Information on EC 2.3.1.184 - acyl-homoserine-lactone synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.184
-
RECOMMENDED NAME
GeneOntology No.
acyl-homoserine-lactone synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an acyl-[acyl-carrier protein] + S-adenosyl-L-methionine = an [acyl-carrier protein] + S-methyl-5'-thioadenosine + an N-acyl-L-homoserine lactone
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
autoinducer AI-1 biosynthesis
-
-
Cysteine and methionine metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:S-adenosyl-L-methionine acyltranserase (lactone-forming, methylthioadenosine-releasing)
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. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes [5]. N-(3-Oxohexanoyl)-[acyl-carrier protein] and hexanoyl-[acyl-carrier protein] are the best substrates [1]. The fatty-acyl substrate is derived from fatty-acid biosynthesis through acyl-[acyl-carrier protein] rather than from fatty-acid degradation through acyl-CoA [1]. S-Adenosyl-L-methionine cannot be replaced by methionine, S-adenosylhomocysteine, homoserine or homoserine lactone [1].
CAS REGISTRY NUMBER
COMMENTARY hide
176023-66-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
pathogen of fish, humans, and amphibians, strain AH-1N, gene ahyI
-
-
Manually annotated by BRENDA team
gene ahpF
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-
Manually annotated by BRENDA team
gene ahpF
-
-
Manually annotated by BRENDA team
several isozymes, including genes btaI1 and btaI3
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-
Manually annotated by BRENDA team
gene cviI encoding HHL synthase
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-
Manually annotated by BRENDA team
strain NZP 2213
TREMBL
Manually annotated by BRENDA team
strain NZP 2213
TREMBL
Manually annotated by BRENDA team
wild-type strain CCBAU060A and quorum-sensing deficient mutant HJC0
TREMBL
Manually annotated by BRENDA team
formerly Erwinia carotovora, gene expI
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-
Manually annotated by BRENDA team
i.e. Pectobacterium carotovora ssp. carotovora, genes expISCC1 and expISCC3065
SwissProt
Manually annotated by BRENDA team
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-
UniProt
Manually annotated by BRENDA team
strain PAO-JP1, gene rhlI
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-
Manually annotated by BRENDA team
strain PUPa3, rice rhizosphere isolate, and knockout mutations
SwissProt
Manually annotated by BRENDA team
gene ppuI
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-
Manually annotated by BRENDA team
gene ppuI
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-
Manually annotated by BRENDA team
gene psyI
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-
Manually annotated by BRENDA team
gene smaI
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-
Manually annotated by BRENDA team
gene smaI
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-
Manually annotated by BRENDA team
symbiont of the Red Sea sponge Theonella swinhoei
UniProt
Manually annotated by BRENDA team
gene yenI
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-
Manually annotated by BRENDA team
strain KIM6+
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-
Manually annotated by BRENDA team
gene yspI
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxydecanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-3-hydroxydecanoyl-L-homoserine lactone
show the reaction diagram
3-hydroxydodecanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
N-(3-hydroxydodecanoyl)-L-homoserine lactone + [acyl-carrier protein] + S-methyl-5'-thioadenosine
show the reaction diagram
3-oxo-dodecanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-3-oxododecanoyl-L-homoserine lactone
show the reaction diagram
3-oxo-octanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + 3-oxo-octanoyl-L-homoserine lactone
show the reaction diagram
3-oxododecanoyl-[acyl carrier protein] + S-adenosyl-L-methionine
N-(3-oxododecanoyl)-homoserine lactone + [acyl carrier protein] + 5'-methyl-thioadenosine
show the reaction diagram
3-oxododecanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
N-(3-oxododecanoyl)-L-homoserine lactone + [acyl-carrier protein] + S-methyl-5'-thioadenosine
show the reaction diagram
3-oxododecanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-3-oxododecanoyl-L-homoserine lactone
show the reaction diagram
-
LasI
-
-
?
3-oxohexanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-3-oxohexanoyl-L-homoserine lactone
show the reaction diagram
3-oxotetradecanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
N-(3-oxotetradecanoyl)-L-homoserine lactone + [acyl-carrier protein] + S-methyl-5'-thioadenosine
show the reaction diagram
-
-
-
?
an acyl-[acyl-carrier protein] + S-adenosyl-L-methionine
an [acyl-carrier protein] + S-methyl-5'-thioadenosine + an N-acyl-L-homoserine lactone
show the reaction diagram
an acyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + an N-acyl-L-homoserine lactone
show the reaction diagram
butanoyl [acyl carrier protein] + S-adenosyl-L-methionine
N-butanoyl homoserine lactone + [acyl carrier protein] + 5'-methyl-thioadenosine
show the reaction diagram
butanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
N-butanoyl-L-homoserine lactone + [acyl-carrier protein] + S-methyl-5'-thioadenosine
show the reaction diagram
butanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + butanoyl-L-homoserine lactone
show the reaction diagram
-
RhlI
-
-
?
decanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
N-decanoyl-L-homoserine lactone + [acyl-carrier protein] + S-methyl-5'-thioadenosine
show the reaction diagram
-
-
-
?
dodecanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
N-dodecanoyl-L-homoserine lactone + [acyl-carrier protein] + S-methyl-5'-thioadenosine
show the reaction diagram
-
-
-
?
hexanoyl [acyl carrier protein] + S-adenosyl-L-methionine
N-hexanoyl homoserine lactone + [acyl carrier protein] + 5'-methyl-thioadenosine
show the reaction diagram
-
production is only 1/15 of N-butanoyl homoserine lactone
-
-
ir
hexanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-hexanoyl -L-homoserine lactone
show the reaction diagram
-
-
-
-
?
N-butanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-butanoyl-L-homoserine lactone
show the reaction diagram
N-decanoyl -[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-decanoyl -L-homoserine lactone
show the reaction diagram
-
-
-
-
?
N-hexanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-hexanoyl-L-homoserine lactone
show the reaction diagram
N-octanoyl -[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-octanoyl -L-homoserine lactone
show the reaction diagram
octanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
N-octanoyl-L-homoserine lactone + [acyl-carrier protein] + S-methyl-5'-thioadenosine
show the reaction diagram
-
-
-
?
octanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-octanoyl-L-homoserine lactone
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 3-hydroxybutyryl-[acyl-carrier protein]
5'-methylthioadenosine + N-3-hydroxybutyryl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
-
substrate of LuxM
-
-
?
S-adenosyl-L-methionine + 3-oxodecanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-3-oxodecanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
S-adenosyl-L-methionine + 3-oxododecanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-3-oxododecanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
S-adenosyl-L-methionine + 3-oxohexanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-3-oxohexanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
S-adenosyl-L-methionine + 3-oxooctanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-3-oxooctanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
S-adenosyl-L-methionine + 3-oxotetradecanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-3-oxotetradecanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
-
substrate of wild-type and mutant LasI, overview
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-
?
S-adenosyl-L-methionine + 3-oxoundecanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-3-oxoundecanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
-
substrate of wild-type and mutant LasI, overview
-
-
?
S-adenosyl-L-methionine + butyryl-CoA
5'-methylthioadenosine + N-butyryl-L-homoserine-1,4-lactone + CoA
show the reaction diagram
S-adenosyl-L-methionine + butyryl-S-adenosyl-L-methionine
5'-methylthioadenosine + N-butyryl-L-homoserine-1,4-lactone + S-adenosyl-L-methionine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + butyryl-[acyl-carrier protein 1]
5'-methylthioadenosine + N-butyryl-L-homoserine-1,4-lactone + [acyl-carrier protein 1]
show the reaction diagram
-
substrate of RhlI, three different [acyl-carrier-protein] isozymes from Pseudomonas aeruginosa serve as substrates
-
-
?
S-adenosyl-L-methionine + butyryl-[acyl-carrier protein 2]
5'-methylthioadenosine + N-butyryl-L-homoserine-1,4-lactone + [acyl-carrier protein 2]
show the reaction diagram
-
substrate of RhlI, three different [acyl-carrier-protein] isozymes from Pseudomonas aeruginosa serve as substrates
-
-
?
S-adenosyl-L-methionine + butyryl-[acyl-carrier protein 3]
5'-methylthioadenosine + N-butyryl-L-homoserine-1,4-lactone + [acyl-carrier protein 3]
show the reaction diagram
-
substrate of RhlI, three different [acyl-carrier-protein] isozymes from Pseudomonas aeruginosa serve as substrates, very low activity with ACP3
-
-
?
S-adenosyl-L-methionine + butyryl-[acyl-carrier protein]
5'-methylthioadenosine + N-butyryl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
S-adenosyl-L-methionine + decanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-decanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
S-adenosyl-L-methionine + hexanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-hexanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
S-adenosyl-L-methionine + octanoyl-CoA
5'-methylthioadenosine + N-octanoyl-L-homoserine-1,4-lactone + CoA
show the reaction diagram
-
substrate of recombinant MBP-AinS, lower activity
-
-
?
S-adenosyl-L-methionine + octanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-octanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
tetradecanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
N-tetradecanoyl-L-homoserine lactone + [acyl-carrier protein] + S-methyl-5'-thioadenosine
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-hydroxydecanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-3-hydroxydecanoyl-L-homoserine lactone
show the reaction diagram
3-oxo-dodecanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-3-oxododecanoyl-L-homoserine lactone
show the reaction diagram
3-oxo-octanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + 3-oxo-octanoyl-L-homoserine lactone
show the reaction diagram
-
TraI synthesizes primarily 3-oxo-octanoyl homoserine lactone
-
-
?
3-oxododecanoyl-[acyl carrier protein] + S-adenosyl-L-methionine
N-(3-oxododecanoyl)-homoserine lactone + [acyl carrier protein] + 5'-methyl-thioadenosine
show the reaction diagram
3-oxododecanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-3-oxododecanoyl-L-homoserine lactone
show the reaction diagram
-
LasI
-
-
?
3-oxohexanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-3-oxohexanoyl-L-homoserine lactone
show the reaction diagram
an acyl-[acyl-carrier protein] + S-adenosyl-L-methionine
an [acyl-carrier protein] + S-methyl-5'-thioadenosine + an N-acyl-L-homoserine lactone
show the reaction diagram
an acyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + an N-acyl-L-homoserine lactone
show the reaction diagram
butanoyl [acyl carrier protein] + S-adenosyl-L-methionine
N-butanoyl homoserine lactone + [acyl carrier protein] + 5'-methyl-thioadenosine
show the reaction diagram
butanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + butanoyl-L-homoserine lactone
show the reaction diagram
-
RhlI
-
-
?
hexanoyl [acyl carrier protein] + S-adenosyl-L-methionine
N-hexanoyl homoserine lactone + [acyl carrier protein] + 5'-methyl-thioadenosine
show the reaction diagram
-
production is only 1/15 of N-butanoyl homoserine lactone
-
-
ir
hexanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-hexanoyl -L-homoserine lactone
show the reaction diagram
-
-
-
-
?
N-butanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-butanoyl-L-homoserine lactone
show the reaction diagram
N-decanoyl -[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-decanoyl -L-homoserine lactone
show the reaction diagram
-
-
-
-
?
N-hexanoyl-[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-hexanoyl-L-homoserine lactone
show the reaction diagram
N-octanoyl -[acyl-carrier protein] + S-adenosyl-L-methionine
[acyl-carrier protein] + S-methyl-5'-thioadenosine + N-octanoyl -L-homoserine lactone
show the reaction diagram
S-adenosyl-L-methionine + 3-hydroxybutyryl-[acyl-carrier protein]
5'-methylthioadenosine + N-3-hydroxybutyryl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
-
substrate of LuxM
-
-
?
S-adenosyl-L-methionine + 3-oxodecanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-3-oxodecanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
S-adenosyl-L-methionine + 3-oxododecanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-3-oxododecanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
-
substrate of LasI
-
-
?
S-adenosyl-L-methionine + 3-oxohexanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-3-oxohexanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
S-adenosyl-L-methionine + 3-oxooctanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-3-oxooctanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
S-adenosyl-L-methionine + butyryl-[acyl-carrier protein]
5'-methylthioadenosine + N-butyryl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
S-adenosyl-L-methionine + decanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-decanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + hexanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-hexanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
S-adenosyl-L-methionine + octanoyl-[acyl-carrier protein]
5'-methylthioadenosine + N-octanoyl-L-homoserine-1,4-lactone + [acyl-carrier protein]
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(4-cyclopentyl-1H-1,2,3-triazol-1-yl)-N-[(3S)-2-oxotetrahydrofuran-3-yl]acetamide
2-(4-hexyl-1H-1,2,3-triazol-1-yl)-N-[(3S)-2-oxotetrahydrofuran-3-yl]acetamide
3-[4-(3-formylphenyl)-1H-1,2,3-triazol-1-yl]-N-[(3S)-2-oxotetrahydrofuran-3-yl]propanamide
5'-methylthioadenosine
9-hydroxy-2-propyl-4H-pyrido[1,2-a]pyrimidin-4-one
-
-
AhyR
-
the AhyR regulates AhyI positively and negatively in a growth phase-dependent manner
-
butyryl-S-adenosyl-L-methionine
-
24% inhibition at 0.05 mM, 65% inhibition at 0.5 mM
E9C-3oxoC6
-
competitively inhibits N-octanoyl -L-homoserine lactone binding to TofR, binding structure, overview
J8-C8
-
binds to TofI, occupying the binding site for the acyl chain of the TofI cognate substrate, acylated acyl-carrier protein, and reaction byproduct, 5'-methylthioadenosine, independently binds to the binding site for a second substrate, S-adenosyl-L-methionine, TofI(3MDELTA)/J8-C8/MTA ternary complex, binding structure, overview. In the ternary complex, J8-C8 is bound to the pocket observed in the apo-TofI(3M?) structure. The octanoyl chain is almost in an elongated conformation
N-(3-oxocyclohex-1-en-1-yl)octanamide
-
-
S-Adenosyl-D-homocysteine
S-adenosyl-L-cysteine
-
77% inhibition at 0.05 mM, 97% inhibition at 0.5 mM
S-adenosyl-L-homocysteine
sinefungin
-
58% inhibition at 0.1 mM
Tannic acid
efficiently inhibits N-acylhomoserine lactone production by isoform RhlI, specifically target short-chain N-acylhomoserine lactone synthase RhlI
trans-cinnamaldehyde
efficiently inhibits N-acylhomoserine lactone production by isoform RhlI, specifically target short-chain N-acylhomoserine lactone synthase RhlI. trans-Cinnamaldehyde reduces the quorum-sensing-regulated pyocyanin production up to 42%; molecular docking ananlysis, mainly interacts with substrate binding sites. trans-Cinnamaldehyde is locked deeply into the binding site and forms hydrophobic and Pi-Pi interactions with surrounding residues Phe27, Trp33 and Phe105 and one hydrogen bond with Arg30
[Acyl-carrier-protein]
additional information
-
no inhibition by N-butyryl-L-homoserine-1,4-lactone, CoA, NADH, L-methionine, L-homocysteine, L-homoserine-1,4-lactone, pantothenate, L-homoserine, butyric acid, cerulenin, ATP, ADP, 4-hydroxybutyrate, butyryl-CoA, and apo-ACP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-hydroxy-C12-HSL
abaI is regulated by a positive-feedback loop involving self-produced acyl-homoserine lactone signals
AhyR
-
the LuxR homologue AhyR regulates AhyI positively and negatively in a growth phase-dependent manner
-
MrlR1
regulatory factor MrlR1 induced gene expression of mrlI1 which is followed by production of homoserine lactones
-
additional information
-
N-butyryl-L-homoserine-1,4-lactone induces the expression of AhyI, not by binding to DNA, requiring AhyR
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 0.23
Butyryl-CoA
0.038
butyryl-S-adenosyl-L-methionine
-
pH 7.8, 37C, recombinant RhlI
0.0074
butyryl-[acyl-carrier protein 1]
-
pH 8.8, 25C, recombinant enzyme
0.0059
butyryl-[acyl-carrier protein 2]
-
pH 8.8, 25C, recombinant enzyme
0.283
butyryl-[acyl-carrier protein 3]
-
pH 8.8, 25C, recombinant enzyme
0.006
butyryl-[acyl-carrier protein]
-
pH 7.8, 37C, recombinant RhlI
0.008 - 0.0096
hexanoyl-[acyl-carrier protein]
0.015
Octanoyl-CoA
-
pH 8.5, 25C, recombinant MBP-AinS
0.004 - 0.043
octanoyl-[acyl-carrier protein]
0.014 - 0.13
S-adenosyl-L-methionine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
Butyryl-CoA
Pseudomonas aeruginosa
-
pH 8.8, 25C, recombinant enzyme
0.35
butyryl-[acyl-carrier protein 1]
Pseudomonas aeruginosa
-
pH 8.8, 25C, recombinant enzyme
0.46
butyryl-[acyl-carrier protein 2]
Pseudomonas aeruginosa
-
pH 8.8, 25C, recombinant enzyme
0.026
butyryl-[acyl-carrier protein 3]
Pseudomonas aeruginosa
-
pH 8.8, 25C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0021
-
purified recombinant RhlI
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1 - 8
-
10% of maximal acivity at pH 7.0, 65% at pH 7.1, and 50% at pH 8.0
8 - 10
-
sharp drop of activity below pH 8.0 and above pH 10.0, inactive at pH 6.0 and pH 11.0
additional information
-
pH-profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 42
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over 60% of maximal activity at 25C and 37C, less than 15% of maximal activity at 15C and 42C
18 - 37
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57% of maximal activity at 18C and 10% at 37C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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functional sites and evolutionary relations, e.g. to the N-acetyltransferase superfamily, amino acid sequence and functionally or structurally important site comparisons
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure
crystal structure analysis, three-dimensional modeling
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purified recombinant His-tagged enzyme, vapor diffusion, 6 mg/ml protein in 0.1 M MES, pH 6.1, 14% PEG 4000, 6% 2-propanol, 0.03% 2-mercaptoethanol, 10 mM EDTA, and 0.5% NaN3, addition of agarose reduces the formation of a protein skin on the drop surface, X-ray diffraction structure determination and analysis at 1.14-1.19 A resolution, MAD phasing, modeling
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purified recombinant detagged LasIDELTAG, hanging drop vapour diffusion method, from 1.5 M ammonium sulfate, 0.125 M disodium sulfate, and 0.1 M MOPS, pH 6.5, cryoprotection with 15% glycerol, heavy atom derivatization with Hg2+, single isomorphous replacement with anomalous scattering, X-ray diffraction structure determination and analysis at 2.3-3.1 A resolution, structure modeling
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recobinant maltose binding protein-fusion AinS from Escherichia coli by amylose affinity chromatography
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
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recombinant His-tagged LasIDELTAG from Escherichia coli by nickel affinity chromatography and gel filtration, the His-tag is removed by thrombin cleavage
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recombinant maltose binding protein-fusion enzyme RhlI from Escherichia coli strain XL 1-Blue by amylose affinity chromatography, recombinant His-tagged RhlI from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant maltose-binding protein-fusion enzyme from Escherichia coli strain XL 1-Blue by amylose affinity chromatography
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recombinant RhlI 95fold from Escherichia coli strain XL 1-Blue by anion and cation exchange chromatography and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli; expressed in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
expression of wild-type and mutant enzymes in Escherichia coli
functional overexpression of His-tagged LasIDELTAG and point mutants in Escherichia coli as soluble proteins
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gene abaI, DNA and amino acid sequence determination and analysis in the different clinical isolates
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gene ainS, expression of AinS as maltose binding protein-fusion enzyme in Escherichia coli strain XL 1-Blue
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gene cviI, a luxI homologue, DNA and amino acid sequence determination and analysis, expression in the wild-type strain KT2440 and a ppoR (luxR homologue) mutant of Pseudomonas putida, the luxI homologue is located on a broad-host-range plasmid. The recombinant PpoR-HHL complex is not involved in the response to oxidative stresses caused by paraquat, hydrogen peroxide, cumene hydroperoxide, and salicylate, but responds to antibiotic stress caused by ampicillin, strain KT2440 harbouring the pHHL plasmid evidences significantly reduced attachment to a polystyrene surface, phenotype, detailed overview. Identification of 71 HHL-signalling target genes regulated by PpoR in the recombinant strain
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gene expI, is transcribed convergently and overlapping at their 3' ends with gene expR
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gene expISCC1, expression of wild-type and mutant enzymes in Escherichai coli, inoculation of Solanum tuberosum tubers
gene lasI, genetic organization and las genetic locus
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gene luxI, expression as maltose-binding protein-fusion enzyme in Escherichia coli strain XL 1-Blue
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gene ppuI, genetic organization and ppu genetic locus
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gene rhlI, expression in Escherichia coli strain XL 1-Blue
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gene rhlI, overexpression in Escherichia coli strain XL 1-Blue as maltose binding protein-fusion protein, overexpression of His-tagged RhlI in Escherichia coli strain BL21(DE3)
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gene yspI, expression of wild-type enzyme in Escherichia coli strain BL21(DE3), the recombinant enzyme shows a similar substrate profile as the native enzyme
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genes esaI and lasI, expression of wild-type and mutant enzymes in Escherichia coli
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overexpression of His-tagged enzyme in Escherichia coli straoin BL21(DE3)
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recombinant maltose binding protein-fusion protein AhyR binds to the ahyI promoter region
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the abaI gene is cloned into the pBluescript SK vector
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ExpR negatively regulates ExpI expression
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ExpR1 negatively regulates ExpI expression
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expression of acyl-homoserine lactone synthase gene mtqI from Mesorhizobium tianshanense requires acyl-homoserine lactones and the LuxR-type transcriptional activator MtqR
expression of isoform LasI increases with increase in biofilm growth
expression of isoform RhlI decreases during log phase of biofilm growth
RsaLWCS displays a strong repressive effect on the promoter of the quorum sensing signal synthase gene, ppuI. Purified RsaLWCS specifically binds to ppuI on a DNA region overlapping the predicted sigma70-binding site, but the RsaLWCS protein is not able to form stable complexes efficiently with a probe encompassing the ppuI promoter, the RsaLWCS/PppuI complex is not stable in vitro, RsaLWCS needs a molecular interactor/cofactor specific for Pseudomonas putida WCS358 to repress ppuI transcription. RsaLWCS regulates siderophore-mediated growth limitation of plant pathogens and biofilmcformation, two processes relevant for plant growth-promoting activity. Mutational analysis using a chimeric RsaLWCS mutant, RsaLWCS molecular mechanism, overview
RsaLWCS does not show a repressive effect on the promoter of the QS signal synthase gene lasI in Pseudomonas aeruginosa. RsaLWCS formed stable complexes with the promoter of lasI, the gene orthologous to ppuI. RsaLWCS regulates siderophore-mediated growth limitation of plant pathogens and biofilm formation, two processes relevant for plant growth-promoting activity. RsaL binds close to LasR on the same bidirectional promoter, repressing the transcription of both the lasI and rsaL genes. Molecular mechanism, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
abaI_Km mutant
mutant failed to produce any detectable acyl-homoserine lactone signals
T140A
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site-directed mutagenesis of EsaI, the mutant shows altered substrate acyl-chain length specificity compared to the wild-type enzyme
T142A
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site-directed mutagenesis of LasI, the mutant shows slightly altered substrate acyl-chain length specificity compared to the wild-type enzyme
T142G
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site-directed mutagenesis of LasI, the mutant shows reduced activity and altered substrate acyl-chain length specificity compared to the wild-type enzyme
T142S
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site-directed mutagenesis of LasI, the mutant shows slightly altered substrate acyl-chain length specificity compared to the wild-type enzyme
T144V
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site-directed mutagenesis of LasI, the mutant shows reduced activity and altered substrate acyl-chain length specificity compared to the wild-type enzyme
F69L
site-directed mutagenesis of ExpISCC1, the mutant shows altered substrate acyl-chain lemgth specificity compared to the wild-type enzyme
M127T
site-directed mutagenesis of ExpISCC1, the mutant shows altered substrate acyl-chain lemgth specificity compared to the wild-type enzyme
C126S
site-directed mutagenesis, the mutant shows 81.5% activity compared to the wild-type enzyme
C67S
site-directed mutagenesis, the mutant shows 1.9% activity compared to the wild-type enzyme
C67S/C69S
site-directed mutagenesis, the mutant shows 0.8% activity compared to the wild-type enzyme
C69S
site-directed mutagenesis, the mutant shows 30.4% activity compared to the wild-type enzyme
C89S
site-directed mutagenesis, the mutant shows 63% activity compared to the wild-type enzyme
D48N
site-directed mutagenesis, inactive mutant
D51N
site-directed mutagenesis, nearly inactive mutant
E101K
site-directed mutagenesis, inactive mutant
E144K
site-directed mutagenesis, the mutant shows 43.5% activity compared to the wild-type enzyme
E46K
site-directed mutagenesis, inactive mutant
E7K/F147L/P159E/E182G
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strain R2: cells produce twicefold amount of butanoyl homoserine lactone compared to wild type and yield a hexanoyl homoserine lactone level comparable to the butanoyl homoserine lactone concentration
E7K/F147L/V201M
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strain R1: cells produce twicefold amount of butanoyl homoserine lactone compared to wild type
F28L
site-directed mutagenesis, the mutant shows 0.18% activity compared to the wild-type enzyme
G159E
site-directed mutagenesis, the mutant shows 44.6% activity compared to the wild-type enzyme
G68D
site-directed mutagenesis, the mutant shows 0.075% activity compared to the wild-type enzyme
G68E
site-directed mutagenesis, inactive mutant
K150E/R154QE
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the fully active mutant LasIDELTAG
K150Q
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site-directed mutagenesis, the mutant shows similar activity as the fully active mutant LasIDELTAG
K150Q/R154Q
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site-directed mutagenesis, the mutant shows reduced activity compared to the fully active mutant LasIDELTAG
R104C
site-directed mutagenesis, nearly inactive mutant
R104H
site-directed mutagenesis, nearly inactive mutant
R154E
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site-directed mutagenesis, the mutant shows reduced activity compared to the fully active mutant LasIDELTAG
R154Q
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site-directed mutagenesis, the mutant shows similar activity as the fully active mutant LasIDELTAG
R172A
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site-directed mutagenesis, the mutant shows increased activity compared to the fully active mutant LasIDELTAG
R24W
site-directed mutagenesis, inactive mutant
R71C
site-directed mutagenesis, the mutant shows 0.05% activity compared to the wild-type enzyme
R71H
site-directed mutagenesis, inactive mutant
S103E
site-directed mutagenesis, the mutant shows 5.4% activity compared to the wild-type enzyme
W34G
site-directed mutagenesis, the mutant shows 0.10% activity compared to the wild-type enzyme
W34Y
site-directed mutagenesis, the mutant shows 60% activity compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
drug development
medicine
Acinetobacter baumannii is an important nosocomial pathogen and can cause a variety of infections including wound infection, bloodstrem infection, ventilator-acquired pneumonia, and urinary tract infections
Show AA Sequence (1883 entries)
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