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Substrate specificity of protein kinase C studied with peptides containing D-amino acid residues.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry. (Ulf Ragnarsson)
Tartu universitet.
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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1993 (English)In: Journal of Biochemistry, ISSN 0021-924X, Vol. 114, no 2, 177-180 p.Article in journal (Refereed) Published
Abstract [en]

A set of stereoisomeric nonapeptides KRPSQRAKY with one, two, or all L-amino acid residues replaced by the corresponding D-amino acids, and two analogs with L- and D-threonine instead of serine, were synthesized and tested as substrates for protein kinase C. All of the peptides were phosphorylated by the enzyme. The maximal rate of the reaction with the all-D peptide was more than one order of magnitude lower than that for all-L peptide with serine. The same applied to the peptides with D-Ser or with D-Arg in position +2 with respect to Ser. The Km values for the peptides containing one D-amino acid were close to that for the prototype peptide (53 microM). On the other hand, when two or more D-amino acids were present, the Km value increased considerably. Replacement of serine by threonine also reduced the phosphorylation rate and increased the Km values. One can conclude that the stereospecificity of protein kinase C is much less pronounced than that of protein kinase A, which is in agreement with the less clearly pronounced substrate specificity of the former enzyme.

Place, publisher, year, edition, pages
1993. Vol. 114, no 2, 177-180 p.
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-173140PubMedID: 8262896OAI: oai:DiVA.org:uu-173140DiVA: diva2:516717
Available from: 2012-04-19 Created: 2012-04-19 Last updated: 2012-04-19Bibliographically approved

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