1. Characterization of BshA, bacillithiol glycosyltransferase from Staphylococcus aureus and Bacillus subtilis
- Author
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Heather Upton, Mamta Rawat, Kelly Lo, Dhiraj Holden, Robert C. Fahey, Gerald L. Newton, and Melissa Gushiken
- Subjects
Models, Molecular ,Protein Conformation ,Malates ,Bacillithiol ,Bacillus subtilis ,medicine.disease_cause ,01 natural sciences ,Biochemistry ,Antioxidants ,Substrate Specificity ,chemistry.chemical_compound ,Structural Biology ,Molecular Targeted Therapy ,Enzyme Inhibitors ,chemistry.chemical_classification ,Glucosamine ,0303 health sciences ,Uridine Diphosphate N-Acetylglucosamine ,biology ,Glycopeptides ,Staphylococcal Infections ,Recombinant Proteins ,Uridine diphosphate N-acetylglucosamine ,Staphylococcus aureus ,Thiol ,Biophysics ,Bacillaceae Infections ,N-Acetylglucosaminyltransferases ,Mycothiol ,010402 general chemistry ,Article ,Microbiology ,03 medical and health sciences ,Bacterial Proteins ,Biosynthesis ,Glycosyltransferase ,Genetics ,medicine ,Cysteine ,Molecular Biology ,030304 developmental biology ,Mycobacteria ,Cell Biology ,biology.organism_classification ,0104 chemical sciences ,Molecular Weight ,Kinetics ,Enzyme ,chemistry ,biology.protein ,Inositol - Abstract
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.
- Published
- 2012
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