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...

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Detalles Bibliográficos
Autores principales: Mueller, Mario, Nidetzky, Bernd
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Research article
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

Internet

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

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