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Protein Engineering and Dual-Module Optimization for Efficient NMN Production in E. coli.

Xu Ma1, Qiang Wang1, Kewei Chen2

  • 1Key Laboratory of Industrial Biotechnology of Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China.

Journal of Agricultural and Food Chemistry
|April 2, 2025
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel dual-module system for efficient nicotinamide mononucleotide (NMN) biosynthesis. This engineered pathway enhances NMN production using uridine and nicotinamide, offering a promising route for NAD+ supplement development.

Keywords:
ATP regeneration systemsmetabolic engineeringmultienzyme cascade synthesisprotein engineeringβ-nicotinamide mononucleotide

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Area of Science:

  • Biotechnology
  • Enzymatic Synthesis
  • Metabolic Engineering

Background:

  • Nicotinamide mononucleotide (NMN) is a crucial NAD+ precursor with significant interest as a supplement.
  • Existing NMN synthesis methods face challenges in efficiency and scalability.

Purpose of the Study:

  • To engineer a novel, efficient dual-module enzymatic system for NMN biosynthesis.
  • To enhance the stability and activity of key enzymes involved in NMN production.
  • To optimize the system for high conversion rates using readily available substrates.

Main Methods:

  • Construction of a two-module enzymatic reaction system for NMN synthesis from uridine and nicotinamide.
  • Engineering of a more stable Nicotinamide Riboside Kinase (NRK) mutant (KlmNRK_M4) through structural and evolutionary analysis.
  • Knockout of endogenous degradative enzyme genes in *Escherichia coli* to improve substrate and intermediate conversion.
  • Optimization of reaction conditions for the dual-module system.

Main Results:

  • Achieved efficient synthesis of NMN from Nicotinamide Riboside (NR) in module 1 using an NRK and ATP regeneration system.
  • Successfully synthesized NMN from uridine and nicotinamide in module 2 via synergistic catalysis of NRK and pyrimidine nucleoside phosphorylase (PyNP).
  • Obtained a highly stable KlmNRK_M4 mutant with improved enzymatic properties.
  • Attained a high NMN conversion rate of 81.1% using 300 mM uridine and nicotinamide under optimized conditions.

Conclusions:

  • The developed dual-module recombination system presents a novel and efficient pathway for NMN biosynthesis.
  • Enzyme engineering and metabolic pathway optimization significantly enhance NMN production efficiency.
  • This study provides a scalable and cost-effective approach for the industrial production of NMN.