Journal
BIOCHEMICAL JOURNAL
Volume 454, Issue -, Pages 239-247Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20130415
Keywords
bacillithiol; bimane; BshB; deacetylase; N-acetylglucosamine malate; zinc hydrolase
Categories
Funding
- Multidisciplinary Research Grant from the North Carolina Biotechnology Center [M2011-MRG-1116]
- Biotechnology and Biological Sciences Research Council [BB/H013504/1]
- BBSRC [BB/H013504/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H013504/1] Funding Source: researchfish
Ask authors/readers for more resources
BshB, a key enzyme in bacillithiol biosynthesis, hydrolyses the acetyl group from N-acetylglucosamine malate to generate glucosamine malate. In Bacillus anthracis, BA1557 has been identified as the N-acetylglucosamine malate deacetylase (BshB); however, a high content of bacillithiol (similar to 70%) was still observed in the B. anthracis Delta BA1557 strain. Genomic analysis led to the proposal that another deacetylase could exhibit cross-functionality in bacillithiol biosynthesis. In the present study, BA1557, its paralogue BA3888 and orthologous Bacillus cereus enzymes BC1534 and BC3461 have been characterized for their deacetylase activity towards N-acetylglucosamine malate, thus providing biochemical evidence for this proposal. In addition, the involvement of deacetylase enzymes is also expected in bacillithiol-detoxifying pathways through formation of S-mercapturic adducts. The kinetic analysis of bacillithiol-S-bimane conjugate favours the involvement of BA3888 as the B. anthracis bacillithiol-S-conjugate amidase (Bca). The high degree of specificity of this group of enzymes for its physiological substrate, along with their similar pH-activity profile and Zn2+-dependent catalytic acid-base reaction provides further evidence for their cross-functionalities.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available