Literature summary for 4.1.1.19 extracted from
Sun, X.; Song, W.; Liu, L.
Enzymatic production of agmatine by recombinant arginine decarboxylase (2015), J. Mol. Catal. B, 121, 1-8 .
No PubMed abstract available
Cloned(Commentary)
Cloned (Comment) |
Organism |
gene speA, recombinant overexpression of the enzyme in a soluble and active form in Escherichia coli strain BL21(DE3), method optimization leading to significant improvement of the production of agmatine. Method optimization, optimum conditions for agmatine production of the recombinant enzyme in vivo are 3.5 g/l intact cells, 4 mM Mg2+, 30 mM pyridoxal-5'-phosphate, pH 7, 37°C, method validation, overview. The specific activity of the overexpressing cell extract is 0.21 U/mg, which is 6.6fold higher than that of the BL21 cells not containing the overexpression plasmid |
Escherichia coli |
Inhibitors
Inhibitors |
Comment |
Organism |
Structure |
Cu2+ |
87% inhibition at 4 mM, complete inhibition at 8 mM |
Escherichia coli |
|
Fe2+ |
80% inhibition at 4 mM |
Escherichia coli |
|
Zn2+ |
97% inhibition at 4 mM, complete inhibition at 8 mM |
Escherichia coli |
|
KM Value [mM]
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
0.03 |
- |
L-arginine |
pH 7.5, 40°C, recombinant enzyme |
Escherichia coli |
|
Metals/Ions
Metals/Ions |
Comment |
Organism |
Structure |
Mg2+ |
required, best at 4 mM in vivo assay, 88% activation of recombinant enzyme at 4 mM |
Escherichia coli |
|
Mn2+ |
32% activation of recombinant enzyme at 4 mM |
Escherichia coli |
|
additional information |
no activation by Ca2+ at 4 mM |
Escherichia coli |
|
Natural Substrates/ Products (Substrates)
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
L-arginine |
Escherichia coli |
- |
agmatine + CO2 |
- |
? |
|
Organism
Organism |
UniProt |
Comment |
Textmining |
Escherichia coli |
P21170 |
- |
- |
Purification (Commentary)
Purification (Comment) |
Organism |
recombinant enzyme 12.4fold from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation and dialysis |
Escherichia coli |
Source Tissue
Source Tissue |
Comment |
Organism |
Textmining |
additional information |
method optimization, overview. Optimum conditions for agmatine production of the recombinant enzyme in vivo are 3.5 g/l intact cells, 4 mM Mg2+, 30 mM pyridoxal 5'-phosphate, pH 7, 37°C. SOC medium is optimal for ADC production compared to others |
Escherichia coli |
- |
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
0.53 |
- |
crude recombinant enzyme in transformed cells, pH 7.5, 40°C |
Escherichia coli |
2.6 |
- |
purified recombinant enzyme, pH 7.5, 40°C |
Escherichia coli |
Substrates and Products (Substrate)
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
L-arginine |
- |
Escherichia coli |
agmatine + CO2 |
- |
? |
|
Subunits
Subunits |
Comment |
Organism |
? |
x * 70000, recombinant enzyme, SDS-PAGE |
Escherichia coli |
Synonyms
Synonyms |
Comment |
Organism |
ADC |
- |
Escherichia coli |
Biosynthetic arginine decarboxylase |
UniProt |
Escherichia coli |
SpeA |
- |
Escherichia coli |
Temperature Optimum [°C]
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
50 |
- |
- |
Escherichia coli |
Temperature Range [°C]
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
30 |
70 |
over 70% of maximal activity within this range, profile overview |
Escherichia coli |
Temperature Stability [°C]
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
20 |
40 |
stable at, the purified recombinant enzyme is stable only up to 40°C with 78.6% of the activity remaining after a 1 h incubation at 40°C. Incubation at temperatures above this causes a rapid drop in activity |
Escherichia coli |
50 |
- |
purified recombinant enzyme, 1 h, inactivation |
Escherichia coli |
pH Optimum
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
7.5 |
- |
- |
Escherichia coli |
pH Range
pH Minimum |
pH Maximum |
Comment |
Organism |
6 |
8 |
over 70% of maximal activity within this range, profile overview |
Escherichia coli |
pH Stability
pH Stability |
pH Stability Maximum |
Comment |
Organism |
6 |
9 |
stable at, purified recombinant enzyme, 1 h, over 80% activity remaining |
Escherichia coli |
Cofactor
Cofactor |
Comment |
Organism |
Structure |
pyridoxal 5'-phosphate |
dependent on |
Escherichia coli |
|