Literature summary for 2.7.3.3 extracted from

Wu, Q.Y.; Li, F.; Wang, X.Y.
Evidence that the amino acid residue P272 of arginine kinase is involved in its activity, structure and stability (2008), Int. J. Biol. Macromol., 43, 367-372.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Locusta migratoria manilensis

Protein Variants

Protein Variants	Comment	Organism
P272D	activity of the mutant P272D is about 40% of that of wild-type enzyme. The binding affinity of arginine and ATP in the P272D is much smaller than that of wild-type enzyme, as indicated by an about 2- to 3fold increase of the Km values for ATP and arginine. The mutation impairs the tertiary structures of the enzyme. Decrease in thermal stability	Locusta migratoria manilensis
P272G	decrease in thermal stability	Locusta migratoria manilensis
P272R	decrease in thermal stability	Locusta migratoria manilensis

General Stability

General Stability	Organism
the unfolding transition curves of mutations P272R and P272G are almost identical to wild-type enzyme for all conditions at GdnHCl concentrations varying from 0.1 to 6 M	Locusta migratoria manilensis

Organism

Organism	UniProt	Comment	Textmining
Locusta migratoria manilensis	-	-	-

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
30	-	10 min, wild-type enzyme, and mutant enzymes P272D, P272G and P272R are stable	Locusta migratoria manilensis
40	-	10 min, wild-type enzyme loses about 10% of its activity, mutant enzyme P272D loses about 30% of its activity, mutant enzyme P272G loses about 25% of its activity and mutant enzyme P272R loses about 35% of its activity	Locusta migratoria manilensis
50	-	10 min, wild-type enzyme loses about 40% of its activity, mutant enzyme P272D loses about 90% of its activity, mutant enzyme P272G loses about 85% of its activity and mutant enzyme P272R loses about 90% of its activity	Locusta migratoria manilensis

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Release 2023.1 (January 2023)