Peptidoglycan glycosyltransferase

Peptidoglycan glycosyltransferase (PGT) is a type of enzyme that plays a crucial role in the synthesis of peptidoglycan, a major component of the bacterial cell wall. This enzyme catalyzes the transfer of a glycosyl moiety from a lipid-linked oligosaccharide donor to a glycan acceptor, forming a glycosidic bond.

Function

PGT is responsible for the polymerization of the glycan strands of the peptidoglycan layer. This layer provides structural integrity to the bacterial cell wall, protecting the cell from osmotic lysis and maintaining its shape. The enzyme's activity is essential for bacterial growth and division, making it a target for antibiotic therapy.

Structure

PGTs are membrane proteins that are embedded in the bacterial cell membrane. They have a conserved domain structure, with a transmembrane domain and a large extracellular domain. The active site of the enzyme is located in the extracellular domain.

Inhibition

Given the crucial role of PGTs in bacterial cell wall synthesis, these enzymes are targets for antibiotic drugs. Inhibitors of PGTs, such as penicillin and other beta-lactam antibiotics, bind to the active site of the enzyme and prevent it from catalyzing the formation of peptidoglycan. This leads to a weakening of the bacterial cell wall and ultimately, cell death.

See also

• Peptidoglycan
• Enzyme
• Antibiotic
• Bacterial cell wall

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Peptidoglycan glycosyltransferase Resources
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