Studies on the Differential Specificity of Protein Kinases and Its Applications
Year: 2001
Type: article
Abstract: Loog, M. 2001. Studies on the differential specificity of protein kinases and its applications. Acta Universitatis Upsaliensis. Comprehensive Summaries of Uppsala Dissertations from the Faculty of Medicine 1073. 48 pp. Uppsala. ISBN 91-554-5116-0. Protein kinases are enzymes that catalyse the phosphoryl transfer from the Ȗ-phosphate of ATP to acceptor amino acids in proteins. The specificity of selected model protein kinases was studied at three different levels using a) novel bi-substrate-analogue inhibitors, b) synthetic peptide substrates and c) mutated protein substrate analogues. A new class of protein kinase bi-substrate-analogue inhibitors was designed on the basis of adenosine-5’-carboxylic acid derivatives, where a short arginine containing peptide was attached to the 5'-carbon atom of the adenosine sugar moiety via a linker chain. These compounds showed high inhibitory potential against two basophilic protein kinases, the protein kinase A (PKA) and protein kinase C (PKC), with IC50 values in the nanomolar range, but no inhibitory activity towards the acidophilic kinases CKI and CK2. The inhibitors were efficiently applied for affinity purification of PKA
Author: Mart Loog
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2165059710