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beta-lactamase
EntityQ311379· pop 34· linked from 453 articles

beta-lactamase

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Also known as cephalosporin-beta-lactamase, beta-lactam hydrolase, ampicillinase, penicillin amido-beta-lactamhydrolase, penicillin beta-lactamase, exopenicillinase, Penicillinase

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).

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

Wikidata facts

Image
Beta-lactamase Citrobacter 3BFC.png
Show 2 more facts
Commons category
Beta-lactamase
EC enzyme number
3.5.2.6
Sources (4)

via Wikidata · CC0

~28 min read

Encyclopedic overview

40 sections
Contents
  • 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.

Excerpted from Wikipedia’s “beta-lactamase” article, available under the CC BY-SA 4.0 licence.

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