Engineering of Phosphoserine Aminotransferase Increases the Conversion of l-Homoserine to 4-Hydroxy-2-ketobutyrate in a Glycerol-Independent Pathway of 1,3-Propanediol Production from Glucose.
Sign Up to like & getrecommendations! Published in 2019 at "Biotechnology journal"
DOI: 10.1002/biot.201900003
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… read more here.
Keywords: phosphoserine aminotransferase; production; phosphoserine; glycerol independent ... See more keywords
N-terminal residues are crucial for quaternary structure and active site conformation for the phosphoserine aminotransferase from enteric human parasite E. histolytica.
Sign Up to like & getrecommendations! Published in 2019 at "International journal of biological macromolecules"
DOI: 10.1016/j.ijbiomac.2019.04.027
Abstract: Phosphoserine aminotransferase (PSAT) is a pyridoxal-5'phosphate (PLP)-dependent enzyme that catalyzes the second reversible step in the phosphoserine biosynthetic pathway producing serine. The crystal structure of E. histolytica PSAT (EhPSAT) complexed with PLP was elucidated at… read more here.
Keywords: phosphoserine aminotransferase; terminal residues; active site; site ... See more keywords