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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Interaction of Non-Phosphorylated Liver Pyruvate Kinase with Fructose 1,6-Bisphosphate and Peptides that Mimic the Phosphorylatable N-terminus of the Enzyme

Author(s): Ilona Faustova and Jaak Järv

Volume 20, Issue 11, 2013

Page: [1200 - 1203] Pages: 4

DOI: 10.2174/09298665113209990008

Price: $65

Abstract

The interaction of non-phosphorylated L-type pyruvate kinase (L-PK) with fructose 1,6-bisphosphate (FBP), which is an allosteric activator of the phosphorylated enzyme, and peptides that mimic the phosphorylatable N-terminal regulatory domain of the enzyme, was studied. It was found that the catalytic activity of the enzyme was not enhanced in the presence of FBP, and this ligand acted as a relatively weak reversible inhibitor of the enzyme activity in the micromolar concentration range. The phosphorylation site analogue peptides RRASVA and RRAAVA had no effect on the activity of the enzyme, while the phosphorylated peptide RRAS(Pi)VA reversibly inhibited the enzyme and this process was characterised by the Ki value 47 μM. As the phosphorylated form of L-PK is a subject of significant allosteric regulation by FBP, it was concluded that phosphorylation should function as a molecular switch of the allosteric properties of this enzyme.

Keywords: Allosteric effector, fructose 1, 6-bisphosphate, L-type pyruvate kinase, N-terminal domain, peptide, phosphoenolpyruvate.


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