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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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| Autori principali: | , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Portland Press Ltd.
2005
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| Soggetti: | |
| Accesso online: | 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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