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Expression and Characterization of the Isolated Glycosyltransferase Module of Escherichia coli PBP1b
- Source :
- Biochemistry. 43:12375-12381
- Publication Year :
- 2004
- Publisher :
- American Chemical Society (ACS), 2004.
-
Abstract
- The enzymes involved in the biosynthesis of peptidoglycan are targets for the development of new antibiotics. The bifunctional high molecular weight (HMW) penicillin-binding proteins (PBPs), which contain both glycosyltransferase (GTase) and transpeptidase (TPase) activities, are particularly attractive targets because of their extracellular location. However, there is limited mechanistic or structural information about the GTase modules of these enzymes. In this paper, we describe the overexpression and characterization of the GTase module of Escherichia coli PBP1b, a paradigm of the HMW PBPs. We define the C-terminal boundary of the GTase module and show that the isolated module can be overexpressed at significantly higher levels than the full-length protein. The catalytic efficiency and other characteristics of the isolated module are comparable in most respects to the full-length enzyme. This work lays the groundwork for mechanistic and structural analysis of GTase modules.
- Subjects :
- Penicillin binding proteins
Peptidyl transferase
Detergents
Muramoylpentapeptide Carboxypeptidase
medicine.disease_cause
Biochemistry
Catalysis
Protein Structure, Secondary
chemistry.chemical_compound
Bacterial Proteins
Glycosyltransferase
Escherichia coli
medicine
Penicillin-Binding Proteins
Sequence Deletion
chemistry.chemical_classification
Peptidoglycan glycosyltransferase
Molecular Structure
biology
Escherichia coli Proteins
Glycosyltransferases
Serine-Type D-Ala-D-Ala Carboxypeptidase
Kinetics
Enzyme
Hexosyltransferases
chemistry
Metals
Peptidyl Transferases
biology.protein
Peptidoglycan Glycosyltransferase
Peptidoglycan
Carrier Proteins
Subjects
Details
- ISSN :
- 15204995 and 00062960
- Volume :
- 43
- Database :
- OpenAIRE
- Journal :
- Biochemistry
- Accession number :
- edsair.doi.dedup.....32866065d3a7de53b3d9d81b9292a2b8