Abstract
5′-p-Fluorosulfonylbenzoyl adenosine (FSBA), an ATP-like affinity labelling reagent, reacted with rabbit skeletal muscle myosin light chain kinase (skMLCK) and its calmodulin complex in a site-specific manner. Reaction was dependent upon the presence of the adenosine moiety of FSBA, saturated with increasing FSBA, was inhibited by MgATP, and was accompanied by stoichiometric incorporation of [14C]FSBA. The kinetic constants describing the reaction were similar for skMLCK and its calmodulin complex: k3= -0.040 min-1 and -0.038 mint-1, and Ki=0.18 mM and 0.40 mM, respectively. It is concluded that the MgATP-binding site on skMLCK remains accessible at all times and maintains a near constant conformation.
Original language | English (US) |
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Pages (from-to) | 217-220 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 286 |
Issue number | 1-2 |
DOIs | |
State | Published - Jul 29 1991 |
Keywords
- 5′-p-Fluorosulfonylbenzoyl adenosine
- Autoinhibition
- Calmodulin
- Myosin light chain kinase
- Pseudosubstrate
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology