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- W2869092741 endingPage "812" @default.
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- W2869092741 abstract "The gene epsN of Bacillus subtilis 168 was cloned and overexpressed in Escherichia coli. Purified recombinant EpsN is shown to be a pyridoxal 5'-phosphate (PLP)-dependent aminotransferase by absorption spectroscopy, l-cycloserine inhibition and reverse phase HPLC studies. EpsN catalyzes the conversion of UDP-2,6-dideoxy 2-acetamido 4-keto glucose to UDP-2,6-dideoxy 2-acetamido 4-amino glucose. Lys190 was found by sequence comparison and site-directed mutagenesis to form Schiff base with PLP. Mutagenesis studies showed that, in addition to Lys190, Ser185, Glu164, Gly58 and Thr59 are essential for aminotransferase activity." @default.
- W2869092741 created "2018-07-19" @default.
- W2869092741 creator A5002493733 @default.
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- W2869092741 date "2018-07-27" @default.
- W2869092741 modified "2023-10-17" @default.
- W2869092741 title "EpsN from Bacillus subtilis 168 has UDP-2,6-dideoxy 2-acetamido 4-keto glucose aminotransferase activity in vitro" @default.
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- W2869092741 doi "https://doi.org/10.1093/glycob/cwy063" @default.
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