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Mutants of smooth muscle myosin light chain kinase at tryptophan 800.

Abstract：

:The importance of Trp 800 in the calmodulin-binding site of myosin light chain kinase was investigated. Truncation mutants from Leu 447 to the C-terminus were expressed in E. coli and these were modified by point mutations of Trp 800 to Gly, Cys, Leu and Tyr. Trp at this position was more effective than any of the other residues. The Leu mutant was partially active and its Km for calmodulin decreased from about 10 nM to 175 nM. The Tyr mutant had detectable activity but the other two mutants were inactive and did not bind calmodulin. Thus Trp at position 800 is critical. The activity of the Leu mutant at high calmodulin concentrations was less than the wild-type mutant, about 20%. This suggests that the binding of calmodulin does not release inhibition in an all-or-none mechanism and that other intramolecular interactions are important.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Matsushima S,Huang YP,Dudas CV,Guerriero V Jr,Hartshorne DJ

doi

10.1006/bbrc.1994.2076

subject

Has Abstract

pub_date

1994-08-15 00:00:00

pages

1329-36

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(84)72076-6

journal_volume

202

pub_type

杂志文章

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