Acylation and carbamylation of equine muscle carbonic anhydrase (CA-III) upon reaction with p-nitrophenyl esters and carbamoyl phosphate.
Equine muscle carbonic anhydrase (CA-III) behaves like ubiquitin in undergoing extensive acylation of N epsilon-lysine residues upon reacting with p-nitrophenyl esters. The enzyme undergoes extensive carbamoylation of lysine residues when reacted with carbamoyl phosphate. The modification of from 6 to 7 lysine residues results in the production of a series of more anodic electrophoretic components. The derivatization of the lysine residues leads to a marked decrease in the enzyme's ability to hydrate CO2. The equine CA-III possesses both acid and alkaline phosphatase activities in contrast to the rabbit which possesses only the former type.
D000215:Acylation; D000818:Animals; D002219:Carbamates / Q000494:pharmacology*; D002221:Carbamyl Phosphate / Q000494:pharmacology*; D002256:Carbonic Anhydrases / Q000378:metabolism*; D004952:Esters; D006736:Horses; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008239:Lysine; D009132:Muscles / Q000201:enzymology*; D009596:Nitrophenols / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D002219:Carbamates; D004952:Esters; D009596:Nitrophenols; D002221:Carbamyl Phosphate; D002256:Carbonic Anhydrases; D008239:Lysine