Bacillus subtilis CwlQ (previous YjbJ) is a bifunctional enzyme exhibiting muramidase and soluble-lytic transglycosylase activities

► The CwlQ protein is a cell wall lytic enzyme of Bacillus subtilis. ► Amino acid sequence of CwlQ is similar to lytic transglycosylase and goose lysozyme. ► A domain of CwlQ exhibits bifunctional activities of SLT and muramidase. CwlQ (previous YjbJ) is one of the putative cell wall hydrolases in B...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2010-07, Vol.398 (3), p.606-612
Main Authors: Sudiarta, I Putu, Fukushima, Tatsuya, Sekiguchi, Junichi
Format: Article
Language:English
Subjects:
Bacillus subtilis
Bacillus subtilis - enzymology
Bifunctional domain
Catalytic Domain - genetics
Cell wall
Cloning, Molecular
Escherichia coli - genetics
Glutamic Acid - chemistry
Glutamic Acid - genetics
Glycosyltransferases - chemistry
Glycosyltransferases - genetics
Muramidase - chemistry
Muramidase - genetics
Mutagenesis, Site-Directed
Peptidoglycan hydrolase
Protein Structure, Tertiary
Site-directed mutagenesis
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Summary:► The CwlQ protein is a cell wall lytic enzyme of Bacillus subtilis. ► Amino acid sequence of CwlQ is similar to lytic transglycosylase and goose lysozyme. ► A domain of CwlQ exhibits bifunctional activities of SLT and muramidase. CwlQ (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 CwlQ was cloned and expressed in E. coli. The purified CwlQ protein exhibited cell wall hydrolytic activity. Surprisingly, RP-HPLC, mass spectrometry (MS), and MS/MS analyses showed that CwlQ produces two products, 1,6-anhydro- N-acetylmuramic acid and N-acetylmuramic acid, thus indicating that CwlQ is a bifunctional enzyme. The site-directed mutagenesis revealed that glutamic acid 85 (Glu-85) is an amino acid residue essential to both activities.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2010.07.001