Acyl-homoserine-lactone synthase

Acyl-homoserine-lactone synthase
Identifiers
EC number 2.3.1.184
CAS number 176023-66-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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 \rightleftharpoons [acyl-carrier protein] + S-methyl-5'-thioadenosine + N-acyl-L-homoserine lactone

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, A.L., Val, D.L., Hanzelka, B.L., Cronan, J.E., Jr. and Greenberg, E.P. (1996). "Generation of cell-to-cell signals in quorum sensing: acyl homoserine lactone synthase activity of a purified Vibrio fischeri LuxI protein". Proc. Natl. Acad. Sci. USA 93 (18): 9505–9509. doi:10.1073/pnas.93.18.9505. PMID 8790360.
  2. Watson, W.T., Murphy, F.V., 4th, Gould, T.A., Jambeck, P., Val, D.L., Cronan, J.E., Jr., Beck von Bodman, S. and Churchill, M.E. (2001). "Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI". Acta Crystallogr. D Biol. Crystallogr. 57 (Pt 12): 1945–1949. doi:10.1107/s0907444901014512. PMID 11717525.
  3. Chakrabarti, S. and Sowdhamini, R. (2003). "Functional sites and evolutionary connections of acylhomoserine lactone synthases". Protein Eng. 16 (4): 271–278. doi:10.1093/proeng/gzg031. PMID 12736370.
  4. Hanzelka, B.L., Parsek, M.R., Val, D.L., Dunlap, P.V., Cronan, J.E., Jr. and Greenberg, E.P. (1999). "Acylhomoserine lactone synthase activity of the Vibrio fischeri AinS protein". J. Bacteriol. 181 (18): 5766–5770. PMID 10482519.
  5. Parsek, M.R., Val, D.L., Hanzelka, B.L., Cronan, J.E., Jr. and Greenberg, E.P. (1999). "Acyl homoserine-lactone quorum-sensing signal generation". Proc. Natl. Acad. Sci. USA 96 (8): 4360–4365. doi:10.1073/pnas.96.8.4360. PMID 10200267.
  6. Ulrich, R.L. (2004). "Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis". Appl. Environ. Microbiol. 70: 6173–6180. doi:10.1128/AEM.70.10.6173-6180.2004. PMID 15466564.
  7. Gould, T.A., Schweizer, H.P. and Churchill, M.E. (2004). "Structure of the Pseudomonas aeruginosa acyl-homoserinelactone synthase LasI". Mol. Microbiol. 53 (4): 1135–1146. doi:10.1111/j.1365-2958.2004.04211.x. PMID 15306017.
  8. Raychaudhuri, A., Jerga, A. and Tipton, P.A. (2005). "Chemical mechanism and substrate specificity of RhlI, an acylhomoserine lactone synthase from Pseudomonas aeruginosa". Biochemistry 44 (8): 2974–2981. doi:10.1021/bi048005m. PMID 15723540.
  9. Gould, T.A., Herman, J., Krank, J., Murphy, R.C. and Churchill, M.E. (2006). "Specificity of acyl-homoserine lactone synthases examined by mass spectrometry". J. Bacteriol. 188 (2): 773–783. doi:10.1128/JB.188.2.773-783.2006. PMID 16385066.

External links

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