Cyclic activity of L‐asparaginase through reversible phosphorylation in Leptosphaeria michotii

FEBS Letters

Jerebzoff, Stéphan¹  Jerebzoff-Quintin, Simonne¹ 

[1] Department of Plant Physiology, CNRS, P. Sabatier University, 118, route de Narbonne, 31062 Toulouse Cédex, France

关键词: Asparaginase;    Protein kinase;    Alkaline phosphatase;    Rhythm;    Leptosphaeria michotii;   

DOI  :  10.1016/0014-5793(84)80461-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 P_i addition; these effects varied according to the phase of the activity rhythm at which enzyme was extracted. A high-M _r aggregate with asparaginase activity was phosphorylated by [γ-³²P]ATP. By SDS-electrophoresis of dephosphorylated asparaginase a ∼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.

【 授权许可】

Unknown