Abstract
Myosin light chain kinase illustrates well how an enzyme simultaneously affects and is affected by interlocking pieces in the puzzle of smooth muscle regulation. Coincident with binding calcium-calmodulin (Ca2+-CaM), myosin light chain kinase (MLCK) is apparently released from pseudosubstrate inhibition and allowed to phosphorylate its substrate, the regulatory myosin light chain (MLC) (Pearson et al., 1988). These events at least facilitate (Sobieszek, 1977; Persechini et al., 1981), and probably trigger, (Itoh et al., 1989) the initiation of contraction in smooth muscle.
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© 1991 Plenum Press, New York
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Garone, L.M. (1991). Isoforms (Conformations?) of Turkey Gizzard Myosin Light Chain Kinase: Separation by Anion Exchange High Performance Liquid Chromatography. In: Moreland, R.S. (eds) Regulation of Smooth Muscle Contraction. Advances in Experimental Medicine and Biology, vol 304. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6003-2_30
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DOI: https://doi.org/10.1007/978-1-4684-6003-2_30
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