EpsN from Bacillus subtilis 168 has UDP-2,6-dideoxy 2-acetamido 4-keto glucose aminotransferase activity in vitro

Kaundinya, Chinmayi R and Savithri, Handanahal S and Rao, Krishnamurthy K and Balaji, Petety V (2018) EpsN from Bacillus subtilis 168 has UDP-2,6-dideoxy 2-acetamido 4-keto glucose aminotransferase activity in vitro. In: GLYCOBIOLOGY, 28 (10). pp. 802-812.

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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.

Item Type:	Journal Article
Publication:	GLYCOBIOLOGY
Publisher:	OXFORD UNIV PRESS INC
Additional Information:	Copyright of this article belongs to OXFORD UNIV PRESS INC
Keywords:	deoxyaminosugars; eps operon; nucleotide sugar pyridoxal 5 `-phosphate dependent aminotransferase (SATs); N,N `-diacetylbacillosamine biosynthetic pathway enzyme
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	24 Jan 2019 10:15
Last Modified:	25 Aug 2022 10:47
URI:	https://eprints.iisc.ac.in/id/eprint/61404

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