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

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
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
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