Elucidation of the noncovalent interactions driving enzyme activity guides branching enzyme engineering for α-glucan modification

Zhiyou Zong (), Xuewen Zhang, Peng Chen, Zhuoyue Fu, Yan Zeng, Qian Wang, Christophe Chipot, Leila Lo Leggio and Yuanxia Sun ()
Additional contact information
Zhiyou Zong: Chinese Academy of Sciences
Xuewen Zhang: Chinese Academy of Sciences
Peng Chen: Chinese Academy of Sciences
Zhuoyue Fu: Chinese Academy of Sciences
Yan Zeng: Chinese Academy of Sciences
Qian Wang: Chinese Academy of Sciences
Christophe Chipot: UMR 7019 Université de Lorraine CNRS
Leila Lo Leggio: University of Copenhagen
Yuanxia Sun: Chinese Academy of Sciences

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: Abstract Branching enzymes (BEs) confer to α-glucans, the primary energy-storage reservoir in nature, a variety of features, like slow digestion. The full catalytic cycle of BEs can be divided in six steps, namely two covalent catalytic steps involving glycosylation and transglycosylation, and four noncatalytic steps involving substrate binding and transfers (SBTs). Despite the ever-growing wealth of biochemical and structural information on BEs, clear mechanistic insights into SBTs from an industrial-performance perspective are still missing. Here, we report a Rhodothermus profundi BE (RpBE) endowed with twice as much enzymatic activity as the Rhodothermus obamensis BE currently used in industry. Furthermore, we focus on the SBTs for RpBE by means of large-scale computations supported by experiment. Engineering of the crucial positions responsible for the initial substrate-binding step improves enzymatic activity significantly, while offering a possibility to customize product types. In addition, we show that the high-efficiency substrate-transfer steps preceding glycosylation and transglycosylation are the main reason for the remarkable enzymatic activity of RpBE, suggestive of engineering directions for the BE family.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-53018-6 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-53018-6

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-53018-6

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().