Bovine brain calmodulin-dependent protein kinase II: molecular mechanisms of autophosphorylation.

Abstract:

:A bovine brain calmodulin-dependent protein kinase undergoes autophosphorylation with a maximal incorporation of 10 mol phosphate per mol enzyme. The autophosphorylated enzyme is fully active, independent of Ca2+ and calmodulin. Although the autophosphorylation reaction depends on Ca2+ and calmodulin, it can be rendered Ca(2+)-independent after about 15 seconds when 1 mol phosphate has been incorporated per mol enzyme. This Ca(2+)-independent autophosphorylation is an intramolecular reaction, since mixing of autophosphorylated and non-phosphorylated calmodulin-dependent protein kinase does not result in the Ca(2+)-independent phosphorylation of the non-phosphorylated enzyme. The Ca(2+)-independent autophosphorylation can be inhibited by an exogenous substrate, e.g., casein. The casein phosphorylation activity is approximately proportional to the level of phosphorylation of the enzyme.

authors

Zhang GY,Wang JH,Sharma RK

doi

10.1006/bbrc.1993.1269

subject

Has Abstract

pub_date

1993-03-15 00:00:00

pages

669-74

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)71269-6

journal_volume

191

pub_type

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