D ALANYL D ALANINE CLEAVING TRANSPEPTIDASE Meaning and
Definition
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D-Alanyl D-Alanine Cleaving Transpeptidase, also known as penicillin-binding protein (PBP), is an enzyme involved in bacterial cell wall synthesis and maintenance. It is primarily found in Gram-positive bacteria, but certain Gram-negative bacteria also possess homologous proteins. This enzyme plays a crucial role in the final steps of peptidoglycan synthesis, which is essential for the structural integrity and shape of bacterial cells.
D-Alanyl D-Alanine Cleaving Transpeptidase facilitates the cross-linking of the peptide side chains in the peptidoglycan layer of the bacterial cell wall. It catalyzes the formation of covalent bonds between adjacent peptide chains, creating a strong and rigid mesh-like structure. This process is known as transpeptidation or cross-linking reaction.
The mechanism of action involves the active site of the enzyme binding to the D-Alanine-D-Alanine terminus of the peptide chain. This binding inhibits the dissociation of the enzyme and prevents the completion of the cross-linking reaction. Antibiotics like penicillin and cephalosporin target D-Alanyl D-Alanine Cleaving Transpeptidase by binding irreversibly to the active site, thereby inhibiting its function.
By disrupting the function of this enzyme, antibiotics inhibit peptidoglycan synthesis, weaken the cell wall structure, and ultimately lead to cell lysis and bacterial death. This makes D-Alanyl D-Alanine Cleaving Transpeptidase a significant target for antibacterial therapy, and its inhibition forms the basis for the mode of action of many clinically important antibiotics.
Common Misspellings for D ALANYL D ALANINE CLEAVING TRANSPEPTIDASE
- s alanyl d alanine cleaving transpeptidase
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- d alwnyl d alanine cleaving transpeptidase
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- d alabyl d alanine cleaving transpeptidase
- d alamyl d alanine cleaving transpeptidase
- d alajyl d alanine cleaving transpeptidase
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