Stability and kinetic behavior of carboxymethylated horse muscle acylphosphatase.
Horse muscle acylphosphatase consists of a main chain S-S bound to glutathione. It was found that removal of the glutathione by reduction and successive carboxymethylation of the only cysteine of the main chain affects the stability of the enzyme, mainly with respect to thermal inactivation. On the other hand, the kinetic properties of the enzyme are affected very little.
D017766:Acid Anhydride Hydrolases; D000478:Alkylation; D000818:Animals; D006736:Horses; D006863:Hydrogen-Ion Concentration; D007461:Iodoacetates; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D010755:Organophosphates; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011489:Protein Denaturation; D013696:Temperature; D014508:Urea / Q000494:pharmacology; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D007461:Iodoacetates; D010755:Organophosphates; D010744:Phosphoric Monoester Hydrolases; D014508:Urea; D000097024:Acylphosphatase