EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.19 | expressed in Escherichia coli | Thermococcus kodakarensis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.1.1.19 | 12600 | - |
6 * 12600 + 6 * 4500, (alphabeta)6 complex, denaturant gel electrophoresis | Thermococcus kodakarensis |
4.1.1.19 | 99400 | - |
gel filtration | Thermococcus kodakarensis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.19 | L-arginine | Thermococcus kodakarensis | first step of polyamine biosynthesis | agmatine + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.19 | Thermococcus kodakarensis | Q5JFI4 | - |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
4.1.1.19 | proteolytic modification | synthesized as an inactive proenzyme | Thermococcus kodakarensis |
4.1.1.19 | 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 (Ser44) 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 | Thermococcus kodakarensis |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.19 | recombinant enzyme | Thermococcus kodakarensis |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
4.1.1.19 | 0.28 | - |
pH 6.0, 70-90°C | Thermococcus kodakarensis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.19 | L-arginine | first step of polyamine biosynthesis | Thermococcus kodakarensis | agmatine + CO2 | - |
? | |
4.1.1.19 | L-arginine | no activity with ornithine and lysine | Thermococcus kodakarensis | agmatine + CO2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.1.19 | hexamer | 6 * 12600 + 6 * 4500, (alphabeta)6 complex, denaturant gel electrophoresis | Thermococcus kodakarensis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.19 | pyruvoyl-dependent arginine decarboxylase | - |
Thermococcus kodakarensis |
4.1.1.19 | Tk-PdaD | - |
Thermococcus kodakarensis |
4.1.1.19 | TK0149 | - |
Thermococcus kodakarensis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.1.19 | 70 | 90 | assay at | Thermococcus kodakarensis |
4.1.1.19 | 100 | - |
- |
Thermococcus kodakarensis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.1.19 | 6 | - |
assay at | Thermococcus kodakarensis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.19 | additional information | pyruvoyl-dependent decarboxylase, synthesised as zymogen. The pyruvoyl cofactor results from the self-modification of an internal serine (Ser44) residue of the proenzyme, the pyruvoyl group functions through the formation of a Schiff base with the substrate to promote decarboxylation | Thermococcus kodakarensis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.1.1.19 | physiological function | a gene disruptant lacking arginine decarboxylase is constructed, showing that it grows only in the medium in the presence of agmatine but not in the absence of agmatine. The results indicates that agmatine is essential for the cell growth of Thermococcus kodakaraensis | Thermococcus kodakarensis |