Information on EC 4.1.1.93 - pyrrole-2-carboxylate decarboxylase

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The expected taxonomic range for this enzyme is: Bacillus megaterium

EC NUMBER
COMMENTARY hide
4.1.1.93
-
RECOMMENDED NAME
GeneOntology No.
pyrrole-2-carboxylate decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
pyrrole-2-carboxylate + H2O = pyrrole + HCO3-
show the reaction diagram
pyrrole-2-carboxylate = pyrrole + CO2
show the reaction diagram
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pyrrole + HCO3-
pyrrole-2-carboxylate + H2O
show the reaction diagram
pyrrole-2-carboxylate
pyrrole + CO2
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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)
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-methyl-2-benzothiazolinonehydrazone
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1 mM, 26% inhibition
5,5'-dithiobis(2-nitrobenzoic acid)
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1 mM, 40% inhibition
AgNO3
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1 mM, complete inhibition
CuCl2
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1 mM, 97% inhibition
cysteamine
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1 mM, 25% inhibition
HgCl2
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1 mM, complete inhibition
KCN
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1 mM, 68% inhibition
NEM
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1 mM, 15% inhibition
p-chloromercuribenzoate
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1 mM, 75% inhibition
phenylhydrazine
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1 mM, 84% inhibition
Pyrrole
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substrate inhibition of carboxylation above 300 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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)
acetate
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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
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)
Butyrate
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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
formate
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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
pimelate
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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
propionate
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
560
HCO3-
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pH 5.5, 20°C
61
Pyrrole
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pH 5.5, 20°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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assay at, carboxylase reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8.5
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pH 4.0: about 40% of maximal activity, pH 8.5: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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assay at, carboxylase reaction
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
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2 * 52000, SDS-PAGE
98000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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stable
711887
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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pH 7.0, stable below
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, with dithiothreitol and glycerol, stable for 6 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE