found. As soon as a carboxylic acid is added, the decarboxylation starts immediately. The enzyme activity is increased with the number of carbon atoms, rising from formate to butyrate. Above four carbon atoms, the activity decreases. Pimelate, butyrate and propionate are the strongest activators
if a carboxylic acid, such as acetate, is omitted from the reaction using the pure enzyme, no enzyme activity is found. As soon as a carboxylic acid is added, the decarboxylation starts immediately. The enzyme activity is increased with the number of carbon atoms, rising from formate to butyrate. Above four carbon atoms, the activity decreases. Pimelate, butyrate and propionate are the strongest activators
if a carboxylic acid, such as acetate, is omitted from the reaction using the pure enzyme, no enzyme activity is found. As soon as an carboxylic acid is added, the decarboxylation starts immediately. The enzyme activity is increased with the number of carbon atoms, rising from formate to butyrate. Above four carbon atoms, the activity decreases. Pimelate, butyrate and propionate are the strongest activators
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
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
4.1.1.93 pyrrole-2-carboxylate decarboxylase
more
top
