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• W2934456286 endingPage "1900003" @default.
• W2934456286 startingPage "1900003" @default.
• W2934456286 abstract "Phosphoserine aminotransferase (SerC) from Escherichia coli (E. coli) MG1655 is engineered to catalyze the deamination of homoserine to 4-hydroxy-2-ketobutyrate, a key reaction in producing 1,3-propanediol (1,3-PDO) from glucose in a novel glycerol-independent metabolic pathway. To this end, a computation-based rational approach is used to change the substrate specificity of SerC from l-phosphoserine to l-homoserine. In this approach, molecular dynamics simulations and virtual screening are combined to predict mutation sites. The enzyme activity of the best mutant, SerCR42W/R77W , is successfully improved by 4.2-fold in comparison to the wild type when l-homoserine is used as the substrate, while its activity toward the natural substrate l-phosphoserine is completely deactivated. To validate the effects of the mutant on 1,3-PDO production, the homoserine to 1,3-PDO pathway is constructed in E. coli by coexpression of SerCR42W/R77W with pyruvate decarboxylase and alcohol dehydrogenase. The resulting mutant strain achieves the production of 3.03 g L-1 1,3-PDO in fed-batch fermentation, which is 13-fold higher than the wild-type strain and represents an important step forward to realize the promise of the glycerol-independent synthetic pathway for 1,3-PDO production from glucose." @default.
• W2934456286 created "2019-04-11" @default.
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• W2934456286 date "2019-05-28" @default.
• W2934456286 modified "2023-09-30" @default.
• W2934456286 title "Engineering of Phosphoserine Aminotransferase Increases the Conversion of<scp>l</scp>‐Homoserine to 4‐Hydroxy‐2‐ketobutyrate in a Glycerol‐Independent Pathway of 1,3‐Propanediol Production from Glucose" @default.
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• W2934456286 doi "https://doi.org/10.1002/biot.201900003" @default.
• W2934456286 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30925016" @default.
• W2934456286 hasPublicationYear "2019" @default.
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