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The oxidation of 4-methyl-2-oxopentanoate (alpha-ketoisocaproate) by rat liver mitochondria was shown to be independent of exogenous coenzyme A and exogenous NAD+. Carnitine stimulated the oxidation of 4-methyl-2-oxopentanoate in rat liver homogenates and mitochondria; octanoate, DL-octanoylcarnitine, 4-pentenoate, and 3-methylbutyrate (isovalerate) were inhibitory, and 2-bromopalmitate had no effect. Addition of carnitine was found to increase the export from the mitochondria of acylcarnitines derived from 4-methyl-2-oxopentanoate in the presence of absence of 4-pentenoate but not in the presence of octanoylcarnitine. It is concluded that the branched chain oxoacid dehydrogenase is localized on the inner surface of the inner mitochondrial membrane and that it is regulated in part by the intramitochondrial levels of branched chain fatty acyl-CoA esters and/or free CoA.
M E May, and
R P Aftring, and
M G Buse
May 1978,
The American journal of physiology,
M E May, and
R P Aftring, and
M G Buse
October 1986,
Biochimica et biophysica acta,
M E May, and
R P Aftring, and
M G Buse
November 1984,
The Journal of nutrition,
M E May, and
R P Aftring, and
M G Buse
March 1967,
Biochimica et biophysica acta,
M E May, and
R P Aftring, and
M G Buse
April 1981,
FEBS letters,
M E May, and
R P Aftring, and
M G Buse
November 1986,
Journal of biochemistry,
M E May, and
R P Aftring, and
M G Buse
July 1982,
FEBS letters,
M E May, and
R P Aftring, and
M G Buse
October 1982,
FEBS letters,
M E May, and
R P Aftring, and
M G Buse
September 1988,
European journal of biochemistry,
M E May, and
R P Aftring, and
M G Buse
March 2024,
Journal of hazardous materials,
