Quorum-quenching N-acyl-homoserine lactonase

Quorum-quenching N-acyl-homoserine lactonase
Identifiers
EC number 3.1.1.81
CAS number 389867-43-0
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB 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 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. Thomas, P.W.; Stone, E.M.; Costello, A.L.; Tierney, D.L.; Fast, W. (2005). "The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein". Biochemistry. 44: 7559–7569. doi:10.1021/bi050050m. PMID 15895999.
  2. Dong, Y.H.; Gusti, A.R.; Zhang, Q.; Xu, J.L.; Zhang, L.H. (2002). "Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species". Appl. Environ. Microbiol. 68: 1754–1759. doi:10.1128/AEM.68.4.1754-1759.2002. PMC 123891Freely accessible. PMID 11916693.
  3. Wang, L.H.; Weng, L.X.; Dong, Y.H.; Zhang, L.H. (2004). "Specificity and enzyme kinetics of the quorum-quenching N-acyl homoserine lactone lactonase (AHL-lactonase)". J. Biol. Chem. 279 (14): 13645–13651. doi:10.1074/jbc.M311194200. PMID 14734559.
  4. Dong, Y.H.; Xu, J.L.; Li, X.Z.; Zhang, L.H. (2000). "AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora". Proc. Natl. Acad. Sci. USA. 97 (7): 3526–3531. doi:10.1073/pnas.060023897. PMID 10716724.
  5. Dong, Y.H.; Wang, L.H.; Xu, J.L.; Zhang, H.B.; Zhang, X.F.; Zhang, L.H. (2001). "Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase". Nature. 411: 813–817. doi:10.1038/35081101. PMID 11459062.
  6. Lee, S.J.; Park, S.Y.; Lee, J.J.; Yum, D.Y.; Koo, B.T.; Lee, J.K. (2002). "Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis". Appl. Environ. Microbiol. 68 (8): 3919–3924. doi:10.1128/aem.68.8.3919-3924.2002. PMID 12147491.
  7. Park, S.Y.; Lee, S.J.; Oh, T.K.; Oh, J.W.; Koo, B.T.; Yum, D.Y.; Lee, J.K. (2003). "AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted homologues in other bacteria". Microbiology. 149 (Pt 6): 1541–1550. doi:10.1099/mic.0.26269-0. PMID 12777494.
  8. Ulrich, R.L. (2004). "Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis". Appl. Environ. Microbiol. 70 (10): 6173–6180. doi:10.1128/AEM.70.10.6173-6180.2004. PMID 15466564.
  9. Kim, M.H.; Choi, W.C.; Kang, H.O.; Lee, J.S.; Kang, B.S.; Kim, K.J.; Derewenda, Z.S.; Oh, T.K.; Lee, C.H.; Lee, J.K. (2005). "The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase". Proc. Natl. Acad. Sci. USA. 102 (49): 17606–17611. doi:10.1073/pnas.0504996102. PMID 16314577.
  10. Liu, D.; Lepore, B.W.; Petsko, G.A.; Thomas, P.W.; Stone, E.M.; Fast, W.; Ringe, D. (2005). "Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis". Proc. Natl. Acad. Sci. USA. 102 (33): 11882–11887. doi:10.1073/pnas.0505255102. PMID 16087890.
  11. Yang, F.; Wang, L.H.; Wang, J.; Dong, Y.H.; Hu, J.Y.; Zhang, L.H. (2005). "Quorum quenching enzyme activity is widely conserved in the sera of mammalian species". FEBS Lett. 579 (17): 3713–3717. doi:10.1016/j.febslet.2005.05.060. PMID 15963993.
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