beta-lactamase
Sign in to savethumb|Core structure of penicillins (top) and [[cephalosporins (bottom). Beta-lactam ring in red.]] right|thumb|Escherichia coli bacteria on the right are sensitive to two beta-lactam antibiotics, and do not grow in the semi-circular regions surrounding antibiotics. E. coli bacteria on the left are resistant to beta-lactam antibiotics, and grow next to one antibiotic (bottom) and are less inhibited by another antibiotic (top).
Key facts
- Protein family.Symbol
- β-lactamase domain
- Protein family.Name
- Metallo-beta-lactamase
- Protein family.image
- 5evb.jpg
- Protein family.width
- 300px
- Protein family.caption
- Metallo-beta-lactamase L1 homotetramer, Stenotrophomonas
- Protein family.Pfam
- PF00753
- Protein family.Pfam_clan
- CL0381
- Protein family.InterPro
- IPR001279
- Protein family.PROSITE
- PS00146
- Protein family.SCOP
- 56601
- Protein family.PDB
- , , , , , , , , , , ,
- Enzyme.Name
- β-lactamase
- Enzyme.EC_number
- 3.5.2.6
- Enzyme.CAS_number
- 9073-60-3
- Enzyme.GO_code
- 0008800
- Enzyme.image
- Lactamase Application V.1.svg
- Enzyme.width
- 300px
- Enzyme.caption
- Action of β-lactamase and decarboxylation of the intermediate
via Wikipedia infobox
Article
40 sectionsContents
- Structure
- Mechanism of action
- Penicillinase
- Resistance in gram-negative bacteria
- Extended-spectrum beta-lactamase (ESBL)
- Types
- TEM beta-lactamases (class A)
- SHV beta-lactamases (class A)
- CTX-M beta-lactamases (class A)
- OXA beta-lactamases (class D)
- Others
- Treatment
- Inhibitor-resistant β-lactamases
- AmpC-type β-lactamases (class C)
- Carbapenemases
- IMP-type carbapenemases (metallo-β-lactamases) (class B)
- VIM (Verona integron-encoded metallo-β-lactamase) (Class B)
- OXA (oxacillinase) group of β-lactamases (class D)
- KPC (''K. pneumoniae'' carbapenemase) (class A)
- CMY (class C)
- SME (Serratia marcescens enzymes), IMI (IMIpenem-hydrolysing β-lactamase), NMC and CcrA
- NDM-1 (New Delhi metallo-β-lactamase) (class B)
- Treatment of pathogens that produce ESBL/AmpC/carbapenemases
- General overview
- According to genes
- ESBLs
- Inhibitor-resistant β-lactamases
- AmpC
- Carbapenemases
- According to species
- ''Escherichia coli'' or ''Klebsiella''
- ''Pseudomonas aeruginosa''
- Use as a pharmaceutical
- Detection
- Evolution
- Etymology
- See also
- References
- Further reading
- External links
thumb|Core structure of penicillins (top) and [[cephalosporins (bottom). Beta-lactam ring in red.]] right|thumb|Escherichia coli bacteria on the right are sensitive to two beta-lactam antibiotics, and do not grow in the semi-circular regions surrounding antibiotics. E. coli bacteria on the left are resistant to beta-lactam antibiotics, and grow next to one antibiotic (bottom) and are less inhibited by another antibiotic (top).
Beta-lactamases (β-lactamases) are enzymes () produced by bacteria that provide multi-resistance to beta-lactam antibiotics such as penicillins, cephalosporins, cephamycins, monobactams and carbapenems (ertapenem), although carbapenems are relatively resistant to beta-lactamase. Beta-lactamase provides antibiotic resistance by breaking the antibiotics' structure. These antibiotics all have a common element in their molecular structure: a four-atom ring known as a beta-lactam (β-lactam) ring. Through hydrolysis, the enzyme lactamase breaks the β-lactam ring open, deactivating the molecule's antibacterial properties.