| Literature DB >> 10217418 |
J Feng1, M Ito, M Nishikawa, T Okinaka, N Isaka, D J Hartshorne, T Nakano.
Abstract
The dephosphorylation of the myosin light chain kinase and protein kinase C sites on the 20 kDa myosin light chain by myosin phosphatase was investigated. The myosin phosphatase holoenzyme and catalytic subunit, dephosphorylated Ser-19, Thr-18 and Thr-9, but not Ser-1/Ser-2. The role of noncatalytic subunits in myosin phosphatase was to activate the phosphatase activity. For Ser-19 and Thr-18, this was due to a decrease in Km and an increase in k(cat) and for Thr-9 to a decrease in Km. Thus, the distinction between the various sites is a property of the catalytic subunit.Entities:
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Year: 1999 PMID： 10217418 DOI： 10.1016/s0014-5793(99)00337-3
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124