Sandbox Reserved 429: Difference between revisions
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==Binding Interactions== | ==Binding Interactions== | ||
Penicillin binding protein binds to beta-lactam antibiotics because they are similar in chemical structure to the modular pieces that form the peptioglycan | The final stages of the synthesis of peptioglycan requires penicillin binding proteins. All bacterial cell walls are made of peptidoglycan and it is important to note that all bacterias have reactions that covalantely link the first petidoglycan between two polysaccharides. This reaction is cataylzed by transpeptidase enzymes which is inhibited by the beta-lactum. Penicillin binding protein binds to beta-lactam antibiotics because they are similar in chemical structure to the modular pieces that form the peptioglycan. | ||
. 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. | 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 dues to the drugs binding tightly to the active site and blocking the reaction. | |||
==Additional Features== | ==Additional Features== | ||
