title: Cyclic activity of L-asparaginase through reversible phosphorylation in Leptosphaeria michotii.
abstract: Asparaginase in L. michotii has previously been shown to have an activity rhythm, the mechanisms of which were investigated. In vitro activation, or reactivation after dephosphorylation, of the partially (200-fold) purified asparaginase with protein kinase activity was obtained by ATP or Pi addition; these effects varied according to the phase of the activity rhythm at which enzyme was extracted. A high-Mr aggregate with asparaginase activity was phosphorylated by [gamma-32P]ATP. By SDS-electrophoresis of dephosphorylated asparaginase a approximately 60-kDa 32P-labelled protein with alkaline phosphatase activity became detectable. Regulation of the asparaginase activity rhythm in L. michotii is dependent on a reversible phosphorylation process.
mesh_terms: D001203:Ascomycota / Q000201:enzymology*; D001215:Asparaginase / Q000378:metabolism*; D007700:Kinetics; D010766:Phosphorylation; D013172:Spores, Fungal / Q000201:enzymology; D013098:Xylariales / Q000201:enzymology* / Q000254:growth & development
chemical_list: D001215:Asparaginase