transpeptidase การใช้

• The older name is gamma-glutamyl transpeptidase ( GGTP ).
• Penicillins exert their effect by competitively inactivating the serine DD-transpeptidase catalytic site.
• Horses also occasionally show anemia and elevated Gamma-glutamyl transpeptidase ( GGT ) levels.
• Elevation in Gamma-glutamyl transpeptidase can be used as a marker for abnormalities in liver function.
• High BMI is associated with type 2 diabetes only in persons with high serum gamma-glutamyl transpeptidase.
• Beta-Iactams may form an adduct E-I * of high stability with DD-transpeptidase.
• The transpeptidase activity of sortase is taken advantage of by structural biologists to produce fusion proteins in vitro.
• This enables transpeptidase activity in the presence of beta-lactams, preventing them from inhibiting cell wall synthesis.
• Ampicillin acts as an irreversible inhibitor of the enzyme transpeptidase, which is needed by bacteria to make the cell membrane.
• Because of the interaction between penicillin and transpeptidase, this enzyme is also known as penicillin-binding protein ( PBP ).
• Here, the ?-glutamate and glycine residues in the glutathione molecule are removed by Gamma-glutamyl transpeptidase and dipeptidases.
• Purified enzymes have been shown to catalyze the following reactions : D-alanine carboxypeptidase, peptidoglycan transpeptidase, and peptidoglycan endopeptidase.
• The antibiotic penicillin irreversibly binds to and inhibits the activity of the transpeptidase enzyme by forming a highly stable penicilloyl-enzyme intermediate.
• It does this by binding to and competitively inhibiting the transpeptidase enzyme ( also known as penicillin-binding proteins ( PBPs ) ).
• The structure of the streptomyces K15 DD-transpeptidase has been studied, and consists of a single polypeptide chain organized into two domains.
• Penicillin-binding protein 4 exchanges d-amino acids into Lipid II ( and Lipid I ), acting as a transpeptidase in vitro.
• Penicillin and related beta lactams work by inhibiting DD-transpeptidase enzyme that is required by bacteria to cross link peptidoglycan to form the cell wall.
• The enzyme is classified as a DD-transpeptidase because the susceptible peptide bond of the carbonyl donor extends between two carbon atoms with the D-configuration.
• Like other cephalosporins, ceftobiprole exerts its antibacterial activity by binding to important penicillin-binding proteins and inhibiting their transpeptidase activity which is essential for the synthesis of bacterial cell walls.
• Cross-linking between amino acids in different linear amino sugar chains occurs with the help of the enzyme DD-transpeptidase and results in a 3-dimensional structure that is strong and rigid.