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alpha-1,4-D-glucan phosphorylase of gram-positive Corynebacterium callunae: isolation, biochemical properties and molecular shape of the enzyme from solution X-ray scattering.

The alpha-1,4-D-glucan phosphorylase from gram-positive Corynebacterium callunae has been isolated and characterized. The enzyme is inducible approx. 2-fold by maltose, but remarkably not repressed by D-glucose. The phosphorylase is a homodimer with a stoichiometric content of the cofactor pyridoxal...

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Autori principali: Weinhäusel, A, Griessler, R, Krebs, A, Zipper, P, Haltrich, D, Kulbe, K D, Nidetzky, B
Natura: Artigo
Lingua:Inglês
Pubblicazione: 1997
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC1218732/
https://ncbi.nlm.nih.gov/pubmed/9307027
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