Back to Search
Start Over
Complete ¹H, ¹⁵N, and ¹³C resonance assignments of Bacillus cereus metallo-β-lactamase and its complex with the inhibitor R-thiomandelic acid.
- Source :
-
Biomolecular NMR assignments [Biomol NMR Assign] 2014 Oct; Vol. 8 (2), pp. 313-8. Date of Electronic Publication: 2013 Jul 10. - Publication Year :
- 2014
-
Abstract
- β-Lactamases inactivate β-lactam antibiotics by hydrolysis of their endocyclic β-lactam bond and are a major cause of antibiotic resistance in pathogenic bacteria. The zinc dependent metallo-β-lactamase enzymes are of particular concern since they are located on highly transmissible plasmids and have a broad spectrum of activity against almost all β-lactam antibiotics. We present here essentially complete (>96%) backbone and sidechain sequence-specific NMR resonance assignments for the Bacillus cereus subclass B1 metallo-β-lactamase, BcII, and for its complex with R-thiomandelic acid, a broad spectrum inhibitor of metallo-β-lactamases. These assignments have been used as the basis for determination of the solution structures of the enzyme and its inhibitor complex and can also be used in a rapid screen for other metallo-β-lactamase inhibitors.
- Subjects :
- beta-Lactamase Inhibitors metabolism
beta-Lactamase Inhibitors pharmacology
Bacillus cereus enzymology
Mandelic Acids metabolism
Mandelic Acids pharmacology
Nuclear Magnetic Resonance, Biomolecular
Sulfhydryl Compounds metabolism
Sulfhydryl Compounds pharmacology
beta-Lactamases chemistry
beta-Lactamases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1874-270X
- Volume :
- 8
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biomolecular NMR assignments
- Publication Type :
- Academic Journal
- Accession number :
- 23838816
- Full Text :
- https://doi.org/10.1007/s12104-013-9507-1