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...
محفوظ في:
| الحاوية / القاعدة: | J Bacteriol |
|---|---|
| المؤلفون الرئيسيون: | , , , |
| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
American Society for Microbiology (ASM)
1991
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| الموضوعات: | |
| الوصول للمادة أونلاين: | 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 |
| الوسوم: |
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