Mammalian α-Keto Acid Dehydrogenase Complexes
It was found that the pig heart pyruvate dehydrogenase complex is capable of oxidatively decarboxylating α-ketobutyrate at about the rate of 62% of that of pyruvate in the over-all reaction assay and about 79% in the dehydrogenase assay. The complex also shows some activities with α-ketovalerate,...
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Published in | The Journal of biological chemistry Vol. 244; no. 5; p. 1183 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
American Society for Biochemistry and Molecular Biology
10.03.1969
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Online Access | Get full text |
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Summary: | It was found that the pig heart pyruvate dehydrogenase complex is capable of oxidatively decarboxylating α-ketobutyrate at
about the rate of 62% of that of pyruvate in the over-all reaction assay and about 79% in the dehydrogenase assay. The complex
also shows some activities with α-ketovalerate, α-ketoisocaproate, and α-ketocaproate. These activities were associated with
this complex throughout the purification process. The 2-oxoglutarate dehydrogenase complex is highly specific for 2-oxoglutarate,
but does also show some activity with α-ketoadipate. The pig heart pyruvate dehydrogenase complex was inhibited competitively
by α-ketoisovalerate and α-keto-β-methylvalerate with pyruvate, α-ketobutyrate, and α-ketoisocaproate. The 2-oxoglutarate
dehydrogenase complex exhibited mixed inhibition by α-ketoisovalerate, α-keto-β-methylvalerate, and α-ketoisocaproate with
2-oxoglutarate. The significances of the results relative to maple syrup disease are discussed. |
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ISSN: | 0021-9258 1083-351X |