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Information on EC 2.3.1.229 - 4-coumaroyl-homoserine lactone synthase
for references in articles please use BRENDA:EC2.3.1.229
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.229 4-coumaroyl-homoserine lactone synthase
IUBMB Comments
The enzyme is found in the bacterium Rhodopseudomonas palustris, which produces N-(4-coumaroyl)-L-homoserine lactone as a quorum-sensing signal.
The expected taxonomic range for this enzyme is: Rhodopseudomonas palustris
Reaction Schemes
showSynonyms
acyl-homoserine lactone synthase, acyl-HSL synthase, autoinducer (acylhomoserine lactone) synthase, p-coumaryl-homoserine lactone synthase, pcoumaroyl-HSL synthase, RpaI, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl-homoserine lactone synthase
acyl-HSL synthase
autoinducer (acylhomoserine lactone) synthase
p-coumaryl-homoserine lactone synthase
-
-
-
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pcoumaroyl-HSL synthase
RpaI
RpaI
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-coumaroyl-CoA + S-adenosyl-L-methionine = CoA + S-methyl-5'-thioadenosine + N-(4-coumaroyl)-L-homoserine lactone
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SYSTEMATIC NAME
IUBMB Comments
4-coumaroyl-CoA:S-adenosyl-L-methionine trans-4-coumaroyltranserase (lactone-forming, methylthioadenosine-releasing)
The enzyme is found in the bacterium Rhodopseudomonas palustris, which produces N-(4-coumaroyl)-L-homoserine lactone as a quorum-sensing signal.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + S-adenosyl-L-methionine
CoA + S-methyl-5'-thioadenosine + N-(4-coumaroyl)-L-homoserine lactone
4-O-methylcinnamoyl-CoA + S-adenosyl-L-methionine
CoA + S-methyl-5'-thioadenosine + N-(4-O-methylcinnamoyl)-L-homoserine lactone
4-coumaroyl-CoA + S-adenosyl-L-methionine
CoA + S-methyl-5'-thioadenosine + N-(4-coumaroyl)-L-homoserine lactone
Substrates: -
Products: -
Products: -
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4-coumaroyl-CoA + S-adenosyl-L-methionine
CoA + S-methyl-5'-thioadenosine + N-(4-coumaroyl)-L-homoserine lactone
Substrates: -
Products: -
Products: -
?
4-O-methylcinnamoyl-CoA + S-adenosyl-L-methionine
CoA + S-methyl-5'-thioadenosine + N-(4-O-methylcinnamoyl)-L-homoserine lactone
Substrates: -
Products: -
Products: -
?
4-O-methylcinnamoyl-CoA + S-adenosyl-L-methionine
CoA + S-methyl-5'-thioadenosine + N-(4-O-methylcinnamoyl)-L-homoserine lactone
Substrates: -
Products: -
Products: -
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additional information
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Substrates: enzyme uses environmental 4-coumaric acid rather than fatty acids from cellular pools
Products: -
Products: -
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additional information
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Substrates: enzyme uses environmental 4-coumaric acid rather than fatty acids from cellular pools
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + S-adenosyl-L-methionine
CoA + S-methyl-5'-thioadenosine + N-(4-coumaroyl)-L-homoserine lactone
4-coumaroyl-CoA + S-adenosyl-L-methionine
CoA + S-methyl-5'-thioadenosine + N-(4-coumaroyl)-L-homoserine lactone
Substrates: -
Products: -
Products: -
?
4-coumaroyl-CoA + S-adenosyl-L-methionine
CoA + S-methyl-5'-thioadenosine + N-(4-coumaroyl)-L-homoserine lactone
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme uses environmental 4-coumaric acid rather than fatty acids from cellular pools
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme uses environmental 4-coumaric acid rather than fatty acids from cellular pools
Products: -
Products: -
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0026
4-coumaroyl-CoA
pH not specified in the publication, temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RPAI_RHOPA
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
218
0
24646
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with CoA and p-coumaroyl S-adenosyl-L-homocysteine, to 1.85 A resolution. The CoA binding pocket is lined with hydrophobic residues, including Ile 28, Tyr29, Trp35, Val106, and Trp147. The indole platform comprises residues Trp146 and Trp147
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q124A
Q124A
mutant shows increased activity with 4-O-methylcinnamoyl-CoA, yielding about 80% N-(4-O-methylcinnamoyl)-L-homoserine lactone
Q124A
-
mutant shows increased activity with 4-O-methylcinnamoyl-CoA, yielding about 80% N-(4-O-methylcinnamoyl)-L-homoserine lactone
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
engineered biosynthetic pathways for the phenylacetyl-homoserine lactones analogs in Escherichia coli with N-acyl-homoserine lactone synthase (RpaI) from Rhodopseudomonas palustris, tyrosine ammonia lyase (TAL) from Saccharothrix espanaensis, coumarate 3-hydroxylase (Sam5) from S. espanaensis, caffeic acid O-methyltransferase (COM) from Arabidopsis thaliana, and p-coumarate-CoA ligase (4CL) from Nicotiana tabacum
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the bacterium has a signal receptor with homology to fatty acyl-homoserine lactone receptors that responds to 4-coumaroyl-homoserine lactone to regulate global gene expression
the bacterium has a signal receptor with homology to fatty acyl-homoserine lactone receptors that responds to 4-coumaroyl-homoserine lactone to regulate global gene expression
the bacterium has a signal receptor with homology to fatty acyl-homoserine lactone receptors that responds to 4-coumaroyl-homoserine lactone to regulate global gene expression
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-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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development of an artificial biosynthetic process for phenylacetyl-homoserine lactone analogs, including cinnamoyl-homoserine lactone, 4-coumaroyl-homoserine lactone, caffeoyl-homoserine lactone, and feruloyl-homoserine lactone, using coexpression of the codon-optimized synthase RpaI and 4-coumaroyl-CoA ligase 4CL2nt, EC 6.2.1.12, in Escherichia coli. De novo production of p-coumaroyl-homoserine lactone in Escherichia coli can be achieved by expression of the rpaI gene in addition to 4-coumaroyl-CoA biosynthetic genes. The yields for 4-coumaroyl-homoserine lactone reach 93 and 142 mg/l in the S-adenosyl-L-methionine and L-methionine feeding culture, respectively
synthesis
production of bacterial quorum sensing antagonists, caffeoyl- and Feruloyl-HSL, by an artificial biosynthetic pathway. An Escherichia coli system containing artificial biosynthetic pathways that yield phenylacetyl-homoserine lactones from simple carbon sources. The artificial biosynthetic pathways contain the LuxI-type synthase gene (rpaI) in addition to caffeoyl-CoA and feruloyl-CoA biosynthetic genes, respectively. The yields for caffeoyl-phenylacetyl-homoserine lactone and feruloyl-phenylacetyl-homoserine lactone are 97.1 and 65.2 mg/l, respectively, by tyrosine-overproducing Escherichia coli with a L-methionine feeding strategy
synthesis
-
production of bacterial quorum sensing antagonists, caffeoyl- and Feruloyl-HSL, by an artificial biosynthetic pathway. An Escherichia coli system containing artificial biosynthetic pathways that yield phenylacetyl-homoserine lactones from simple carbon sources. The artificial biosynthetic pathways contain the LuxI-type synthase gene (rpaI) in addition to caffeoyl-CoA and feruloyl-CoA biosynthetic genes, respectively. The yields for caffeoyl-phenylacetyl-homoserine lactone and feruloyl-phenylacetyl-homoserine lactone are 97.1 and 65.2 mg/l, respectively, by tyrosine-overproducing Escherichia coli with a L-methionine feeding strategy
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schaefer, A.; Greenberg, E.; Oliver, C.; Oda, Y.; Huang, J.; Bittan-Banin, G.; Peres, C.; Schmidt, S.; Juhaszova, K.; Sufrin, J.; Harwood, C.
A new class of homoserine lactone quorum-sensing signals
Nature
454
595-599
2008
Rhodopseudomonas palustris (Q6NCZ6), Rhodopseudomonas palustris ATCC BAA-98 (Q6NCZ6)
brenda
Kang, S.Y.; Lee, J.K.; Jang, J.H.; Hwang, B.Y.; Hong, Y.S.
Production of phenylacetyl-homoserine lactone analogs by artificial biosynthetic pathway in Escherichia coli
Microb. Cell Fact.
14
191
2015
Rhodopseudomonas palustris
brenda
Kang, S.; Kim, B.; Heo, K.; Jang, J.; Kim, W.; Hong, Y.
Production of bacterial quorum sensing antagonists, caffeoyl- and Feruloyl-HSL, by an artificial biosynthetic pathway
J. Microbiol. Biotechnol.
27
2104-2111
2017
Rhodopseudomonas palustris (Q6NCZ6), Rhodopseudomonas palustris ATCC BAA-98 (Q6NCZ6)
brenda
Dong, S.; Nhu-Lam, M.; Nagarajan, R.; Nair, S.
Structure-guided biochemical analysis of quorum signal synthase specificities
ACS Chem. Biol.
15
1497-1504
2020
Rhodopseudomonas palustris (Q6NCZ6), Rhodopseudomonas palustris ATCC BAA-98 (Q6NCZ6)
brenda
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