ADP-ribose is a competitive inhibitor of methanol dehydrogenases from Bacillus methanolicus.

Bao-Di Ma, Jia-Yi Li, Jian-He Xu, Tao Yu, Xu-Dong Kong

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Article in The Journal of biological chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

Identification of overoxidizing and non-overoxidizing NAD-dependent methanol dehydrogenases and implications for synthetic methylotrophy.Nature communications · 2025
Article

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5 · Who and what money

Authors and funding

5 authors.

Bao-Di MaState Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, and Zhangjiang Institute for Advanced Study, Shanghai Jiao Tong University, Shanghai, China; School of Chemical and Environmental Engineering, Shanghai Institute of Technology, Shanghai, China.

Jia-Yi LiState Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, and Zhangjiang Institute for Advanced Study, Shanghai Jiao Tong University, Shanghai, China; State Key Laboratory of Bioreactor Engineering, Shanghai Collaborative Innovation Center for Biomanufacturing, East China University of Science and Technology, Shanghai, China.

Jian-He XuState Key Laboratory of Bioreactor Engineering, Shanghai Collaborative Innovation Center for Biomanufacturing, East China University of Science and Technology, Shanghai, China.

Tao YuShenzhen Key Laboratory for the Intelligent Microbial Manufacturing of Medicines, Key Laboratory of Quantitative Synthetic Biology, Center for Synthetic Biochemistry, Shenzhen Institute of Synthetic Biology, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen, China.

Xu-Dong KongState Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, and Zhangjiang Institute for Advanced Study, Shanghai Jiao Tong University, Shanghai, China. Electronic address: xudong.kong@sjtu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methanol dehydrogenase (MDH), a representative of Type III alcohol dehydrogenases (ADHs), plays a pivotal role in methanol assimilation pathways, making it a key enzyme for the biosynthesis of chemicals and fuels from one-carbon feedstocks. An activator protein belonging to the Nudix hydrolase family, ACT, was found to increase the activity of MDH by 40-fold. Despite the widespread observation of this in vitro activation phenomenon in pairs of type III alcohol dehydrogenases and Nudix hydrolases, the mechanistic details have remained unresolved for decades. Here, we uncover a regulation mechanism in which MDH activation arises from the hydrolytic removal of ADP-ribose (ADPR), a potent inhibitor derived from NAD

Indexed as

Adenosine Diphosphate RiboseAlcohol OxidoreductasesBacillusBacterial ProteinsEnzyme InhibitorsCrystallography, X-RayKineticsMethanolAdenosine Diphosphate Ribosealcohol dehydrogenase (acceptor)Alcohol OxidoreductasesBacterial ProteinsEnzyme InhibitorsMethanolactivation mechanismactivator proteinADP-ribosemethanol dehydrogenaseNAD(+) hydrolysis

Identifiers

PMID40818608

DOI10.1016/j.jbc.2025.110599

PMCPMC12926040

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.