Title : Saccharomyces cerevisiae protein kinase dependent on Ca2+ and calmodulin.

Pub. Date : 1989 Mar

PMID : 2537817






3 Functional Relationships(s)
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1 When the kinase was incubated in the presence of ATP, Ca2+, and CaM before the assay, the enzyme showed activity even in the presence of the Ca2+ chelator ethylene glycol-bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid (EGTA) and TFP. Egtazic Acid calmodulin Saccharomyces cerevisiae S288C
2 When the kinase was incubated in the presence of ATP, Ca2+, and CaM before the assay, the enzyme showed activity even in the presence of the Ca2+ chelator ethylene glycol-bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid (EGTA) and TFP. Egtazic Acid calmodulin Saccharomyces cerevisiae S288C
3 At the highest level of conversion, Ca2+- and CaM-independent kinase activity, which was measured in the presence of EGTA and TFP, was nearly equal to the total kinase activity, which was measured in the presence of Ca2+ and CaM. Egtazic Acid calmodulin Saccharomyces cerevisiae S288C