Characterization of BshA, bacillithiol glycosyltransferase from Staphylococcus aureus and Bacillus subtilis

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• 作者：Heather Upton^a ; Gerald L. Newton^b ; Melissa Gushiken^a ; Kelly Lo^b ; Dhiraj Holden^a ; Robert C. Fahey^b ; Mamta Rawat^a ; ^{mrawat@csufresno.edu}
• 关键词：BSH ; bacillithiol ; MSH ; mycothiol ; UDP-GlcNAc ; UDP-N-acetyl glucosamine ; GlcNAc-Mal ; N-acetylglucosaminylmalate ; DTT ; dithiothreitol ; DTNB ; 5 ; 5&prime ; -dithiobis(2-nitrobenzoic acid) ; TCEP ; Tris(2-carboxyethyl) phosphine
• 刊名：FEBS Letters
• 出版年：2012
• 期刊代码：70_00145793
• 类别：bio
• 出版时间：5 April, 2012
• 卷：586
• 期：7
• 页码：1004-1008
• 文件大小：619 K

摘要

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.