Abstract:
:In Bacillus subtilis, the yoxA and dacC genes were proposed to form an operon. The yoxA gene was overexpressed in Escherichia coli and its product fused to a polyhistidine tag was purified. An aldose-1-epimerase or mutarotase activity was measured with the YoxA protein that we propose to rename as GalM by analogy with its counterpart in E. coli. The peptide D-Glu-delta-m-A(2)pm-D-Ala-m-A(2)pm-D-Ala mimicking the B. subtilis and E. coli interpeptide bridge was synthesized and incubated with the purified dacC product, the PBP4a. A clear dd-endopeptidase activity was obtained with this penicillin-binding protein, or PBP. The possible role of this class of PBP, present in almost all bacteria, is discussed.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Duez C,Zervosen A,Teller N,Melkonian R,Banzubazé E,Bouillenne F,Luxen A,Frère JMdoi
10.1111/j.1574-6968.2009.01761.xsubject
Has Abstractpub_date
2009-11-01 00:00:00pages
42-7issue
1eissn
0378-1097issn
1574-6968pii
FML1761journal_volume
300pub_type
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