Sandbox Reserved 429: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 34: | Line 34: | ||
. The <scene name='48/483886/betalactem/2'>beta-lactam</scene> amide bond | . The <scene name='48/483886/betalactem/2'>beta-lactam</scene> amide bond | ||
is ruptured to form a covalent bond with the catalytic serine at the binding protein's active site. When the PBP form a stable covalent complex with the beta-lactum antibiotics, the cell dies due to PBP inactivation. | is ruptured to form a covalent bond with the catalytic serine at the binding protein's active site. When the PBP form a stable covalent complex with the beta-lactum antibiotics, the cell dies due to PBP inactivation. | ||
The beta-lactum area in most drugs resemble the D-Ala-D-Ala end of peptides to which the transpeptidase enzyme binds. At the DA-DA , there is a serine 62 which is used to bind peptide strands to other stands and this is also where penicillin binds and inhibits the protein. Almost every bacteria has PBP genes but most enzymes are inhibited by the beta-lactums. The enzymes become inactive | The beta-lactum area in most drugs resemble the D-Ala-D-Ala end of peptides to which the transpeptidase enzyme binds. At the DA-DA , there is a serine 62 which is used to bind peptide strands to other stands and this is also where penicillin binds and inhibits the protein. Almost every bacteria has PBP genes but most enzymes are inhibited by the beta-lactums. The enzymes become inactive due to the drugs binding tightly to the active site and blocking the reaction. | ||
==Additional Features== | ==Additional Features== | ||