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Literature summary for 2.7.3.3 extracted from

  • Fang, N.; Lee, J.; Yin, S.; Wang, W.; Wang, Z.; Yang, J.; Qian, G.; Si, Y.; Park, Y.
    Effects of osmolytes on arginine kinase from Euphausia superba: A study on thermal denaturation and aggregation (2014), Process Biochem., 49, 936-947.
No PubMed abstract available

General Stability

General Stability Organism
protective effects of osmolytes on the thermal denaturation and aggregation of arginine kinase from Euphausia superba: when the concentration of glycine, proline and glycerol increases, the relative activation is significantly enhanced, while the aggregation of the enzyme during thermal denaturation is decreased. The presence of these three osmolytes significantly decreases the tertiary structural changes of enzyme ESAK Euphausia superba

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required 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
-
-
-

Purification (Commentary)

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

Synonyms

Synonyms Comment Organism
ESAK
-
Euphausia superba

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
assay at Euphausia superba

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
thermal denaturation directly induced ESAK aggregation, glycine, proline and glycerol not only prevent enzyme ESAK from inactivation and unfolding but also inhibit aggregation by stabilizing the enzyme conformation. Evaluation of the inactivation kinetics and rate constants, calculation of the transition free energy Euphausia superba
5 50 purified enzyme, activity is relatively stable from 5°C to 23°C, but decreases rapidly from 25°C to 40°C. The activity is almost abolished at 50°C, half -life at 31.88°C Euphausia superba

pH Optimum

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

Cofactor

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

General Information

General Information Comment Organism
additional information enzyme structure homology modeling and docking simulations, overview Euphausia superba