Article
Calcium regulation of non-kinase and kinase activities of recombinant myosin light-chain kinase and its mutants.
IUBMB life - 1 Nov 2009
Xie Ce, Zhang Yue, Wang Hong Hui, Matsumoto Atsushi, Nakamura Akio, Ishikawa Ryoki, Yoshiyama Shinji, Hayakawa Kohichi, Kohama Kazuhiro, Gao Ying
Abstract excerpt
Myosin light-chain kinase (MLCK) comprised of N-terminal actin-binding domain, central catalytic domain, and C-terminal myosin-binding domain. It exerted not only kinase activity to phosphorylate 20 kDa regulatory light chain of smooth muscle but also exerted non-kinase activity on myosin motor and myosin ATPase activities (Nakamura et al., Biochem. Biophys. Res. Commun. 2008, 369, 135). The previous studies on...
Topics
- Actins
- Binding Sites
- Calcium
- Calcium-Binding Proteins
- Catalytic Domain
- Escherichia coli
- Mutation
- Myosin Light Chains
- Myosin-Light-Chain Kinase
- Myosins
- Protein Structure, Tertiary
- Recombinant Proteins
