Biology:Quorum-quenching N-acyl-homoserine lactonase

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Quorum-quenching N-acyl-homoserine lactonase
Identifiers
EC number3.1.1.81
CAS number389867-43-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Quorum-quenching N-acyl-homoserine lactonase (EC 3.1.1.81, acyl homoserine degrading enzyme, acyl-homoserine lactone acylase, AHL lactonase, AHL-degrading enzyme, AHL-inactivating enzyme, AHLase, AhlD, AhlK, AiiA, AiiA lactonase, AiiA-like protein, AiiB, AiiC, AttM, delactonase, lactonase-like enzyme, N-acyl homoserine lactonase, N-acyl homoserine lactone hydrolase, N-acyl-homoserine lactone lactonase, N-acyl-L-homoserine lactone hydrolase, quorum-quenching lactonase, quorum-quenching N-acyl homoserine lactone hydrolase) is an enzyme with systematic name N-acyl-L-homoserine-lactone lactonohydrolase.[1][2][3][4][5][6][7][8][9][10][11] This enzyme catalyses the following chemical reaction

an N-acyl-L-homoserine lactone + H2O [math]\displaystyle{ \rightleftharpoons }[/math] an N-acyl-L-homoserine

Acyl-homoserine lactones are produced by numerous bacterial species. They use them to regulate the expression of virulence genes within their quorum-sensing process.

References

  1. "The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein". Biochemistry 44 (20): 7559–69. May 2005. doi:10.1021/bi050050m. PMID 15895999. 
  2. "Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species". Applied and Environmental Microbiology 68 (4): 1754–9. April 2002. doi:10.1128/AEM.68.4.1754-1759.2002. PMID 11916693. 
  3. "Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)". The Journal of Biological Chemistry 279 (14): 13645–51. April 2004. doi:10.1074/jbc.M311194200. PMID 14734559. 
  4. "AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora". Proceedings of the National Academy of Sciences of the United States of America 97 (7): 3526–31. March 2000. doi:10.1073/pnas.060023897. PMID 10716724. 
  5. "Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase". Nature 411 (6839): 813–7. June 2001. doi:10.1038/35081101. PMID 11459062. 
  6. "Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis". Applied and Environmental Microbiology 68 (8): 3919–24. August 2002. doi:10.1128/aem.68.8.3919-3924.2002. PMID 12147491. 
  7. "AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted homologues in other bacteria". Microbiology 149 (Pt 6): 1541–50. June 2003. doi:10.1099/mic.0.26269-0. PMID 12777494. 
  8. "Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis". Applied and Environmental Microbiology 70 (10): 6173–80. October 2004. doi:10.1128/AEM.70.10.6173-6180.2004. PMID 15466564. 
  9. "The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase". Proceedings of the National Academy of Sciences of the United States of America 102 (49): 17606–11. December 2005. doi:10.1073/pnas.0504996102. PMID 16314577. 
  10. "Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis". Proceedings of the National Academy of Sciences of the United States of America 102 (33): 11882–7. August 2005. doi:10.1073/pnas.0505255102. PMID 16087890. 
  11. "Quorum quenching enzyme activity is widely conserved in the sera of mammalian species". FEBS Letters 579 (17): 3713–7. July 2005. doi:10.1016/j.febslet.2005.05.060. PMID 15963993. 

External links