Thioredoxin elicits a new dihydrolipoamide dehydrogenase activity by interaction with the electron-transferring flavoprotein in Clostridium litoralis and Eubacterium acidaminophilum.

The glycine-utilizing bacterium Clostridium litoralis contained two enzyme systems for oxidizing dihydrolipoamide. The first one was found to be a genuine dihydrolipoamide dehydrogenase, present only in low amounts. This enzyme had the typical dimeric structure with a subunit molecular mass of about...

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Veröffentlicht in:	J Bacteriol
Hauptverfasser:	Meyer, M, Dietrichs, D, Schmidt, B, Andreesen, J R
Format:	Artigo
Sprache:	Inglês
Veröffentlicht:	American Society for Microbiology (ASM) 1991
Schlagworte:	Research Article
Online-Zugang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC207289/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1995593/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.173.4.1509-1513.1991
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