Phosphorylation site sequence of smooth muscle myosin light chain (M r = 20 000)

FEBS Letters

Kemp, B.E.¹  Kendrick-Jones, J.¹  Jakes, R.¹  John, M.¹  Pearson, R.B.¹ 

[1] Howard Florey Institute of Experimental Physiology and Medicine, University of Melbourne, Parkville, Victoria 3052, Australia

关键词: Protein kinase;    Myosin;    Specificity;   

DOI  :  10.1016/0014-5793(84)80216-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The amino terminal sequence of the myosin light chain (M _r = 20 000) isolated from chicken gizzards was found to be acetyl-Ser-Ser-Lys-Arg-Ala-Lys-Ala-Lys-Thr-Thr-Lys-Lys-Arg-Pro-Gln-Arg-Ala-Thr-Ser(P)-Asn-Val-Phe. This sequence assignment differs from that reported by Maita et al. [(1981) European J. Biochem. 117, 417] in the order of the tryptic peptides. The revised amino acid sequence exhibits greater homology with the phosphorylation site sequences of the regulatory light chains from cardiac and skeletal muscle. Moreover it is now apparent why synthetic peptides corresponding to the previously reported sequence were very poor substrates for the myosin light chain kinase.

【 授权许可】

Unknown