Unusual kinetic behavior predicted for α‐keto acid dehydrogenase complexes
Open Access
- 22 March 1993
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 319 (3) , 267-270
- https://doi.org/10.1016/0014-5793(93)80560-h
Abstract
A novel regulation type, which may be observed as an unusual kinetic ‘cooperativity’, is predicted for the α‐keto acid dehydrogenase complexes. The inter‐relationship of this regulation with the well‐known regulatory effect of enzyme phosphorylation is discussed.Keywords
This publication has 10 references indexed in Scilit:
- Functional analysis of the domains of dihydrolipoamide acetyltransferase from Saccharomyces cerevisiaeBiochemistry, 1991
- Molecular biology and biochemistry of pyruvate dehydrogenase complexes 1The FASEB Journal, 1990
- Change in α‐ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADHFEBS Letters, 1990
- 2‐Oxo Acid Dehydrogenase Multienzyme Complexes: Domains, Dynamics, and DesignaAnnals of the New York Academy of Sciences, 1989
- Role of protein X in the function of the mammalian pyruvate dehydrogenase complexBiochemical and Biophysical Research Communications, 1989
- The 2-oxo acid dehydrogenase complexes: recent advancesBiochemical Journal, 1989
- Hormonal regulation of 6‐phosphofructo‐2‐kinase/fructose‐2,6‐bisphosphatase: Kinetic modelsFEBS Letters, 1987
- Elementary steps in the reaction mechanism of the .alpha.-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: kinetics of succinylation and desuccinylationBiochemistry, 1984
- Cooperativity in highly aggregated enzyme systems. A slow transition model for the pyruvate dehydrogenase complex from Escherichia coli.Journal of Biological Chemistry, 1984
- Elementary steps in the reaction mechanism of pyruvate dehydrogenase multienzyme complex from Escherichia coli: kinetics of flavin reductionBiochemistry, 1981