تحميل...
Orthophosphate binding at the dimer interface of Corynebacterium callunae starch phosphorylase: mutational analysis of its role for activity and stability of the enzyme
BACKGROUND: Orthophosphate recognition at allosteric binding sites is a key feature for the regulation of enzyme activity in mammalian glycogen phosphorylases. Protein residues co-ordinating orthophosphate in three binding sites distributed across the dimer interface of a non-regulated bacterial sta...
محفوظ في:
| المؤلفون الرئيسيون: | , |
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| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
BioMed Central
2010
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| الموضوعات: | |
| الوصول للمادة أونلاين: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2837607/ https://ncbi.nlm.nih.gov/pubmed/20113461 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/1471-2091-11-8 |
| الوسوم: |
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