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Moenomycin-Mediated Affinity Purification of Penicillin-Binding Protein 1b
- Source :
- ChemBioChem. 3:332-340
- Publication Year :
- 2002
- Publisher :
- Wiley, 2002.
-
Abstract
- The antibiotic moenomycin A inhibits the biosynthesis of peptidoglycan, the main structural polymer of the bacterial cell wall. The inhibition is based on a reversible binding of the antibiotic to one of the substrate binding sites at enzymes such as the penicillin binding protein 1b (PBP 1b). This binding has been employed to isolate PBP 1b by affinity chromatography. Suitable ligands have been prepared from moenomycin A and coupled both to affinity supports and to surface plasmon resonance sensor surfaces. The reactions that take place upon immobilization of the ligands to the affinity support and the sensor surface, respectively, have been studied in detail. With the help of surface plasmon resonance the optimal conditions for binding of PBP 1b to moenomycin-derivated ligands have been established. For the first time the selective binding of the moenomycin sugar moiety to the enzyme has been demonstrated.
- Subjects :
- Penicillin binding proteins
Peptidyl transferase
Stereochemistry
Plasma protein binding
Muramoylpentapeptide Carboxypeptidase
Biochemistry
Chromatography, Affinity
chemistry.chemical_compound
Bacterial Proteins
Affinity chromatography
Multienzyme Complexes
Escherichia coli
Penicillin-Binding Proteins
Binding site
Surface plasmon resonance
Molecular Biology
Chromatography, High Pressure Liquid
chemistry.chemical_classification
biology
Organic Chemistry
Membrane Proteins
Bambermycins
Enzyme
Hexosyltransferases
chemistry
Peptidyl Transferases
biology.protein
Molecular Medicine
Peptidoglycan
Carrier Proteins
Protein Binding
Subjects
Details
- ISSN :
- 14397633 and 14394227
- Volume :
- 3
- Database :
- OpenAIRE
- Journal :
- ChemBioChem
- Accession number :
- edsair.doi.dedup.....2fda5c6550ae08012dbc53bb416ab594