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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...
| Autores principales: | , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
BioMed Central
2010
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2837607/ https://www.ncbi.nlm.nih.gov/pubmed/20113461 http://dx.doi.org/10.1186/1471-2091-11-8 |