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Structural elements determining the transglycosylating activity of glycoside hydrolase family 57 glycogen branching enzymes
  • Gang Xiang,
  • Hans Leemhuis,
  • Marc van der Maarel
Gang Xiang
University of Groningen

Corresponding Author:[email protected]

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Hans Leemhuis
Avebe Group
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Marc van der Maarel
University of Groningen
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Glycoside hydrolase family 57 glycogen branching enzymes (GH57GBE) catalyze the formation of an α-1,6 glycosidic bond between α-1,4 linked glucooliogosaccharides. As an atypical family, a limited number of GH57GBEs have been biochemically characterized so far. This study aimed at acquiring a better understanding of the GH57GBE family by a systematic sequence-based bioinformatics analysis of almost 2,500 gene sequences and determining the branching activity of several native and mutant GH57GBEs. A correlation was found between a very low or even no branching activity with the absence of a flexible loop, a tyrosine at the loop tip, and two β-sheets.
03 May 2021Submitted to PROTEINS: Structure, Function, and Bioinformatics
04 May 2021Submission Checks Completed
04 May 2021Assigned to Editor
04 May 2021Reviewer(s) Assigned
05 Jul 2021Review(s) Completed, Editorial Evaluation Pending
11 Jul 2021Editorial Decision: Revise Minor
22 Jul 20211st Revision Received
23 Jul 2021Submission Checks Completed
23 Jul 2021Assigned to Editor
24 Jul 2021Review(s) Completed, Editorial Evaluation Pending
25 Jul 2021Editorial Decision: Accept
09 Aug 2021Published in Proteins: Structure, Function, and Bioinformatics. 10.1002/prot.26200