The structure of a GH149 β‐(1 → 3) glucan phosphorylase reveals a new surface oligosaccharide binding site and additional domains that are absent in the disaccharide‐specific GH94 glucose‐β‐(1 → 3)‐glucose (laminaribiose) phosphorylase-Reference-Cited by-同舟云学术

The structure of a GH149 β‐(1 → 3) glucan phosphorylase reveals a new surface oligosaccharide binding site and additional domains that are absent in the disaccharide‐specific GH94 glucose‐β‐(1 → 3)‐glucose (laminaribiose) phosphorylase

Published:2019-06-06 Issue:10 Volume:87 Page:885-892
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Kuhaudomlarp Sakonwan¹^ORCID,Stevenson Clare E. M.¹,Lawson David M.¹,Field Robert A.¹^ORCID

Affiliation:

1. Department of Biological ChemistryJohn Innes Centre, Norwich Research Park Norwich UK

Funder

Biotechnology and Biological Sciences Research Council

FP7 Ideas: European Research Council

John Innes Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.25745

Reference38 articles.

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4. Characterization of Oligocellulose Synthesized by Reverse Phosphorolysis Using Different Cellodextrin Phosphorylases

5. Cellodextrin phosphorylase from Ruminiclostridium thermocellum: X-ray crystal structure and substrate specificity analysis

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