Insights into the Structure–Function Relationship of GH70 GtfB α-Glucanotransferases from the Crystal Structure and Molecular Dynamic Simulation of a Newly Characterized Limosilactobacillus reuteri N1 GtfB Enzyme

Jingjing Dong, Yuxiang Bai, Qin Wang, Qiuming Chen, Xiaoxiao Li, Yanli Wang, Hangyan Ji, Xiangfeng Meng, Tjaard Pijning, Birte Svensson, Lubbert Dijkhuizen, Maher Abou Hachem*, Zhengyu Jin*

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

2 Citaten (Scopus)


α-Glucanotransferases of the CAZy family GH70 convert starch-derived donors to industrially important α-glucans. Here, we describe characteristics of a novel GtfB-type 4,6-α-glucanotransferase of high enzyme activity (60.8 U mg -1) from Limosilactobacillus reuteri N1 (LrN1 GtfB), which produces surprisingly large quantities of soluble protein in heterologous expression (173 mg pure protein per L of culture) and synthesizes the reuteran-like α-glucan with (α1 → 6) linkages in linear chains and branch points. Protein structural analysis of LrN1 GtfB revealed the potential crucial residues at subsites -2∼+2, particularly H265, Y214, and R302, in the active center as well as previously unidentified surface binding sites. Furthermore, molecular dynamic simulations have provided unprecedented insights into linkage specificity hallmarks of the enzyme. Therefore, LrN1 GtfB represents a potent enzymatic tool for starch conversion, and this study promotes our knowledge on the structure-function relationship of GH70 GtfB α-glucanotransferases, which might facilitate the production of tailored α-glucans by enzyme engineering in future.

Originele taal-2English
Pagina's (van-tot)5391-5402
Aantal pagina's12
TijdschriftJournal of Agricultural and Food Chemistry
Nummer van het tijdschrift10
Vroegere onlinedatum1-mrt.-2024
StatusPublished - 13-mrt.-2024

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