Structural elements determining the transglycosylating activity of glycoside hydrolase family 57 glycogen branching enzymes

Gang Xiang, Hans Leemhuis, Marc Jos Elise Cornelis van Der Maarel*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

4 Citations (Scopus)
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Abstract

Glycoside hydrolase family 57 glycogen branching enzymes (GH57GBE) catalyze the formation of an alpha-1,6 glycosidic bond between alpha-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 2500 gene sequences and determining the branching activity of several native and mutant GH57GBEs. A correlation was found in a very low or even no branching activity with the absence of a flexible loop, a tyrosine at the loop tip, and two beta-strands.

Original languageEnglish
Pages (from-to)155-163
Number of pages9
JournalProteins-Structure Function and Bioinformatics
Volume90
Issue number1
Early online date9-Aug-2021
DOIs
Publication statusPublished - Jan-2022

Keywords

  • amylose
  • glycogen
  • glycogen branching enzymes
  • glycoside hydrolase family 57
  • ALPHA-AMYLASE
  • METABOLISM
  • BIOSYNTHESIS
  • SUBFAMILIES

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