Acyl-homoserine-lactone synthase
Identifiers
EC no.2.3.1.184
CAS no.176023-66-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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 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.

External links

Transferases: acyltransferases (EC 2.3)
Enzymes
More
Category