Neisseria gonorrhoeae penicillin-binding protein 3 exhibits exceptionally high carboxypeptidase and beta-lactam binding activities. [electronic resource]
Producer: 20040408Description: 14614-25 p. digitalISSN:- 0006-2960
- Acylation
- Anti-Bacterial Agents -- chemistry
- Bacterial Proteins -- antagonists & inhibitors
- Carrier Proteins -- antagonists & inhibitors
- Cell Division -- genetics
- Cell Survival -- genetics
- Cloning, Molecular
- Drug Resistance, Microbial
- Endopeptidases -- chemistry
- Enzyme Stability
- Escherichia coli Proteins
- Gene Expression Regulation, Bacterial
- Hexosyltransferases -- antagonists & inhibitors
- Hydrogen-Ion Concentration
- Microscopy, Electron, Scanning
- Molecular Sequence Data
- Muramoylpentapeptide Carboxypeptidase -- antagonists & inhibitors
- Neisseria gonorrhoeae -- enzymology
- Penicillin-Binding Proteins
- Peptidoglycan Glycosyltransferase
- Peptidyl Transferases -- antagonists & inhibitors
- Protein Binding
- Substrate Specificity
- beta-Lactams -- chemistry
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Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
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