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Characterization of BshA, bacillithiol glycosyltransferase from Staphylococcus aureus and Bacillus subtilis
Author(s) -
Upton Heather,
Newton Gerald L.,
Gushiken Melissa,
Lo Kelly,
Holden Dhiraj,
Fahey Robert C.,
Rawat Mamta
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.02.028
Subject(s) - bacillus subtilis , biosynthesis , glycosyltransferase , biochemistry , enzyme , staphylococcus aureus , chemistry , lipid ii , recombinant dna , microbiology and biotechnology , biology , bacteria , gene , genetics
The first step during bacillithiol (BSH) biosynthesis involves the formation of N ‐acetylglucosaminylmalate from UDP‐ N ‐acetylglucosamine and l ‐malate and is catalyzed by a GT4 class glycosyltransferase enzyme (BshA). Recombinant Staphylococcus aureus and Bacillus subtilis BshA were highly specific and active with l ‐malate but the former showed low activity with d ‐glyceric acid and the latter with d ‐malate. We show that BshA is inhibited by BSH and similarly that MshA (first enzyme of mycothiol biosynthesis) is inhibited by the final product MSH.