YAKHAK HOEJI (약학회지)

The Pharmaceutical Society of Korea (대한약학회)
권호 표지

Changes in Kinetic Properties of $Ca^{2+}$/Calmodulin-Dependent Protein Kinase la Activated by $Ca^{2+}$/Calmodulin-Dependent Protein Kinase I Kinase

칼슘/칼모듈린-의존성 단백질 키나아제 I 키나아제에 의한 칼슘/칼모듈린-의존성 단백질 키나아제 Ia의 활성화에 따른 효소반응 특성의 변화

  • Cho, Jung-Sook (Department of Pharmacology, College of Medicine, Dongguk University)
  • 조정숙 (동국대학교 의과대학 의학과 약리학교실)
  • Published : 1997.12.01
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Abstract

The activity of $Ca^{2+}$calmodulin (CaM)-dependent protein kinase Ia (CaM kinase Ia) is shown to be regulated through direct phosphorylation by CaM kinase I kinase (CaMK IK). In the present study, three distinct CaMKIK peaks were separated from Q-Sepharose colunm chromatography of pig brain homogenate using a Waters 650 Protein Purification System. The purified CaMKIK from the major peak potently and rapidly enhanced CaM kinase Ia activity, reaching a maximal stimulation within 2min at the concentrations of 12-15nM. The activated state of CaM kinase Ia is characterized by a markedly enhanced $V_{max}4 as well as significantly decreased $K_m\;and\;K_a$ values toward peptide substrate and CaM, respectively. These observations suggest the activation process of CaM kinase Ia. The phosphorylation of CaM kinase Ia by CaMKIK may induce its conformational change responsible for the alterations in the kinetic properties, which ultimately leads to the rapid enzyme activation.

Keywords

References

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