The effects of phospholipids on the activation of glutamate dehydrogenase by L-leucine. |
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Authors: | I Couée and K F Tipton |
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Affiliation: | Department of Biochemistry, Trinity College, Dublin, Ireland. |
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Abstract: | 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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