Synthesis, purification and kinetic properties of fluorescein-labelled penicillins
- 15 May 1994
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 300 (1) , 141-145
- https://doi.org/10.1042/bj3000141
Abstract
The synthesis and properties of six fluorescein-labelled penicillins are reported. The two isomers of fluoresceyl-glycyl-6-amino-penicillanic acid are probably the best compounds to use for detection of all the penicillin-binding proteins (PBPs) present in a bacterial membrane preparation. However, the derivatives of ampicillin were much more efficient against Enterobacter aerogenes PBP3. The two isomers obtained when a commercial mixture of the two isomers of carboxyfluorescein was used most often exhibited similar properties, but the Streptomyces R61 extracellular DD-peptidase was only efficiently acylated by the 5′-carboxyfluorescein derivative of glycyl-6-aminopenicillanic acid.Keywords
This publication has 17 references indexed in Scilit:
- Penicillin binding protein 2x as a major contributor to intrinsic β‐lactam resistance of Streptococcus pneumoniaeFEBS Letters, 1993
- The pH dependence of the active‐site serine DD‐peptidase of Streptomyces R61European Journal of Biochemistry, 1987
- Penicillin-Sensitive Enzymes in Peptidoglycan BiosynthesisCRC Critical Reviews in Microbiology, 1984
- Interaction between non-classical β-lactam compounds and the Zn2+-containing G and serine R61 and R39 d-alanyl-d-alanine peptidasesBiochemical Journal, 1981
- Affinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K-12 and their antibacterial activityAntimicrobial Agents and Chemotherapy, 1979
- Properties of the Penicillin‐Binding Proteins of Escherichia coli K12European Journal of Biochemistry, 1977
- Kinetics of Interaction between the Exocellular DD‐Carboxypeptidase‐Transpeptidase from Streptomyces R61 and β‐Lactam AntibioticsEuropean Journal of Biochemistry, 1975
- Interaction between β‐Lactam Antibiotics and Exocellular dd‐Carboxypeptidase‐Transpeptidase of Streptomyces R61European Journal of Biochemistry, 1974
- Molecular weight, amino acid composition and physicochemical properties of the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R39Biochemical Journal, 1974
- Fluorescence and circular-dichroism studies on the Streptomyces R61 dd-carboxypeptidase–transpeptidase. Penicillin binding by the enzymeBiochemical Journal, 1973