Basic residues are important for Ca2+/calmodulin binding and activation but not autoinhibition of rabbit skeletal muscle myosin light chain kinase.

Abstract excerpt

Several allosterically modulated protein kinases have been shown to be regulated by an autoinhibitory domain located within the kinase molecules. The inhibitory domain has been proposed to act as a "pseudosubstrate" inhibitor binding to the substrate binding site of the kinase, thereby blocking the binding of the enzyme's true substrate. In this report, site-directed mutagenesis has been used to further...

Topics

• Amino Acid Sequence
• Animals
• Base Sequence
• Biotin
• Calcium
• Calmodulin
• Enzyme Activation
• Kinetics
• Molecular Sequence Data
• Muscles
• Mutation
• Myosin-Light-Chain Kinase