Literature summary for 2.7.3.3 extracted from

Si, Y.X.; Song, J.J.; Fang, N.Y.; Wang, W.; Wang, Z.J.; Yang, J.M.; Qian, G.Y.; Yin, S.J.; Park, Y.D.
Purification, characterization, and unfolding studies of arginine kinase from Antarctic krill (2014), Int. J. Biol. Macromol., 67, 426-432.

Search for more literature for 2.7.3.3

Inhibitors

Inhibitors	Comment	Organism	Structure
SDS	complete inactivation at 1.0 mM, the inactivation is a first-order reaction, with the kinetic processes shifting from a monophase to biphase as SDS concentrations increase. SDS concentrations lower than 5 mM do not induce conspicuous changes in tertiary structures, while higher concentrations of SDS exposedhydrophobic surfaces and induce conformational changes	Euphausia superba

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.3	-	L-arginine	pH 8.0, 20°C	Euphausia superba
0.47	-	ATP	pH 8.0, 20°C	Euphausia superba

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Euphausia superba

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
40000	-	1 * 40000	Euphausia superba

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-arginine	Euphausia superba	-	ADP + Nomega-phospho-L-arginine	-	r

Organism

Organism	UniProt	Comment	Textmining
Euphausia superba	W8GJF4	from Antarctic krill	-

Purification (Commentary)

Purification (Comment)	Organism
native enzyme from muscle, 2.4fold by ammonium sulfate fractionation, gel filtration, and affinity chromatography	Euphausia superba

Source Tissue

Source Tissue	Comment	Organism	Textmining
muscle	-	Euphausia superba	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1780	-	pH 8.0, 20°C, purified native enzyme from muscles	Euphausia superba

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-arginine	-	Euphausia superba	ADP + Nomega-phospho-L-arginine	-	r

Subunits

Subunits	Comment	Organism
monomer	1 * 40000	Euphausia superba

Synonyms

Synonyms	Comment	Organism
ATP: L-arginine phosphotransferase	-	Euphausia superba
ESAK	-	Euphausia superba

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	-	Euphausia superba

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
-	60	activity range, 50% activity at 0°C and 52°C, profile overview	Euphausia superba

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
84.8	-	L-arginine	pH 8.0, 20°C	Euphausia superba

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	-	Euphausia superba

pH Range

pH Minimum	pH Maximum	Comment	Organism
6	10	activity range, profile overview	Euphausia superba

Cofactor

Cofactor	Comment	Organism	Structure
ADP	-	Euphausia superba
ATP	-	Euphausia superba

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.56	-	pH 8.0, 20°C	Euphausia superba	SDS

General Information

General Information	Comment	Organism
additional information	the active region of enzyme AK is more flexible than the overall enzyme molecule	Euphausia superba

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
282.7	-	L-arginine	pH 8.0, 20°C	Euphausia superba

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Release 2023.1 (January 2023)