Abstract
Calmodulin is a calcium-binding protein of 16,800 daltons which underwrites many of the enzyme-activating actions of calcium in eucaryotic tissues (Klee and Vanaman, 1982; Cheung, 1980). There are four calcium-binding domains in calmodulin; each domain binds one calcium with micromolar affinity. Calmodulin undergoes a conformational change when it binds calcium (Walsh, et al, 1979) and then can bind to calmodulinbinding proteins (Means and Dedman, 1980). altering their biological activities. Several calmodulin-binding proteins have been identified as important enzymes; these include cyclic nucleotide phosphodiesterase (Cheung, 1970), adenylate cyclase (Brostrom, et al, 1975), Ca2+, Mg2+ ATPase (Gopinath and Vincenzi, 1977), NAD kinase (Roberts, et al, 1984), protein kinase (Browning, et al, 1985), Phosphorylase kinase (Cohen, et al, 1978), myosin light chain kinase (Dabrowska, et al, 1978), tyrosine hydroxylase (Vuillet, 1985), phosphoprotein phosphatase (Klee, et al, 1983) and an hepatic protein methyltransferase (Siegel and Wright, 1985). Calmodulin also binds to a number of other calmodulin-binding proteins with as-yet-unknown biological activities. The distribution of calmodulin-binding proteins differs between tissues and subcellular fractions, presumably reflecting tissue and organelle differences in calmodulin activities (Means and Dedman, 1980).
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Siegel, F.L. (1988). Enzymatic N-Methylation of Calmodulin. In: Zappia, V., Galletti, P., Porta, R., Wold, F. (eds) Advances in Post-Translational Modifications of Proteins and Aging. Advances in Experimental Medicine and Biology, vol 231. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-9042-8_27
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DOI: https://doi.org/10.1007/978-1-4684-9042-8_27
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