Literature summary for 2.7.3.3 extracted from

Zhu, W.J.; Li, M.; Wang, X.Y.
Chemical modification studies on arginine kinase: Essential cysteine and arginine residues at the active site (2007), Int. J. Biol. Macromol., 41, 564-571.

Search for more literature for 2.7.3.3

Activating Compound

Activating Compound	Comment	Organism	Structure
ATP	about 80% of the activity formerly inhibited by phenylglyoxal is retained by incubating with 20 mM ATP	Locusta migratoria manilensis
dithiothreitol	once treated with 5,5'-dithiobis-2-nitrobenzoic acid, the enzyme activity can be recovered more than 95% after incubation for 20 min with 0.15 mM dithiothreitol	Locusta migratoria manilensis

Inhibitors

Inhibitors	Comment	Organism	Structure
5,5'-dithiobis-2-nitrobenzoic acid	-	Locusta migratoria manilensis
DTNB	the arginine kinase modified by DTNB can be fully reactivated by dithiothreitol in a monophasic kinetic course. This reactivation can be slowed down in the presence of ATP, suggesting that the essential Cys is located near the ATP binding site	Locusta migratoria manilensis
Phenylglyoxal	the enzyme loses 84.7% of its initial activity after incubation for 90 min with 0.0009 mM phenyllyoxal	Locusta migratoria manilensis

Organism

Organism	UniProt	Comment	Textmining
Locusta migratoria manilensis	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
the arginine kinase modified by DTNB can be fully reactivated by dithiothreitol in a monophasic kinetic course	Locusta migratoria manilensis

Source Tissue

Source Tissue	Comment	Organism	Textmining
muscle	-	Locusta migratoria manilensis	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-Arg	-	Locusta migratoria manilensis	ADP + Nomega-phospho-L-Arg	-	r

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Release 2023.1 (January 2023)