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D-amino acid residues as substrate specificity determinants for casein kinase II
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (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 Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry. (Ragnarsson Ulf)
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1994 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 200, no 3, 1564-1569 p.Article in journal (Refereed) Published
Abstract [en]

A set of diastereomeric peptides RRRDDDSDDD each with a corresponding D-amino acid residue successively in every position (except the arginines) was tested as substrates for casein kinase II. It was found that the D-serine containing peptide was not detectably phosphorylated. The replacements at the positions +1, -1 and +2 decreased the kII values more than 60, 30 and 20 times, respectively. The effect of the L/D replacements decreased with increased distance from the serine. The D-amino acid scan used herein seems to be a helpful complementary tool for studies of substrate specificity determinants for different protein kinases.

Place, publisher, year, edition, pages
1994. Vol. 200, no 3, 1564-1569 p.
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-173141DOI: 10.1006/bbrc.1994.1629OAI: oai:DiVA.org:uu-173141DiVA: diva2:516718
Available from: 2012-04-19 Created: 2012-04-19 Last updated: 2017-12-07Bibliographically approved

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