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Studies on the substrate specificity of cAMP-dependent protein kinase using diastereomeric peptides
Tartu universitet. (Jaak Järv)
Tartu universitet. (engström lorentz)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology. (ek pia)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology. (ek pia)
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1991 (English)In: Biochemistry International, ISSN 0158-5231, Vol. 25, no 3, 453-460 p.Article in journal (Refereed) Published
Abstract [en]

A set of six different diastereomeric hexapeptides RRASVA, each with a D-amino acid residue successively in the six positions, was synthesized and tested as substrates of protein kinase A. It was found that the peptide with D-Ser was neither a substrate, nor an inhibitor of the enzyme. The other five peptides were active as substrates with slightly lower kcat values than that of the all-L amino acid peptide. However, the apparent Km values increased by one to two orders of magnitude, especially when the second arginine or the alanine residue preceding the serine was substituted. The results are discussed.

Place, publisher, year, edition, pages
1991. Vol. 25, no 3, 453-460 p.
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-173131PubMedID: 1805790OAI: oai:DiVA.org:uu-173131DiVA: diva2:516700
Available from: 2012-04-19 Created: 2012-04-19 Last updated: 2012-04-19Bibliographically approved

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