1988
DOI: 10.1007/bf01534650
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Gene for lipoamide dehydrogenase maps to human chromosome 7

Abstract: The gene for lipoamide dehydrogenase (LD) has been assigned to human chromosome 7 based on filter hybridization analysis of genomic DNA from rodent-human somatic cell hybrids using a cDNA probe for human LD. No indication of multiple copies of the gene was found, in accordance with previous evidence that LD in the pyruvate, alpha-ketoglutarate, and branched chain alpha-ketoacid dehydrogenase complexes is genetically as well as biochemically identical.

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Cited by 18 publications
(10 citation statements)
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“…Using a driven NADH regenerating system (␣-ketoglutarate dehydrogenase complex reaction) to convert and maintain lipoyl groups via the E3 reaction in the reduced form, rates of acetylation by E1 of reduced lipoyl groups using pyruvate at least 100-fold faster than the above rate obtained using the 8-thioloctanoyl-L2. 6 In both cases, O 2 presumably serves as the electron acceptor for the required oxidation of the HE-TPP to acetyl-TPP (4). Assuming that very low levels of oxidized lipoyl groups were not contributing to the higher rates with the dihydrolipoyl-containing substrate, 6 this finding suggests that the presence of a thiol in the 6-position is important for the reductive acetylation reaction to proceed even though acetylation is at the 8-position (4).…”
Section: Figmentioning
confidence: 99%
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“…Using a driven NADH regenerating system (␣-ketoglutarate dehydrogenase complex reaction) to convert and maintain lipoyl groups via the E3 reaction in the reduced form, rates of acetylation by E1 of reduced lipoyl groups using pyruvate at least 100-fold faster than the above rate obtained using the 8-thioloctanoyl-L2. 6 In both cases, O 2 presumably serves as the electron acceptor for the required oxidation of the HE-TPP to acetyl-TPP (4). Assuming that very low levels of oxidized lipoyl groups were not contributing to the higher rates with the dihydrolipoyl-containing substrate, 6 this finding suggests that the presence of a thiol in the 6-position is important for the reductive acetylation reaction to proceed even though acetylation is at the 8-position (4).…”
Section: Figmentioning
confidence: 99%
“…6 In both cases, O 2 presumably serves as the electron acceptor for the required oxidation of the HE-TPP to acetyl-TPP (4). Assuming that very low levels of oxidized lipoyl groups were not contributing to the higher rates with the dihydrolipoyl-containing substrate, 6 this finding suggests that the presence of a thiol in the 6-position is important for the reductive acetylation reaction to proceed even though acetylation is at the 8-position (4). As shown in Fig.…”
Section: Figmentioning
confidence: 99%
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“…In Saccharomyces cerevisiae (Dickinson et al, 1986) and in man, PDC and OGDC contain identical lipoamide dehydrogenases. In man this lipoamide dehydrogenase is also found in BCOADC (Otulakowski et al, 1988).…”
Section: J a E B E N E N A N D O T H E R Smentioning
confidence: 76%