|Kaundinya CR, Savithri HS, Rao KK, Balaji PV
|EpsN from Bacillus subtilis 168 has UDP 2,6-dideoxy 2-acetamido 4-keto glucose aminotransferase activity in vitro
| doi: 10.1093/glycob/cwy063
|The gene epsN of Bacillus subtilis 168 was cloned and overexpressed in E. coli. Purified recombinant EpsN is shown to be a PLP-dependent aminotransferase by absorption spectroscopy, L-cycloserine inhibition and reverse phase HPLC studies. EpsN catalyses 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.