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 | ||||||||
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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
- ↑ Schaefer, A.L.; Val, D.L.; Hanzelka, B.L.; Cronan, J.E. Jr.; 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.
- ↑ Watson, W.T.; Murphy, F.V. 4th; Gould, T.A.; Jambeck, P.; Val, D.L.; Cronan, J.E. Jr.; Beck von Bodman, S.; Churchill, M.E. (2001). "Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI". Acta Crystallogr. D. 57 (Pt 12): 1945–1949. doi:10.1107/s0907444901014512. PMID 11717525.
- ↑ Chakrabarti, S.; 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.
- ↑ Hanzelka, B.L.; Parsek, M.R.; Val, D.L.; Dunlap, P.V.; Cronan, J.E. Jr.; Greenberg, E.P. (1999). "Acylhomoserine lactone synthase activity of the Vibrio fischeri AinS protein". J. Bacteriol. 181 (18): 5766–5770. PMID 10482519.
- ↑ Parsek, M.R.; Val, D.L.; Hanzelka, B.L.; Cronan, J.E. Jr.; 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.
- ↑ 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.
- ↑ Gould, T.A.; Schweizer, H.P.; 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.
- ↑ Raychaudhuri, A.; Jerga, A.; 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.
- ↑ Gould, T.A.; Herman, J.; Krank, J.; Murphy, R.C.; 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
- Acyl-homoserine-lactone synthase at the US National Library of Medicine Medical Subject Headings (MeSH)