dd-Carboxypeptidases (dd-CPases) are low-molecular-mass (LMM) penicillin-binding
proteins (PBPs) that are mainly involved in peptidoglycan remodelling, but little is known …

The biological roles of low molecular weight penicillin‐binding proteins (LMW PBP) have
been difficult to discern in G ram‐negative organisms. In E scherichia coli, mutants lacking …

Escherichia coli PBP5, PBP6 and DacD, encoded by dacA, dacC and dacD, respectively,
share substantial amino acid identity and together constitute~ 50% of the total penicillin …

The bacterial dd-peptidases or penicillin-binding proteins (PBPs) catalyze the formation and
regulation of cross-links in peptidoglycan biosynthesis. They are classified into two groups …

Of the five dd-carboxypeptidases in Escherichia coli, only PBP5 demonstrates its
physiological significance by maintaining cell shape and intrinsic beta-lactam resistance …

Escherichia coli PBP5, a DD-carboxypeptidase (DD-CPase), helps in maintaining cell shape
and intrinsic β-lactam resistance. Though PBP5 does not have β-lactamase activity under …

With the growing threat of drug-resistant Acinetobacter baumannii, there is an urgent need to
comprehensively understand the physiology of this nosocomial pathogen. As penicillin …

Mycobacterial peptidoglycan (PG) is an unsolved puzzle due to its complex structure and
involvement of multiple enzymes in the process of its remodelling. dd-Carboxypeptidases …

The protonation states of the two active‐site lysines (Lys69 and Lys235) of PBP 6 of
Escherichia coli were explored to understand the active site chemistry of this enzyme. Each …

With the growing threat of drug-resistant Acinetobacter baumannii, there is an urgent need to
comprehensively understand the physiology of this nosocomial pathogen. As penicillin …