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- Title
Kinetic analysis of cooperativity of phosphorylated L-type pyruvate kinase.
- Authors
Faustova, Ilona; Järv, Jaak
- Abstract
Kinetics of L-type pyruvate kinase (EC 2.7.1.40) catalysed reaction between phosphoenolpyruvate (PEP) and ADP was analysed under steady-state conditions and the interaction of both substrates with the enzyme was characterized proceeding from bi-substrate kinetic mechanism of this process. Cooperative regulation of the rate of this process by one of the substrates, PEP, was taken into consideration by using a sequential ligand binding model. It was found that two PEP molecules may bind with similar affinity with the tetrameric enzyme (K =30mM), while the effectiveness of the binding of the next two substrate molecules is enhanced through cooperative interaction between the enzyme subunits, which decreases the dissociation constant of the enzyme—substrate complex approximately 10 times.
- Subjects
PYRUVATE kinase; CHEMICAL kinetics; ENZYMES; LIGAND binding (Biochemistry); PHOSPHOTRANSFERASES; RADIOLIGAND assay
- Publication
Proceedings of the Estonian Academy of Sciences, Chemistry, 2006, Vol 55, Issue 4, p179
- ISSN
1406-0124
- Publication type
Article
- DOI
10.3176/chem.2006.4.01