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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-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-[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 edit

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 edit

  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 edit

acyl, homoserine, lactone, synthase, enzyme, with, systematic, name, acyl, acyl, carrier, protein, adenosyl, methionine, acyltranserase, lactone, forming, methylthioadenosine, releasing, this, enzyme, catalyses, following, chemical, reactionidentifiersec, 184c. 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 reactionAcyl homoserine lactone synthaseIdentifiersEC no 2 3 1 184CAS no 176023 66 8DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins acyl acyl carrier protein S adenosyl L methionine displaystyle 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 editacyl 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 edit 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 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 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 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 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 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 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 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 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 editAcyl homoserine lactone synthase at the U S National Library of Medicine Medical Subject Headings MeSH Portal nbsp Biology Retrieved from https en wikipedia org w index php title Acyl homoserine lactone synthase amp oldid 1172338396, wikipedia, wiki, book, books, library,

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