A precise swaying map for how promiscuous cellobiose-2-epimerase operate bi-reaction.

Cellobiose / chemistry Racemases and Epimerases Catalysis Substrate Specificity
Cellobiose 2-epimerase Cis-enediol intermediate Promiscuous enzyme

Journal

International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578

Informations de publication

Date de publication:
31 Dec 2023
Historique:
received: 09 08 2023
revised: 24 09 2023
accepted: 24 09 2023
medline: 29 11 2023
pubmed: 28 9 2023
entrez: 27 9 2023
Statut: ppublish

Résumé

Promiscuous enzymes play a crucial role in organism survival and new reaction mining. However, comprehensive mapping of the catalytic and regulatory mechanisms hasn't been well studied due to the characteristic complexity. The cellobiose 2-epimerase from Caldicellulosiruptor saccharolyticus (CsCE) with complex epimerization and isomerization was chosen to comprehensively investigate the promiscuous mechanisms. Here, the catalytic frame of ring-opening, cis-enediol mediated catalysis and ring-closing was firstly determined. To map the full view of promiscuous CE, the structure of CsCE complex with the isomerized product glucopyranosyl-β1,4-fructose was determined. Combined with computational calculation, the promiscuity was proved a precise cooperation of the double subsites, loop rearrangement, and intermediate swaying. The flexible loop was like a gear, whose structural reshaping regulates the sway of the intermediates between the two subsites of H377-H188 and H377-H247, and thus regulates the catalytic directions. The different protonated states of cis-enediol intermediate catalyzed by H188 were the key point for the catalysis. The promiscuous enzyme tends to utilize all elements at hand to carry out the promiscuous functions.

Identifiants

DOI: 10.1016/j.ijbiomac.2023.127093 PMID: 37758108
pubmed: 37758108
pii: S0141-8130(23)03990-9
doi: 10.1016/j.ijbiomac.2023.127093
pii:
doi:

Substances chimiques

Cellobiose 16462-44-5
Racemases and Epimerases EC 5.1.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

127093

Informations de copyright

Copyright © 2023. Published by Elsevier B.V.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare no conflict of interest.

Auteurs

Yinghui Feng (Y)

Shanghai Engineering Research Center of Molecular Therapeutics & New Drug Development, School of Chemistry and Molecular Engineering, East China Normal University, Shanghai 200062, China; State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, 214122 Wuxi, China.

Xiaomei Lyu (X)

State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, 214122 Wuxi, China; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Jiangnan University, Wuxi, Jiangsu 214122, China.

Yalong Cong (Y)

Shanghai Engineering Research Center of Molecular Therapeutics & New Drug Development, School of Chemistry and Molecular Engineering, East China Normal University, Shanghai 200062, China.

Tingwei Miao (T)

Shanghai Engineering Research Center of Molecular Therapeutics & New Drug Development, School of Chemistry and Molecular Engineering, East China Normal University, Shanghai 200062, China.

Bohuan Fang (B)

Department of Micro/Nano Electronics, School of Electronic Information and Electrical Engineering, Shanghai Jiao Tong University, Shanghai 200240, China.

Chuanxi Zhang (C)

Department of Micro/Nano Electronics, School of Electronic Information and Electrical Engineering, Shanghai Jiao Tong University, Shanghai 200240, China.

Qiang Shen (Q)

Shanghai Engineering Research Center of Molecular Therapeutics & New Drug Development, School of Chemistry and Molecular Engineering, East China Normal University, Shanghai 200062, China.

Melissa Matthews (M)

Okinawa Institute of Science and Technology, Onna, Okinawa 904-0495, Japan; Department of Chemistry, University of California Davis, Davis, CA 95616, United States; Department of Molecular and Cellular Biology, University of California Davis, Davis, CA 95616, United States.

Andrew J Fisher (AJ)

Department of Chemistry, University of California Davis, Davis, CA 95616, United States; Department of Molecular and Cellular Biology, University of California Davis, Davis, CA 95616, United States.

John Z H Zhang (JZH)

Shanghai Engineering Research Center of Molecular Therapeutics & New Drug Development, School of Chemistry and Molecular Engineering, East China Normal University, Shanghai 200062, China; NYU-ECNU Center for Computational Chemistry at NYU Shanghai, Shanghai 200062, China; Department of Chemistry, New York University, New York, NY 10003, United States.

Lujia Zhang (L)

Shanghai Engineering Research Center of Molecular Therapeutics & New Drug Development, School of Chemistry and Molecular Engineering, East China Normal University, Shanghai 200062, China; NYU-ECNU Center for Computational Chemistry at NYU Shanghai, Shanghai 200062, China. Electronic address: Ljzhang@chem.ecnu.edu.cn.

Ruijin Yang (R)

State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, 214122 Wuxi, China; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Jiangnan University, Wuxi, Jiangsu 214122, China. Electronic address: yrj@jiangnan.edu.cn.

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Classifications MeSH

questionsmedicales.fr › Glucides › Sucres › Diholoside › Cellobiose › A precise swaying map for how promiscuous...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Isomerases › Racémases et épimérases › A precise swaying map for how promiscuous...
questionsmedicales.fr › Phénomènes chimiques › Catalyse › A precise swaying map for how promiscuous...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Spécificité du substrat › A precise swaying map for how promiscuous...