Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli. The phylogeny of the crenarchaeal homologs suggests that the arginine decarboxylase gene evolves from a single duplication of an ancestral S-adenosylmethionine decarboxylase gene early in the crenarchaeota | Saccharolobus solfataricus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit | Saccharolobus solfataricus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
difluoromethyl-L-arginine | 1 mM, 80 °C, 15 min, 64% loss of activity, irreversible inhibition | Saccharolobus solfataricus | |
difluoromethyl-L-ornithine | 1 mM, reduces activity by 20% | Saccharolobus solfataricus | |
L-argininamide | 1 mM, almost completely abolished arginine decarboxylase activity | Saccharolobus solfataricus | |
L-arginine methyl ester | 1 mM, 70% loss of activity | Saccharolobus solfataricus | |
L-canavanine | 1 mM, 46% inhibition | Saccharolobus solfataricus | |
L-histidine | 1 mM, 20-30% inhibition | Saccharolobus solfataricus | |
L-homoarginine | 1 mM, 20-30% inhibition | Saccharolobus solfataricus | |
additional information | 1 mM phenylhydrazine does not inactivate the enzyme. No inhibition with D-arginine, L-citrulline, L-lysine, Nalpha-methyl-L-arginine, L-methionine, Nalpha-nitro-L-arginine methyl ester, or L-ornithine | Saccharolobus solfataricus | |
Nalpha-acetyl-L-arginine | 1 mM, 20-30% inhibition | Saccharolobus solfataricus | |
O-(4-nitrobenzyl)hydroxylamine | 1 mM, 50% inhibition, pyruvoyl group modification | Saccharolobus solfataricus | |
O-Methylhydroxylamine | 1 mM, 50% inhibition, pyruvoyl group modification | Saccharolobus solfataricus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.2 | - |
L-arginine | pH 6.5, 70°C | Saccharolobus solfataricus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | no stimulation by KCl | Saccharolobus solfataricus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
6123 | - |
4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE | Saccharolobus solfataricus |
11759 | - |
4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE | Saccharolobus solfataricus |
17940 | - |
inactive proenzyme, mass spectrometry | Saccharolobus solfataricus |
80000 | - |
His10-tagged enzyme, gel filtration | Saccharolobus solfataricus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginine | Saccharolobus solfataricus | - |
agmatine + CO2 | - |
? | |
L-arginine | Saccharolobus solfataricus P2 | - |
agmatine + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharolobus solfataricus | Q9UWU1 | - |
- |
Saccharolobus solfataricus P2 | Q9UWU1 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | synthesized as an inactive proenzyme | Saccharolobus solfataricus |
pyruvoyl group formation | the enzyme is synthesized as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue (Ser82) via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme | Saccharolobus solfataricus |
Purification (Comment) | Organism |
---|---|
- |
Saccharolobus solfataricus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginine | - |
Saccharolobus solfataricus | agmatine + CO2 | - |
? | |
L-arginine | the crenarchaeal arginine decarboxylase has no S-adenosylmethionine decarboxylase activity | Saccharolobus solfataricus | agmatine + CO2 | - |
? | |
L-arginine | - |
Saccharolobus solfataricus P2 | agmatine + CO2 | - |
? | |
L-arginine | the crenarchaeal arginine decarboxylase has no S-adenosylmethionine decarboxylase activity | Saccharolobus solfataricus P2 | agmatine + CO2 | - |
? | |
L-canavanine | decarboxylation at 40% of the activity compared with L-arginine | Saccharolobus solfataricus | N-(3-aminopropoxy)guanidine + CO2 | - |
? | |
L-canavanine | decarboxylation at 40% of the activity compared with L-arginine | Saccharolobus solfataricus P2 | N-(3-aminopropoxy)guanidine + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
octamer | 4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE | Saccharolobus solfataricus |
Synonyms | Comment | Organism |
---|---|---|
ARGDC | - |
Saccharolobus solfataricus |
protein SSO0536 | - |
Saccharolobus solfataricus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
assay at | Saccharolobus solfataricus |
80 | - |
- |
Saccharolobus solfataricus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
90 | - |
pH 6.0, 10 min, enzyme retains 80% of ist original activity | Saccharolobus solfataricus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.6 | - |
L-arginine | pH 6.5, 70°C | Saccharolobus solfataricus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
- |
Saccharolobus solfataricus |
6.5 | - |
assay at | Saccharolobus solfataricus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 6 | pH 4.0: about 65% of maximal activity, pH 6.0: optimum | Saccharolobus solfataricus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Pyruvoyl group | pyruvoyl-dependent decarboxylase, synthesised as zymogen. The pyruvoyl cofactor results from the self-modification of an internal serine (Ser82) residue of the proenzyme, the pyruvoyl group functions through the formation of a Schiff base with the substrate to promote decarboxylation | Saccharolobus solfataricus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
13 | - |
L-arginine | pH 6.5, 70°C | Saccharolobus solfataricus |