Sandbox Reserved 992: Difference between revisions
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Bush, Karen. The ABCD’s of β-lactamase nomenclature. J Infect chemother. (2013) 19, 549-559.</ref> | Bush, Karen. The ABCD’s of β-lactamase nomenclature. J Infect chemother. (2013) 19, 549-559.</ref> | ||
Class C β-lactamases share a very similar mechanism as the Class A β-lactams, acylation followed by hydrolytic deacylation.4 Class C differs from A in that the hydrolytic water, activated by tyrosine 150, approaches the enzyme from the opposite side. This activated water is what allows β-lactamases to deacylation and maintain their catalytic function, while PBPs cannot.<ref name="Bush 2013" />Class D differs from A and C in that it has an N-carboxylated active site lysine which hydrogen bonds with the active site serine.<ref>Mobashery, Shahriar. Bacterial Resistance to β-Lactam Antibiotics: Compelling Opportunism, Compelling Opportunity. Chem. Rev. (2005) 105, 395-424.</ref> | |||
Class C β-lactamases share a very similar mechanism as the Class A β-lactams, acylation followed by hydrolytic deacylation.4 Class C differs from A in that the hydrolytic water, activated by tyrosine 150, approaches the enzyme from the opposite side. This activated water is what allows β-lactamases to deacylation and maintain their catalytic function, while PBPs cannot.<ref name="Bush 2013" /> Class D differs from A and C in that it has an N-carboxylated active site lysine which hydrogen bonds with the active site serine.<ref>Mobashery, Shahriar. Bacterial Resistance to β-Lactam Antibiotics: Compelling Opportunism, Compelling Opportunity. Chem. Rev. (2005) 105, 395-424.</ref> | |||
[[Image:Beta lactamase mechaism.jpg|1000px|thumb|center|Class C β-lactamase general mechanism, showing covalently bound β-lactam antibiotic in intermidiate state.]] | [[Image:Beta lactamase mechaism.jpg|1000px|thumb|center|Class C β-lactamase general mechanism, showing covalently bound β-lactam antibiotic in intermidiate state.]] |