The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance. [electronic resource]
Producer: 19980831Description: 75-84 p. digitalISSN:- 1097-2765
- Alanine -- metabolism
- Amino Acid Sequence
- Animals
- Bacterial Proteins -- antagonists & inhibitors
- Binding Sites
- Carboxypeptidases -- chemistry
- Copper -- pharmacology
- Crystallography, X-Ray
- DNA Transposable Elements -- genetics
- Dipeptidases -- antagonists & inhibitors
- Dipeptides -- metabolism
- Drug Resistance, Microbial -- genetics
- Enterococcus faecium -- enzymology
- Enzyme Inhibitors -- pharmacology
- Hedgehog Proteins
- Mice
- Models, Molecular
- Molecular Sequence Data
- Organophosphorus Compounds -- pharmacology
- Propionates -- pharmacology
- Protein Conformation
- Proteins -- chemistry
- Sequence Alignment
- Sequence Homology, Amino Acid
- Serine-Type D-Ala-D-Ala Carboxypeptidase
- Structure-Activity Relationship
- Trans-Activators
- Vancomycin -- pharmacology
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Publication Type: Comparative Study; Journal Article
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