Partial characterisation of aspartate transcarbamylase from the mantle of the mussel Mytilus edulis.
The stability and the effect of pH and temperature on the activity of aspartate transcarbamylase from mantle of mussel were studied. The Km values for aspartic acid and carbamylphosphate at 35 degrees C are 1.8 X 10(-2) M and 7 X 10(-3) M respectively, values of Vmax being identical at 17.54 nM carbamylaspartate formed/min/mg protein. Allosteric effectors of ATCase (ATP and CTP) have no effect on the activity of mantle ATCase. PHMB and Cu2+ are strong inhibitors of the ATCase activity, organic solvents (DMF, DMSO) having a strong stimulatory action. ATCase from mantle of mussel has been compared to ATCase from different sources.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000494:Allosteric Regulation; D000818:Animals; D001221:Aspartate Carbamoyltransferase / Q000378:metabolism*; D049872:Bivalvia / Q000201:enzymology*; D003570:Cytidine Triphosphate / Q000494:pharmacology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D013045:Species Specificity; D014544:Uridine Triphosphate / Q000494:pharmacology
D003570:Cytidine Triphosphate; D000255:Adenosine Triphosphate; D001221:Aspartate Carbamoyltransferase; D014544:Uridine Triphosphate