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0  structures 19  species 0  interactions 23  sequences 2  architectures

Family: AHL_synthase (PF17327)

Summary: Acyl homoserine lactone synthase

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This is the Wikipedia entry entitled "Acyl-homoserine-lactone synthase". More...

Acyl-homoserine-lactone synthase Edit Wikipedia article

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 [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.; 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. PMC 38458Freely accessible. 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.; 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. 
  3. ^ 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. 
  4. ^ 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. PMC 94098Freely accessible. PMID 10482519. 
  5. ^ 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. PMC 16337Freely accessible. 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. PMC 522112Freely accessible. PMID 15466564. 
  7. ^ 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. 
  8. ^ 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. 
  9. ^ 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. PMC 1347284Freely accessible. PMID 16385066. 

External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Acyl homoserine lactone synthase Provide feedback

Members of this family are involved in quorum sensing processes. In gram negative bacteria, N-acylhomoserine lactones (AHLs) act as signals. As the bacterial density increases, AHLs accumulate, and once they reach a critical level (quorum), they interact with cognate receptor proteins, which then affect target gene expression. Some AHLs are synthesized by LuxM (AHL synthase) and homologs (VanM and opaM)[1]. LuxM enzymes use S-adenosyl-methionine (SAM) as one of its two substrates and are capable of using either acyl-acyl-carrier-protein (acyl-ACP) or acyl-coenzyme A (acyl-CoA) as the other substrate [2]. VanM, the LuxM homolog, produces two auto-inducers C6HSL and 3OC6HSL. Both autoinducers are detected by the VanN receptor. The autoinducers HAI-1, is synthesized by the cytoplasmic enzymes LuxM [3].

Literature references

  1. Britstein M, Devescovi G, Handley KM, Malik A, Haber M, Saurav K, Teta R, Costantino V, Burgsdorf I, Gilbert JA, Sher N, Venturi V, Steindler L;, Appl Environ Microbiol. 2015;82:1274-1285.: A New N-Acyl Homoserine Lactone Synthase in an Uncultured Symbiont of the Red Sea Sponge Theonella swinhoei. PUBMED:26655754 EPMC:26655754

  2. Li Z, Nair SK;, Protein Sci. 2012;21:1403-1417.: Quorum sensing: how bacteria can coordinate activity and synchronize their response to external signals?. PUBMED:22825856 EPMC:22825856

  3. Ng WL, Bassler BL;, Annu Rev Genet. 2009;43:197-222.: Bacterial quorum-sensing network architectures. PUBMED:19686078 EPMC:19686078


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Full
(23)
Representative proteomes UniProt
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NCBI
(417)
Meta
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RP15
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RP35
(4)
RP55
(23)
RP75
(51)
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This family is new in this Pfam release.

Seed source: PRODOM:PD097636
Previous IDs: none
Type: Family
Author: El-Gebali S
Number in seed: 11
Number in full: 23
Average length of the domain: 343.50 aa
Average identity of full alignment: 30 %
Average coverage of the sequence by the domain: 94.61 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 114.6 114.3
Noise cut-off 19.3 18.7
Model length: 377
Family (HMM) version: 1
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