D-alanine—D-alanine ligase
D-alanine—D-alanine ligase (also known as D-Ala-D-Ala ligase or Ddl) is an enzyme that plays a crucial role in the bacterial cell wall synthesis. It is involved in the last step of the cytoplasmic phase of peptidoglycan biosynthesis.
Function[edit | edit source]
D-alanine—D-alanine ligase catalyzes the ATP-dependent ligation of two D-alanine molecules to form D-alanyl-D-alanine, a critical component of the peptidoglycan layer of the bacterial cell wall. This reaction involves the formation of a phosphorylated intermediate and the release of inorganic phosphate.
Structure[edit | edit source]
The enzyme is a monomer with a molecular weight of approximately 37 kDa. It consists of three domains: the N-terminal domain, the C-terminal domain, and the central domain. The active site is located in a cleft between the N-terminal and central domains.
Clinical significance[edit | edit source]
D-alanine—D-alanine ligase is a target for several antibiotics, including vancomycin and cycloserine. These antibiotics inhibit the enzyme's activity, preventing the formation of the D-alanyl-D-alanine dipeptide and thus disrupting the synthesis of the bacterial cell wall.
See also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD