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Characterization of the functional role of allosteric site residue Asp(102) in the regulatory mechanism of human mitochondrial NAD(P)(+)-dependent malate dehydrogenase (malic enzyme)

Human mitochondrial NAD(P)(+)-dependent malate dehydrogenase (decarboxylating) (malic enzyme) can be specifically and allosterically activated by fumarate. X-ray crystal structures have revealed conformational changes in the enzyme in the absence and in the presence of fumarate. Previous studies hav...

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Detaylı Bibliyografya
Asıl Yazarlar: Hung, Hui-Chih, Kuo, Meng-Wei, Chang, Gu-Gang, Liu, Guang-Yaw
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Portland Press Ltd. 2005
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC1317662/
https://ncbi.nlm.nih.gov/pubmed/15989682
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20050641
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