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Phosphorylation of Sepharose-coupled peptides by protein kinase A
Tartu universitet. (Jaak Järv)
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)
1996 (English)In: Bioorganic chemistry (Print), ISSN 0960-894X, E-ISSN 1090-2120, Vol. 24, no 1, 1-9 p.Article in journal (Refereed) Published
Abstract [en]

The kinetics of phosphorylation of the Sepharose-coupledpeptide RRASVA by catalytic subunit of proteinkinaseA, and diastereomers of this peptide, containingd-amino acids successively in each position, were studied. Coupling of these peptides with the amino and carboxyl termini to CH- and AH-Sepharoses had similar effects on the phosphorylation reaction, increasing theKmand decreasing theVvalues, respectively. The diastereomeric peptides were also phosphorylated by the enzyme and the rate of this reaction depended on the position of substitution ofl-amino acids with theird-analogs. However, this dependence was much less pronounced if compared with stereoselectivity of the enzyme in reactions with these peptides in solution: theKmvalues for the Sepharose-coupledpeptides were almost insensitive to the replacement ofl-amino acids withd-analogs and moderate stereoselectivity was revealed in the maximal velocity of the reaction. The Sepharose-coupledpeptide containingd-serine was also phosphorylated by proteinkinaseA while the same peptide in solution did not interact with the enzyme. Consequently, the polymer, enveloping the phosphorylatable peptide, may remarkably influence the recognition of the reaction site, altering both V and Km values.

Place, publisher, year, edition, pages
1996. Vol. 24, no 1, 1-9 p.
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-173202DOI: 10.1006/bioo.1996.0001OAI: oai:DiVA.org:uu-173202DiVA: diva2:516898
Available from: 2012-04-20 Created: 2012-04-20 Last updated: 2017-12-07Bibliographically approved

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