Scientific background: |
DLD, Dihydrolipoamide dehydrogenase, is a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acid dehydrogenase complex (BCKD). DLD is a flavoprotein enzyme that degrades lipoamide, and produces dihydrolipoamide. The DLD gene contains 14 exons. The gene is localized to 7q31-q32. This gene encodes the L protein of the mitochondrial glycine cleavage system. The L protein, also named dihydrolipoamide dehydrogenase, is also a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. |
References: |
1. Feigenbaum, A. S., Robinson, B. H.The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements.Genomics 17: 376-381, 1993.
2. Sakata, Y., Owada, Y., Sato, K., Kojima, K., Hisanaga, K., Shinka, T., Suzuki, Y., Aoki, Y., Satoh, J., Kondo, H., Matsubara, Y., Kure, S.Structure and expression of the glycine cleavage system in rat central nervous system.Molec. Brain Res. 94: 119-130, 2001.
3. Scherer, S. W., Otulakowski, G., Robinson, B. H., Tsui, L.-C.Localization of the human dihydrolipoamide dehydrogenase gene (DLD) to 7q31-q32.Cytogenet. Cell Genet. 56: 176-177, 1991.
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