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Serine protease (serine β-lactamase)
- Molecular classification
- Enzyme, Hydrolase, Serine Protease, Beta-Lactamase
01
Overview
Serine β-lactamases are a subclass of serine proteases that hydrolyze the β-lactam ring of beta-lactam antibiotics, conferring antibiotic resistance in bacteria. They utilize a serine residue in their active site for catalysis. They are classified into Ambler classes A, C, and D, based on sequence homology. The catalytic mechanism involves acylation and deacylation reactions. Inhibitors of serine β-lactamases are being developed to restore the efficacy of beta-lactam antibiotics. Variants of these enzymes, such as ESBLs and carbapenemases, are clinically relevant due to their expanded substrate range.
- Other names
- Serine beta-lactamaseSBLClass A beta-lactamaseClass C beta-lactamaseClass D beta-lactamasePenicillinaseCephalosporinaseOxacillinase
02
Mechanism of action
Acylation/deacylation via nucleophilic attack by serine on beta-lactam ring.
03
Biological functions
Hydrolysis of beta-lactam antibioticsDrug resistancePeptidase activity (mammalian homologs)
04
Disease associations
InfectionAntibiotic resistance
05
Safety considerations
Antibiotic resistanceTreatment failure in bacterial infections
06
Interacting drugs
Beta-lactam antibiotics (substrates)
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