De novo biosynthesis of 1,5-diamino-2-hydroxypentane from glucose via combination of fermentation and whole-cell catalysis

1,5-Diamino-2-hydroxypentane (2-OH-PDA) is a novel aliphatic β-amino alcohol with potential for a wide range of applications, and its efficient and green synthesis has attracted increasing attention. In this study, we developed a biosynthetic pathway for 2-OH-PDA from glucose. Firstly, the Fe<sup>2+</sup>/α-ketoglutarate (α-KG)-dependent l-Lysine-3-hydroxylase (K3H) was heterologously expressed in <i>E coli</i> NT1003 capable of highly producing l-lysine to construct a biosynthetic pathway strain of 3-hydroxylysine (3-OH-lysine). By intensifying the pathway, introducing a glutamate oxidation system, and optimizing the fermentation conditions, 40.2 g/L 3-OH-lysine were achieved in the fed-batch fermentation. Then, lysine decarboxylase (SpLDC) was used to catalyze the decarboxylation of 3-OH-lysine to 2-OH-PDA, yielding 29.2 g/L with a molar conversion efficiency of 99.7%. This study provides an economical, efficient and green route for the biosynthesis of 2-OH-PDA.

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Publication Details

Journal
Synthetic and Systems Biotechnology
Published
2026-02-14
DOI
https://doi.org/10.1016/j.synbio.2026.01.036
Primary Topic
Enzyme Structure and Function
Type
article
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article

De novo biosynthesis of 1,5-diamino-2-hydroxypentane from glucose via combination of fermentation and whole-cell catalysis

Alei Zhang, Tian Tang, Shewei Hu, Qian Xu et al.
Synthetic and Systems Biotechnology
Enzyme Structure and Function
article

De novo biosynthesis of 1,5-diamino-2-hydroxypentane from glucose via combination of fermentation and whole-cell catalysis

Alei Zhang, Tian Tang, Shewei Hu, Qian Xu, H. Turan Durgunog ̆lu, Feifei Chen, Wei Liu, Chaoqiang Wu, Kequan Chen, Zhijie Zheng, Zhongliang Chen, Zixun Yang
article en

Abstract

1,5-Diamino-2-hydroxypentane (2-OH-PDA) is a novel aliphatic β-amino alcohol with potential for a wide range of applications, and its efficient and green synthesis has attracted increasing attention. In this study, we developed a biosynthetic pathway for 2-OH-PDA from glucose. Firstly, the Fe<sup>2+</sup>/α-ketoglutarate (α-KG)-dependent l-Lysine-3-hydroxylase (K3H) was heterologously expressed in <i>E coli</i> NT1003 capable of highly producing l-lysine to construct a biosynthetic pathway strain of 3-hydroxylysine (3-OH-lysine). By intensifying the pathway, introducing a glutamate oxidation system, and optimizing the fermentation conditions, 40.2 g/L 3-OH-lysine were achieved in the fed-batch fermentation. Then, lysine decarboxylase (SpLDC) was used to catalyze the decarboxylation of 3-OH-lysine to 2-OH-PDA, yielding 29.2 g/L with a molar conversion efficiency of 99.7%. This study provides an economical, efficient and green route for the biosynthesis of 2-OH-PDA.

Synthetic and Systems BiotechnologyVol. 13
Nanjing Tech University (CN), Bozhou People's Hospital (CN)
Responsible consumption and production
Openalex Percentile: Top 57%
Enzyme Structure and Function
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