serine-type D-Ala-D-Ala carboxypeptidase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: (Ac)2-L-Lys-D-alanyl-D-alanine + H2O = (Ac)2-L-Lys-D-alanine + D-alanine. [EC:3.4.16.4]

Serine-type D-Ala-D-Ala carboxypeptidases are a class of enzymes that cleave the terminal D-Ala-D-Ala dipeptide from peptidoglycan precursors. Peptidoglycan is a major component of bacterial cell walls, and its synthesis is essential for bacterial survival. These enzymes are involved in the final step of peptidoglycan biosynthesis, where they remove the terminal D-Ala-D-Ala dipeptide from the pentapeptide side chain of lipid-linked peptidoglycan precursors. This removal is crucial for the transpeptidation reaction that cross-links peptidoglycan strands, creating a strong and rigid cell wall. Serine-type D-Ala-D-Ala carboxypeptidases are highly specific for the D-Ala-D-Ala dipeptide and typically exhibit a preference for the pentapeptide side chain. They utilize a catalytic mechanism that involves a conserved serine residue in the active site. This serine residue acts as a nucleophile and attacks the carbonyl group of the terminal D-Ala residue in the D-Ala-D-Ala dipeptide. The resulting covalent intermediate is then hydrolyzed, releasing the D-Ala-D-Ala dipeptide and regenerating the active enzyme. Serine-type D-Ala-D-Ala carboxypeptidases play a critical role in bacterial cell wall biosynthesis and are essential for bacterial viability. They are therefore attractive targets for the development of new antibiotics. Some antibiotics, such as penicillin and vancomycin, inhibit the activity of these enzymes and have been used to treat bacterial infections. However, the emergence of antibiotic resistance is a growing concern, and the development of new drugs that target these enzymes is an ongoing area of research.'
"

Proteins (1)

Compounds (1)