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Ligand-induced changes in the conformational stability and flexibility of glutamate dehydrogenase and their role in catalysis and regulation
Bovine glutamate dehydrogenase (GDH) is allosterically regulated and requires substrate-induced subunit interactions for maximum catalytic activity. Steady-state and presteady-state kinetics indicate that the rate-limiting step depends on the nature of the substrate and are likely associated with co...
Tallennettuna:
| Päätekijät: | , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Wiley Subscription Services, Inc., A Wiley Company
2010
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2998718/ https://ncbi.nlm.nih.gov/pubmed/20665690 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.459 |
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