Abstract
Pseudomonas putida KT2440 is a promising chassis of industrial biotechnology due to its metabolic versatility. Butane-2,3-diol (2,3-BDO) is a precursor of numerous value-added chemicals. It is also a microbial metabolite which widely exists in various habiting environments of P. putida KT2440. It was reported that P. putida KT2440 is able to use 2,3-BDO as a sole carbon source for growth. There are three stereoisomeric forms of 2,3-BDO: (2R,3R)-2,3-BDO, meso-2,3-BDO and (2S,3S)-2,3-BDO. However, whether P. putida KT2440 can utilize three stereoisomeric forms of 2,3-BDO has not been elucidated. Here, we revealed the genomic and enzymic basis of P. putida KT2440 for dehydrogenation of different stereoisomers of 2,3-BDO into acetoin, which will be channeled to central mechanism via acetoin dehydrogenase enzyme system. (2R,3R)-2,3-BDO dehydrogenase (PP0552) was detailedly characterized and identified to participate in (2R,3R)-2,3-BDO and meso-2,3-BDO dehydrogenation. Two quinoprotein alcohol dehydrogenases, PedE (PP2674) and PedH (PP2679), were confirmed to be responsible for (2S,3S)-2,3-BDO dehydrogenation. The function redundancy and inverse regulation of PedH and PedE by lanthanide availability provides a mechanism for the adaption of P. putida KT2440 to variable environmental conditions. Elucidation of the mechanism of 2,3-BDO catabolism in P. putida KT2440 would provide new insights for bioproduction of 2,3-BDO-derived chemicals based on this robust chassis.
Highlights
Pseudomonas putida is known for its rapid growth, low nutrient demand, and adaption to various physicochemical stresses (Nikel and de Lorenzo, 2018)
The first step of 2,3BDO catabolism is its dehydrogenation to AC and three key enzymes catalyzing different stereoisomers of 2,3-BDO were identified in P. putida KT2440
The lanthanide-responsive switch of the two quinoprotein alcohol dehydrogenases was identified to lead to growth of P. putida KT2440 in (2S,3S)2,3-BDO depending on the presence or absence of lanthanides
Summary
Pseudomonas putida is known for its rapid growth, low nutrient demand, and adaption to various physicochemical stresses (Nikel and de Lorenzo, 2018). Based on the toolbox for genetic engineering of P. putida KT2440 (Poblete-Castro et al, 2020; Sun et al, 2020; Weimer et al, 2020; Zhou et al, 2020), it has been engineered for heterologous production of diverse value-added products Existence of multiple stereospecific dehydrogenases in 2,3BDO producing bacteria results in the presence of three stereoisomeric forms in natural habitats (Yang et al, 2017). The first step of 2,3BDO catabolism is its dehydrogenation to AC and three key enzymes catalyzing different stereoisomers of 2,3-BDO were identified in P. putida KT2440. The lanthanide-responsive switch of the two quinoprotein alcohol dehydrogenases was identified to lead to growth of P. putida KT2440 in (2S,3S)2,3-BDO depending on the presence or absence of lanthanides
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