Global InformationLactonase information
| acyl-L-homoserine-lactone lactonohydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.1.81 | ||||||||
| CAS no. | 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 | ||||||||
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Lactonase (EC 3.1.1.81, acyl-homoserine lactonase; systematic name N-acyl-L-homoserine-lactone lactonohydrolase) is a metalloenzyme, produced by certain species of bacteria, which targets and inactivates acylated homoserine lactones (AHLs). It catalyzes the reaction
- an N-acyl-L-homoserine lactone + H2O an N-acyl-L-homoserine
Many species of α-, β-, and γ-proteobacteria produce acylated homoserine lactones, small hormone-like molecules commonly used as communication signals between bacterial cells in a population to regulate certain gene expression and phenotypic behaviours.[1] This type of gene regulation is known as quorum sensing.
Other names for these types of enzymes are Quorum-quenching N-acyl-homoserine lactonase, 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.[2][3][4][5][6][7][8][9][10][11][12]
- ^ Fuqua, C.; Winans, S. C.; Greenberg, E. P. (1996). "Census and consensus in bacterial ecosystems: the LuxR-LuxI family of quorum-sensing transcriptional regulators". Annu. Rev. Microbiol. 50: 727–751. doi:10.1146/annurev.micro.50.1.727. PMID 8905097.
- ^ Thomas PW, Stone EM, Costello AL, Tierney DL, Fast W (May 2005). "The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein". Biochemistry. 44 (20): 7559–69. doi:10.1021/bi050050m. PMID 15895999.
- ^ Dong YH, Gusti AR, Zhang Q, Xu JL, Zhang LH (April 2002). "Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species". Applied and Environmental Microbiology. 68 (4): 1754–9. doi:10.1128/AEM.68.4.1754-1759.2002. PMC 123891. PMID 11916693.
- ^ Wang LH, Weng LX, Dong YH, Zhang LH (April 2004). "Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase)". The Journal of Biological Chemistry. 279 (14): 13645–51. doi:10.1074/jbc.M311194200. PMID 14734559.
- ^ Dong YH, Xu JL, Li XZ, Zhang LH (March 2000). "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. doi:10.1073/pnas.060023897. PMC 16273. PMID 10716724.
- ^ Dong YH, Wang LH, Xu JL, Zhang HB, Zhang XF, Zhang LH (June 2001). "Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase". Nature. 411 (6839): 813–7. doi:10.1038/35081101. PMID 11459062. S2CID 4324448.
- ^ Lee SJ, Park SY, Lee JJ, Yum DY, Koo BT, Lee JK (August 2002). "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. doi:10.1128/aem.68.8.3919-3924.2002. PMC 124016. PMID 12147491.
- ^ Park SY, Lee SJ, Oh TK, Oh JW, Koo BT, Yum DY, Lee JK (June 2003). "AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted homologues in other bacteria". Microbiology. 149 (Pt 6): 1541–50. doi:10.1099/mic.0.26269-0. PMID 12777494.
- ^ Ulrich RL (October 2004). "Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis". Applied and Environmental Microbiology. 70 (10): 6173–80. doi:10.1128/AEM.70.10.6173-6180.2004. PMC 522112. PMID 15466564.
- ^ Kim MH, Choi WC, Kang HO, Lee JS, Kang BS, Kim KJ, Derewenda ZS, Oh TK, Lee CH, Lee JK (December 2005). "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. doi:10.1073/pnas.0504996102. PMC 1295591. PMID 16314577.
- ^ Liu D, Lepore BW, Petsko GA, Thomas PW, Stone EM, Fast W, Ringe D (August 2005). "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. doi:10.1073/pnas.0505255102. PMC 1187999. PMID 16087890.
- ^ Yang F, Wang LH, Wang J, Dong YH, Hu JY, Zhang LH (July 2005). "Quorum quenching enzyme activity is widely conserved in the sera of mammalian species". FEBS Letters. 579 (17): 3713–7. doi:10.1016/j.febslet.2005.05.060. PMID 15963993.