Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 398, Issue 3, Pages 606-612Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2010.07.001
Keywords
Cell wall; Peptidoglycan hydrolase; Bifunctional domain; Bacillus subtilis; Site-directed mutagenesis
Categories
Funding
- Grants-in-Aids for Scientific Research [19380047, 22248008]
- New Energy and Industrial Technology Department Organization (NEDO)
- Grant-in-Aid for Young Scientists [21780067]
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
- Grants-in-Aid for Scientific Research [22248008, 21780067, 19380047] Funding Source: KAKEN
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CwIQ (previous YjbJ) is one of the putative cell wall hydrolases in Bacillus subtilis. Its domain has an amino acid sequence similar to the soluble-lytic transglycosylase (SLT) of Escherichia coli Slt70 and also goose lysozyme (muramidase). To characterize the enzyme, the domain of CwIQ was cloned and expressed in E. coli. The purified CwIQ protein exhibited cell wall hydrolytic activity. Surprisingly, RP-HPLC, mass spectrometry (MS), and MS/MS analyses showed that CwIQ produces two products, 1,6-anhydro-N-acetylmuramic acid and N-acetylmuramic acid, thus indicating that CwIQ is a bifunctional enzyme. The site-directed mutagenesis revealed that glutamic acid 85 (Glu-85) is an amino acid residue essential to both activities. (C) 2010 Elsevier Inc. All rights reserved.
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