Function of phosphorylation sites on pyruvate dehydrogenase. |
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| Authors: | W M Teague F H Pettit S J Yeaman L J Reed |
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| Affiliation: | 1. Clayton Foundation Biochemical Institute The University of Texas at Austin, Austin, Texas 78712 USA;2. the Department of Chemistry The University of Texas at Austin, Austin, Texas 78712 USA |
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| Abstract: | Evidence is presented that dephosphorylation of the three phosphorylation sites on bovine kidney pyruvate dehydrogenase by pyruvate dehydrogenase phosphatase is random. The relative rates of dephosphorylation were in the order site 2 > site 3 > site 1. Phosphorylation site 2, and possibly site 3, function, in addition to site 1, as inactivating sites. However, the presence of phosphoryl groups at sites 2 and 3 did not significantly affect the rate of dephosphorylation at site 1 or the rate of reactivation of the enzyme by the phosphatase. The rate-limiting step in the reactivation of phosphorylated pyruvate dehydrogenase is apparently the dephosphorylation at site 1. |
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| Keywords: | ATPγS adenosine 5′-O-(γ-thio)triphosphate MOPS 2-(N-morpholinopropane sulfonate) |
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