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Information on EC 3.1.1.81 - quorum-quenching N-acyl-homoserine lactonase and Organism(s) Homo sapiens and UniProt Accession P27169
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3.1.1.81 quorum-quenching N-acyl-homoserine lactonaseIUBMB Comments
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 . Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL-signalling and the expression of virulence genes in quorum-sensing bacteria . N-(3-Oxohexanoyl)-L-homoserine lactone, N-(3-oxododecanoyl)-L-homoserine lactone, N-butanoyl-L-homoserine lactone and N-(3-oxooctanoyl)-L-homoserine lactone can act as substrates .
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Word Map
- 3.1.1.81
- thuringiensis
- pectobacterium
- carotovorum
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ahl-mediated
- pyocyanin
- n-hexanoyl-l-homoserine
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c6-hsl
- drug development
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biofouling
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qs-regulated
- pharmacology
- analysis
- medicine
- agriculture
- biotechnology
- food industry
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
ahl-lactonase, ahl-acylase, ahl-degrading enzyme, aiia lactonase, aii20j, n-acyl-homoserine lactonase, n-acylhomoserine lactonase, n-acyl homoserine lactonase, quorum-quenching enzyme, ahl-1, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
quorum-sensing enzyme
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SYSTEMATIC NAME
IUBMB Comments
N-acyl-L-homoserine-lactone lactonohydrolase
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]. Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL-signalling and the expression of virulence genes in quorum-sensing bacteria [5]. N-(3-Oxohexanoyl)-L-homoserine lactone, N-(3-oxododecanoyl)-L-homoserine lactone, N-butanoyl-L-homoserine lactone and N-(3-oxooctanoyl)-L-homoserine lactone can act as substrates [5].
CAS REGISTRY NUMBER
COMMENTARY
389867-43-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-3-oxodecanoyl-DL-homoserine lactone + H2O
N-3-oxodecanoyl-DL-homoserine
the N-oxodecanoyl-DL-homoserine lactone-hydrolyzing activity of recombinant h-PON1 enzyme is determined by using a recombinant quorum-sensing reporter Escherichia coli strain
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N-3-oxododecanoyl-L-homoserine lactone + H2O
N-3-oxododecanoyl-L-homoserine
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additional information
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the h-PON1 can hydrolyze (and inactivate) a variety of substrates including aryl esters, thioesters, phosphotriesters, carbonates, lactones and thiolactones, and its various hydrolytic activities can be broadly grouped into three categories, namely arylesterase, organophosphatase, and lactonase. The native activity of h-PON1 seems to be lactonase. Polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme
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additional information
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h-PON1 enzyme is also active with diethyl-paraoxon, diisopropyl fluorophosphate and chlorpyrifos-oxon, cf. EC 3.1.8.1 and EC 3.1.8.2
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additional information
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acyl-homoserine lactone quorum-sensing signals play a key role in synchronizing virulence gene expression during bloodstream infections of mammals, the enzyme inactivates the AHL signaling by hydrolysis of the lactone ring thus acting as quorum-quenching enzyme
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-3-oxododecanoyl-L-homoserine lactone + H2O
N-3-oxododecanoyl-L-homoserine
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additional information
?
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the h-PON1 can hydrolyze (and inactivate) a variety of substrates including aryl esters, thioesters, phosphotriesters, carbonates, lactones and thiolactones, and its various hydrolytic activities can be broadly grouped into three categories, namely arylesterase, organophosphatase, and lactonase. The native activity of h-PON1 seems to be lactonase. Polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme
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?
additional information
?
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acyl-homoserine lactone quorum-sensing signals play a key role in synchronizing virulence gene expression during bloodstream infections of mammals, the enzyme inactivates the AHL signaling by hydrolysis of the lactone ring thus acting as quorum-quenching enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-hydroxyquinoline
a specific reversible competitive inhibitor of h-PON1 that is known to bind in the active site of the enzyme and inhibit the hydrolytic activities of the enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the h-PON1 can hydrolyze (and inactivate) a variety of substrates including aryl esters, thioesters, phosphotriesters, carbonates, lactones and thiolactones, and its various hydrolytic activities can be broadly grouped into three categories, namely arylesterase, organophosphatase and lactonase. It has been suggested that the native activity of h-PON1 is lactonase. Polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme. The enzyme has been shown to possess anti-inflammatory, anti-oxidative, anti-diabetic and quorum sensor-hydrolyzing activities. It is proposed that the lactonase activity of enzyme is important for these defensive roles
additional information
h-PON1 is a polymorphic enzyme. Molecular docking analysis, homology modelling, overview
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). PON1_HUMAN
355
0
39731
Swiss-Prot
Secretory Pathway (Reliability: 4)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
features observed in the structure of PON1, i.e. the six-bladed beta-propeller scaffold, the three alpha-helices at the top of the propeller and the putative calcium-binding residues, are well conserved in the modelled structures
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H115W/R192K
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type
H115W/R192K/A137T
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type
H115W/R192K/A137T/D94H/S211T
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type
H115W/R192K/A137T/L130F
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type
H115W/R192K/A137T/M127I/D263H
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type
H115W/R192K/A137T/S81R/P165A
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type
L55M
natural polymorphism, the polymorphism at the 55th position of h-PON1 does not affect the catalytic properties of the enzyme
R192E
natural polymorphism, polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme
additional information
the h-PON1 is a polymorphic enzyme, and two polymorphisms are reported in the coding region of the enzyme: one at position 55 (Leu/Met) and the other at position 192 (Arg/Gln). It is observed that the polymorphism at the 55th position of h-PON1 does not affect the catalytic properties of the enzyme, while polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme. Random mutagenesis approach to increase the organophosphate (OP)-hydrolyzing activity of recombinant h-PON1, and mutant screening for OP-hydrolyzing activity. The mutants show a 10-340fold increased organophosphate-hydrolyzing activity against different organophosphate substrates but also exhibit differential lactonase and arylesterase activities compared to the wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PON1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, F.; Wang, L.H.; Wang, J.; Dong, Y.H.; Hu, J.Y.; Zhang, L.H.
Quorum quenching enzyme activity is widely conserved in the sera of mammalian species
FEBS Lett.
579
3713-3717
2005
Bos taurus, Capra hircus, Oryctolagus cuniculus, Equus caballus, Homo sapiens, Mus musculus, no activity in Gallus gallus, Capra hircus aiiA, Mus musculus aiiA, Oryctolagus cuniculus aiiA, Homo sapiens aiiA, Bos taurus aiiA, Equus caballus aiiA
EXTERNAL LINKS (specific for EC-Number 3.1.1.81)
Transporter Classification Database (TCDB): 1.A.6.2.6
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