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Comparision of substrate specificities of protein kinases A and C based on peptide substrates
(ek pia)
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry. (Ulf Ragnarsson)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (ek pia)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (engström lorentz)
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1994 (English)In: Bioorganic chemistry (Print), ISSN 0960-894X, E-ISSN 1090-2120, Vol. 22, no 3, 328-336 p.Article in journal (Refereed) Published
Abstract [en]

Peptides, obtained by gradual removal of amino acids from both ends of pEKRPSQRSKYL, and stereoisomeric nonapeptides KRPSQRAKY with one D-amino acid residue successively in each position, were tested as substrates for protein kinase A, All these compounds were phosphorylated but at quite different rates by the enzyme. Comparison of the kinetic data with the appropriate results for protein kinase C, measured earlier, was used to analyze and compare the specificity determining factors of these enzymes. The analysis of the cross-specificity points to the possibility that only a short part, mainly the sequence of 1 to 2 amino acids around the phosphorylatable serine residue, is important for differentiation of substrates by these enzymes, while the remaining part of the peptide structure has similar influence on their reactivity in the case of these two protein kinases. Thus, the active center of these enzymes can be conventionally divided into two parts, which are responsible for selectivity and effectiveness of the phosphorylation reaction, respectively.

Place, publisher, year, edition, pages
1994. Vol. 22, no 3, 328-336 p.
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-173192DOI: 10.1006/bioo.1994.1026OAI: oai:DiVA.org:uu-173192DiVA: diva2:516887
Available from: 2012-04-20 Created: 2012-04-20 Last updated: 2017-12-07Bibliographically approved

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