NDLI: BlaB, a protein involved in the regulation of Streptomyces cacaoi β-lactamases, is a penicillin-binding protein

Content Provider	Springer Nature Link
Author	Raskin, C. Gérard, C. Donfut, S. Giantta, F. Van Driessche, G. Van Beeumen, J. Dusart, J.
Copyright Year	2003
Abstract	Streptomyces cacaoi β-lactamase genes are controlled by two regulators named blaA and blaB. Whereas BlaA has been identified as a LysR-type activator, the function of BlaB is still unknown. Its primary structure is similar to that of the serine penicillin-recognizing enzymes (PREs). Indeed, the SXXK and KTG motifs are perfectly conserved in BlaB, whereas the common SXN element found in PREs is replaced by a SDG motif. Site-directed mutations were introduced in these motifs and they all disturb β-lactamase regulation. A water-soluble form of BlaB was also overexpressed in the Streptomyces lividans TK24 cytoplasm and purified. To elucidate the activity of BlaB, several compounds recognized by PREs were tested. BlaB could be acylated by some of them, and it can therefore be considered as a penicillin-binding protein. BlaB is devoid of β-lactamase, D-aminopeptidase, DD-carboxypeptidase or thiolesterase activity.
Starting Page	1460
Ending Page	1469
Page Count	10
File Format	PDF
ISSN	1420682X
Journal	Cellular and Molecular Life Sciences
Volume Number	60
Issue Number	7
e-ISSN	14209071
Language	English
Publisher	Birkhäuser-Verlag
Publisher Date	2003-01-01
Publisher Place	Basel
Access Restriction	Subscribed
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience

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BlaB, a protein involved in the regulation of Streptomyces cacaoi β-lactamases, is a penicillin-binding protein