Unknown

Dataset Information

0

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


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.

SUBMITTER: Upton H 

PROVIDER: S-EPMC3668096 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Upton Heather H   Newton Gerald L GL   Gushiken Melissa M   Lo Kelly K   Holden Dhiraj D   Fahey Robert C RC   Rawat Mamta M  

FEBS letters 20120306 7


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 bi  ...[more]

Similar Datasets

| S-EPMC4802972 | biostudies-literature
| S-EPMC1428434 | biostudies-literature
| S-EPMC4914364 | biostudies-literature
| S-EPMC99532 | biostudies-literature
| S-EPMC6511738 | biostudies-literature
| S-EPMC3352172 | biostudies-literature
| S-EPMC3911838 | biostudies-literature
| S-EPMC4227968 | biostudies-literature
| S-EPMC4065351 | biostudies-literature
| S-EPMC5815605 | biostudies-literature