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Catalytic mechanism of α-retaining glucosyl transfer by Corynebacterium callunae starch phosphorylase: the role of histidine-334 examined through kinetic characterization of site-directed mutants

Purified site-directed mutants of Corynebacterium callunae starch phosphorylase in which His-334 was replaced by an alanine, glutamine or asparagine residue were characterized by steady-state kinetic analysis of enzymic glycosyl transfer to and from phosphate and studies of ligand binding to the act...

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Autori principali: Schwarz, Alexandra, Pierfederici, Francesco Maria, Nidetzky, Bernd
Natura: Artigo
Lingua:Inglês
Pubblicazione: Portland Press Ltd. 2005
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC1134972/
https://ncbi.nlm.nih.gov/pubmed/15535798
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20041593
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