Penicillin-binding proteins

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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]].
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== References ==
== References ==
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Revision as of 12:43, 19 March 2024

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References

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