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EpsM from Bacillus subtilis 168 has UDP-2,4,6-trideoxy-2-acetamido-4-amino glucose acetyltransferase activity in vitro

Kaundinya, CR and Savithri, HS and Rao, KK and Balaji, PV (2018) EpsM from Bacillus subtilis 168 has UDP-2,4,6-trideoxy-2-acetamido-4-amino glucose acetyltransferase activity in vitro. In: Biochemical and Biophysical Research Communications, 505 (4). pp. 1057-1062.

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Official URL: https://doi.org/10.1016/j.bbrc.2018.09.185


Bacillus subtilis 168 EpsM (UniProt id P71063) has been electronically annotated as putative acetyltransferase in the UniProt database. The gene epsM was cloned and overexpressed in E. coli with an N-terminal GST tag. The purified fusion protein was shown by absorption spectroscopy, autoradiography and reverse phase HPLC to catalyse the conversion of UDP-2,4,6-trideoxy-2-acetamido-4-amino glucose to UDP-2,4,6-trideoxy-2,4-diacetamido glucose, commonly known as N,N′-diacetylbacillosamine, using acetyl coenzyme A as the donor substrate. His146 was shown by site-directed mutagenesis to be essential for acetyltransferase activity. It is hypothesized that EpsC (NAD+ dependent UDP GlcNAc 4,6-dehydratase), EpsN (PLP dependent aminotransferase) and EpsM, all of which are part of the eps operon, are involved in the biosynthesis of N,N′-diacetylbacillosamine.

Item Type: Journal Article
Publication: Biochemical and Biophysical Research Communications
Publisher: Elsevier B.V.
Additional Information: The copyright for this article belongs to the Elsevier Inc.
Keywords: acetyl coenzyme A; acyltransferase; bacterial protein; EpsM protein; UDP 2,4,6 trideoxy 2 acetamido 4 amino glucose acetyltransferase; unclassified drug; acyltransferase; bacterial protein, absorption spectroscopy; amino terminal sequence; Article; autoradiography; Bacillus subtilis; bacterial gene; catalysis; controlled study; enzyme activity; enzyme substrate complex; epsM gene; gene overexpression; in vitro study; molecular cloning; nonhuman; operon; priority journal; protein function; reversed phase high performance liquid chromatography; site directed mutagenesis; Bacillus subtilis; genetics; metabolism, Acetyltransferases; Bacillus subtilis; Bacterial Proteins
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 05 Aug 2022 05:32
Last Modified: 05 Aug 2022 05:32
URI: https://eprints.iisc.ac.in/id/eprint/75156

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