Increased glutarate production by blocking the glutaryl-CoA dehydrogenation pathway and a catabolic pathway involving l-2-hydroxyglutarate

Manman Zhang, Chao Gao (), Xiaoting Guo, Shiting Guo, Zhaoqi Kang, Dan Xiao, Jinxin Yan, Fei Tao, Wen Zhang, Wenyue Dong, Pan Liu, Chen Yang, Cuiqing Ma and Ping Xu ()
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Manman Zhang: Shandong University
Chao Gao: Shandong University
Xiaoting Guo: Shandong University
Shiting Guo: Shandong University
Zhaoqi Kang: Shandong University
Dan Xiao: Shandong University
Jinxin Yan: Shandong University
Fei Tao: Shanghai Jiao Tong University
Wen Zhang: The Second Hospital of Shandong University
Wenyue Dong: Chinese Academy of Sciences
Pan Liu: Shandong University
Chen Yang: Chinese Academy of Sciences
Cuiqing Ma: Shandong University
Ping Xu: Shanghai Jiao Tong University

Nature Communications, 2018, vol. 9, issue 1, 1-14

Abstract: Abstract Glutarate is a five carbon platform chemical produced during the catabolism of l-lysine. It is known that it can be catabolized through the glutaryl-CoA dehydrogenation pathway. Here, we discover that Pseudomonas putida KT2440 has an additional glutarate catabolic pathway involving l-2-hydroxyglutarate (l-2-HG), an abnormal metabolite produced from 2-ketoglutarate (2-KG). In this pathway, CsiD, a Fe2+/2-KG-dependent glutarate hydroxylase, is capable of converting glutarate into l-2-HG, and LhgO, an l-2-HG oxidase, can catalyze l-2-HG into 2-KG. We construct a recombinant strain that lacks both glutarate catabolic pathways. It can produce glutarate from l-lysine with a yield of 0.85 mol glutarate/mol l-lysine. Thus, l-2-HG anabolism and catabolism is a metabolic alternative to the glutaryl-CoA dehydrogenation pathway in P. putida KT2440; l-lysine can be both ketogenic and glucogenic.

Date: 2018
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DOI: 10.1038/s41467-018-04513-0

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