Acyl-homoserine-lactone synthase

Acyl-homoserine-lactone synthase (EC 2.3.1.184) is an enzyme with systematic name acyl-(acyl-carrier protein):S-adenosyl-L-methionine acyltranserase (lactone-forming, methylthioadenosine-releasing).[1][2][3][4][5][6][7][8][9] This enzyme catalyses the following chemical reaction

acyl-[acyl-carrier protein] + S-adenosyl-L-methionine [acyl-carrier protein] + S-methyl-5'-thioadenosine + N-acyl-L-homoserine lactone
Acyl-homoserine-lactone synthase
Identifiers
EC no.2.3.1.184
CAS no.176023-66-8
Databases
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BRENDABRENDA entry
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KEGGKEGG entry
MetaCycmetabolic pathway
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NCBIproteins

Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing.

Alternate names

acyl-homoserine lactone synthase, acyl homoserine lactone synthase, acyl-homoserinelactone synthase, acylhomoserine lactone synthase, AHL synthase, AHS, AHSL synthase, AhyI, AinS, AinS protein, autoinducer synthase, autoinducer synthesis protein rhlI, EsaI, ExpISCC1, ExpISCC3065, LasI, LasR, LuxI, LuxI protein, LuxM, N-acyl homoserine lactone synthase, RhlI, YspI, acyl-[acyl carrier protein]:S-adenosyl-L-methionine acyltranserase (lactone-forming, methylthioadenosine-releasing)

References
  1. Schaefer AL, Val DL, Hanzelka BL, Cronan JE, Greenberg EP (September 1996). "Generation of cell-to-cell signals in quorum sensing: acyl homoserine lactone synthase activity of a purified Vibrio fischeri LuxI protein". Proceedings of the National Academy of Sciences of the United States of America. 93 (18): 9505–9. doi:10.1073/pnas.93.18.9505. PMC 38458. PMID 8790360.
  2. Watson WT, Murphy FV, Gould TA, Jambeck P, Val DL, Cronan JE, Beck von Bodman S, Churchill ME (December 2001). "Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI". Acta Crystallographica D. 57 (Pt 12): 1945–9. doi:10.1107/s0907444901014512. PMID 11717525.
  3. Chakrabarti S, Sowdhamini R (April 2003). "Functional sites and evolutionary connections of acylhomoserine lactone synthases". Protein Engineering. 16 (4): 271–8. doi:10.1093/proeng/gzg031. PMID 12736370.
  4. Hanzelka BL, Parsek MR, Val DL, Dunlap PV, Cronan JE, Greenberg EP (September 1999). "Acylhomoserine lactone synthase activity of the Vibrio fischeri AinS protein". Journal of Bacteriology. 181 (18): 5766–70. doi:10.1128/JB.181.18.5766-5770.1999. PMC 94098. PMID 10482519.
  5. Parsek MR, Val DL, Hanzelka BL, Cronan JE, Greenberg EP (April 1999). "Acyl homoserine-lactone quorum-sensing signal generation". Proceedings of the National Academy of Sciences of the United States of America. 96 (8): 4360–5. doi:10.1073/pnas.96.8.4360. PMC 16337. PMID 10200267.
  6. 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.
  7. Gould TA, Schweizer HP, Churchill ME (August 2004). "Structure of the Pseudomonas aeruginosa acyl-homoserinelactone synthase LasI". Molecular Microbiology. 53 (4): 1135–46. doi:10.1111/j.1365-2958.2004.04211.x. PMID 15306017.
  8. Raychaudhuri A, Jerga A, Tipton PA (March 2005). "Chemical mechanism and substrate specificity of RhlI, an acylhomoserine lactone synthase from Pseudomonas aeruginosa". Biochemistry. 44 (8): 2974–81. doi:10.1021/bi048005m. PMID 15723540.
  9. Gould TA, Herman J, Krank J, Murphy RC, Churchill ME (January 2006). "Specificity of acyl-homoserine lactone synthases examined by mass spectrometry". Journal of Bacteriology. 188 (2): 773–83. doi:10.1128/JB.188.2.773-783.2006. PMC 1347284. PMID 16385066.
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