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The structure of a GH149 ß-(1 → 3) glucan phosphorylase reveals a new surface oligosaccharide binding site and additional domains that are absent in the disaccharide-specific GH94 glucose-ß-(1 → 3)-glucose (laminaribiose) phosphorylase.
Kuhaudomlarp, Sakonwan; Stevenson, Clare E M; Lawson, David M; Field, Robert A.
Affiliation
  • Kuhaudomlarp S; Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, UK.
  • Stevenson CEM; Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, UK.
  • Lawson DM; Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, UK.
  • Field RA; Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, UK.
Proteins ; 87(10): 885-892, 2019 10.
Article in En | MEDLINE | ID: mdl-31134667

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Oligosaccharides / Bacterial Proteins / Beta-Glucans / Glucosyltransferases / Phosphorylases / Glycosides Language: En Journal: Proteins Journal subject: BIOQUIMICA Year: 2019 Document type: Article Affiliation country: United kingdom Country of publication: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Oligosaccharides / Bacterial Proteins / Beta-Glucans / Glucosyltransferases / Phosphorylases / Glycosides Language: En Journal: Proteins Journal subject: BIOQUIMICA Year: 2019 Document type: Article Affiliation country: United kingdom Country of publication: United States