Chemical modification studies on arginine kinase: essential cysteine and arginine residues at the active site

International Journal of Biological Macromolecules
Wen-Jing ZhuXiao-Yun Wang

Abstract

Chemical modification was used to elucidate the essential amino acids in the catalytic activity of arginine kinase (AK) from Migratoria manilensis. Among six cysteine (Cys) residues only one Cys residue was determined to be essential in the active site by Tsou's method. Furthermore, the AK modified by DTNB can be fully reactivated by dithiothreitol (DTT) in a monophasic kinetic course. At the same time, this reactivation can be slowed down in the presence of ATP, suggesting that the essential Cys is located near the ATP binding site. The ionizing groups at the AK active site were studied and the standard dissociation enthalpy (DeltaH degrees ) was 12.38kcal/mol, showing that the dissociation group may be the guanidino of arginine (Arg). Using the specific chemical modifier phenylglyoxal (PG) demonstrated that only one Arg, located near the ATP binding site, is essential for the activity of AK.

Citations

Dec 25, 2012·International Journal of Biological Macromolecules·Wei-Dong WangGuo-Lin Zou
May 31, 2012·International Journal of Biological Macromolecules·Qing-Yun WuKai-Lin Xu

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