DD-transpeptidase
DD-transpeptidase is an enzyme that plays a crucial role in the final stages of cell wall synthesis in bacteria. It is also known as a penicillin-binding protein because it is the target of penicillin and other beta-lactam antibiotics.
Function[edit | edit source]
DD-transpeptidase catalyzes the cross-linking of the peptidoglycan layer in the bacterial cell wall, providing strength and rigidity to the cell structure. This is achieved by the formation of a peptide bond between the third amino acid of a pentapeptide and the terminal D-alanine of another pentapeptide.
Inhibition by antibiotics[edit | edit source]
Beta-lactam antibiotics, such as penicillin, inhibit the function of DD-transpeptidase. They mimic the D-alanine-D-alanine site of the peptide chain, binding to the active site of the enzyme and preventing it from cross-linking the peptidoglycan layer. This results in a weakened cell wall and eventual cell death.
Clinical significance[edit | edit source]
The inhibition of DD-transpeptidase by beta-lactam antibiotics forms the basis of their therapeutic use in the treatment of bacterial infections. However, resistance to these antibiotics can occur through the production of beta-lactamase enzymes that hydrolyze the beta-lactam ring, or through the alteration of the DD-transpeptidase enzyme itself.
See also[edit | edit source]
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