|
type |
Journal Article |
authors |
Kaundinya CR, Savithri HS, Rao KK, Balaji PV |
title |
EpsN from Bacillus subtilis 168 has UDP 2,6-dideoxy 2-acetamido 4-keto glucose aminotransferase activity in vitro |
journal |
Glycobiology |
Activity |
2.6.1.34 |
Family |
2.6.1.34.a |
sel |
selected |
ui |
29982582 |
year |
(2018) |
volume |
28 |
number |
10 |
pages |
802-812 |
| |
keywords |
doi: 10.1093/glycob/cwy063 |
abstract |
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. |
last changed |
2019/12/04 09:59 |
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