A model for the regulation of the activity of L-asparaginase/ kinase enzyme of Tetrahymena pyriformis

Abstract

L-Asparaginase of Tetrahymena pyriformis is a lipoprotein with relative M(r) approximately 200 kDa and one subunit size of 39 kDa. This enzyme also exhibits protein kinase activity and it is autophosphorylated in tyrosine residues. Phosphorylation-dephosphorylation of L-asparaginase resulted in complete loss or activation by more than 10-fold of its catalytic activity. Both native and dephosphorylated forms of L-asparaginase are inactivated by phospholipase C and this inactivation can be reversed by the addition of lipids. Based on these results a working hypothesis is suggested that L-asparaginase of T. pyriformis exists in four interconvertible forms: Form A, phosphorylated complexed with lipids, form HA, dephosphorylated (highly active), form I, free of lipids, (inactive) and form B, free of lipids and phosphate.