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Novel Xylose Dehydrogenase in the Halophilic Archaeon Haloarcula marismortui

During growth of the halophilic archaeon Haloarcula marismortui on d-xylose, a specific d-xylose dehydrogenase was induced. The enzyme was purified to homogeneity. It constitutes a homotetramer of about 175 kDa and catalyzed the oxidation of xylose with both NADP(+) and NAD(+) as cosubstrates with 1...

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Библиографические подробности
Главные авторы: Johnsen, Ulrike, Schönheit, Peter
Формат: Artigo
Язык:Inglês
Опубликовано: American Society for Microbiology 2004
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Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC515137/
https://ncbi.nlm.nih.gov/pubmed/15342590
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JB.186.18.6198-6207.2004
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