Penicillin-binding proteins
From Proteopedia
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<StructureSection load='3oc2' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='3oc2' size='340' side='right' caption='Caption for this structure' scene=''> | ||
Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics (except for tabtoxinine-β-lactam, which inhibits glutamine synthetase) bind to PBPs, which are essential for bacterial cell wall synthesis. PBPs are members of a subgroup of enzymes called transpeptidases. Specifically, PBPs are DD-transpeptidases. See also [https://en.wikipedia.org/wiki/Penicillin-binding_proteins Penicillin-binding proteins]. | Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics (except for tabtoxinine-β-lactam, which inhibits glutamine synthetase) bind to PBPs, which are essential for bacterial cell wall synthesis. PBPs are members of a subgroup of enzymes called transpeptidases. Specifically, PBPs are DD-transpeptidases. See also [https://en.wikipedia.org/wiki/Penicillin-binding_proteins Penicillin-binding proteins]. | ||
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+ | See [[Sandbox 126|Penicillin-binding proteins and antibiotics]]. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 12:43, 19 March 2024
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