Glutamate dehydrogenase in disrupted mitochondrial preparations is activated by L-leucine to a much greater extent than is the purified enzyme. A factor, or factors, responsible for modulating the sensitivity of L-leucine is lost during the purification of the enzyme. Although both cardiolipin and phosphatidylserine are inhibitors of the enzyme, only the inhibition by the former phospholipid is reversed by L-leucine. The inhibition of glutamate dehydrogenase by its binding to cardiolipin in the disrupted mitochondrial preparations and its relief by L-leucine could account for the greater sensitivity of such preparations to activation by that amino acid.
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Research Article| August 01 1989
The effects of phospholipids on the activation of glutamate dehydrogenase by l-leucine
I Couée ;
Biochem J (1989) 261 (3): 921–925.
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I Couée, K F Tipton; The effects of phospholipids on the activation of glutamate dehydrogenase by l-leucine. Biochem J 1 August 1989; 261 (3): 921–925. doi: https://doi.org/10.1042/bj2610921
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