Crystallographic mapping of β-lactams bound to a d-alanyl-d-alanine peptidase target enzyme
- 1 September 1989
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 209 (2) , 281-295
- https://doi.org/10.1016/0022-2836(89)90277-5
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Antibacterial properties of (2,3)-alpha- and (2,3)-beta-methylene analogs of penicillin GAntimicrobial Agents and Chemotherapy, 1988
- Interaction of (2,3)-methylenepenams with penicillin-binding proteinsAntimicrobial Agents and Chemotherapy, 1987
- Cephalosporins 1945-1986Drugs, 1987
- Elucidating the leaving group effect in the .beta.-lactam ring opening mechanism of cephalosporinsThe Journal of Organic Chemistry, 1985
- Elimination of a good leaving group from the 3'-position of a cephalosporin need not be concerted with .beta.-lactam ring opening: TEM-2 .beta.-lactamase-catalyzed hydrolysis of pyridine-2-azo-4'-(N',N'-dimethylaniline) cephalosporin (PADAC) and of cephaloridineJournal of the American Chemical Society, 1984
- Penicillin-Sensitive Enzymes in Peptidoglycan BiosynthesisCRC Critical Reviews in Microbiology, 1984
- Interaction between Monobactams and Streptomyces R61 dd‐CarboxypeptidaseEuropean Journal of Biochemistry, 1982
- Conformational Analysis of Peptide Substrates and Inhibitors of the Zn2+ G and Serine R61 d‐Alanyl‐d‐alanine PeptidasesEuropean Journal of Biochemistry, 1981
- The Beta-Lactam AntibioticsScientific American, 1981
- Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolutionJournal of Molecular Biology, 1981