Related Experiment Video
Updated: Jul 6, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Substrate specificity of bacterial DD-peptidases (penicillin-binding proteins)
1Department of Chemistry, Wesleyan University, Lawn Avenue, Middletown, Connecticut 06459, USA. rpratt@wesleyan.edu
Abstract:
The DD-peptidase enzymes (penicillin-binding proteins) catalyze the final transpeptidation reaction of bacterial cell wall (peptidoglycan) biosynthesis. Although there is now much structural information available about these enzymes, studies of their activity as enzymes lag. It is now established that representatives of two low-molecular-mass classes of DD-peptidases recognize elements of peptidoglycan structure and rapidly react with substrates and inhibitors incorporating these elements. No members of other DD-peptidase classes, including the high-molecular-mass enzymes, essential for bacterial growth, appear to interact strongly with any particular elements of peptidoglycan structure. Rational design of inhibitors for these enzymes is therefore challenging.
Related Concept Videos
Inhibitors of Gram-positive Cell Wall Synthesis
Production of Antibiotics
Factors Affecting Protein-Drug Binding: Drug-Related Factors
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In contrast,...
Mechanism of Antibiotic Resistance in MRSA
Inhibitors of Bacterial Protein Synthesis
Bacterial Cell Wall

