Characterization of N omega-phosphoarginine hydrolase from rat liver.
N omega-Phosphoarginine hydrolase from rat liver hydrolyzed N omega-phosphoarginine into arginine and inorganic phosphate, whereas it did not release inorganic phosphate from 19 other phosphorylated compounds containing a N-P bond, an O-P bond or a C-P bond. In addition, it was not able to transfer the phosphoryl moiety from N omega-phosphoarginine to ADP. These results indicated that this enzyme was distinct from both phosphoamidase and arginine kinase. Its properties were as follows: thiol compounds were essential for its activity; it was stimulated by 1.5-2-fold in the presence of 0.001% Lubrol, Tween 20, poly(oxyethylene) 9-lauryl ether and Nonidet P-40, while 0.004% sodium lauryl sulfate inhibited the activity completely; concentrations of sodium molybdate and sodium vanadate necessary for 50% inhibition were 7 microM and 12 microM, respectively; some proteins stimulated the activity, while lysophosphatidic acid, lysophosphatidylinositol, and phosphatidic acid suppressed the activity even in the presence of poly(oxyethylene) 9-lauryl ether.
Kuba
M
M
Department of Biochemistry, Saga Medical School, Japan.
Ohmori
H
H
Kumon
A
A
D000818:Animals; D001120:Arginine / Q000031:analogs & derivatives* / Q000378:metabolism; D002712:Chlorides / Q000737:chemistry; D003902:Detergents; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008670:Metals / Q000737:chemistry; D009943:Organophosphorus Compounds / Q000378:metabolism; D010743:Phospholipids / Q000494:pharmacology; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors; D051381:Rats; D013379:Substrate Specificity
D002712:Chlorides; D003902:Detergents; D008670:Metals; D009943:Organophosphorus Compounds; D010743:Phospholipids; C015441:phospho-L-arginine; D001120:Arginine; D006867:Hydrolases; D010744:Phosphoric Monoester Hydrolases; C076871:N-omega-phosphoarginine hydrolase