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Lipoamide Dehydrogenase Regulation in Rat Brain

Published online by Cambridge University Press:  18 September 2015

T. T. Ngo  and
A. Barbeau
T. T. Ngo
Affiliation:
Department of Neurobiology, Clinical Research Institute of Montreal
A. Barbeau*
Affiliation:
Department of Neurobiology, Clinical Research Institute of Montreal
*
Clinical Research Institute of Montreal, 110 Pine Avenue West, Montreal, Quebec, Canada H2W 1R7
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Summary:

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The Pyruvate dehydrogenase multienzyme complex (PDHC) purified from rat brain is phosphorylated in the presence of low concentrations of ATP and MgCl2. The phosphorylated PDHC is incapable of catalyzing the oxidative decarboxylation of pyruvate. In the presence of high concentrations (10 mM) of MgCl2, the phosphorylated (inactive) PDHC is converted back to the dephospho-form of PDHC which is catalytically active.

The dihydrolipoyl dehydrogenase (LAD) component, E3, of PDHC is inactivated by pyridoxal phosphate (PLP) and the PLP-inactivated LAD can be reactivated by an amino acid, taurine. These results indicate the reversible formation of Schiff base between PLP and LAD. They also provide clear evidence for the involvement of LAD (E3) in the previously reported inactivation of PDHC by PLP.

Type
Quebec Cooperative Study of Friedreich's Ataxia
Information
Canadian Journal of Neurological Sciences , Volume 5 , Issue 1 , February 1978 , pp. 105 - 109
Copyright
Copyright © Canadian Neurological Sciences Federation 1978

References

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