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Information on EC 3.5.1.97 - acyl-homoserine-lactone acylase
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EC Tree
3.5.1.97 acyl-homoserine-lactone acylaseIUBMB 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. This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine lactone ring of AHL-dependent quorum-sensing signal molecules. It has broad specificity for AHLs with side changes ranging in length from 11 to 14 carbons. Substituents at the 3'-position, as found in N-(3-oxododecanoyl)-L-homoserine lactone, do not affect this activity.
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Word Map
- 3.5.1.97
- acylases
- lactonase
-
quorum-sensing
- penicillin
-
pectobacterium
- carotovorum
- pyocyanin
-
ahl-degrading
- ahl-acylase
- utahensis
-
actinoplanes
-
ahl-mediated
-
c12-hsl
-
3-oxo-c12-hsl
-
pyoverdine
- violacein
- atrosepticum
-
aculeacin
-
chromobacterium
-
ahl-dependent
- rhamnolipids
-
biofouling
- agriculture
- biotechnology
- drug development
- pharmacology
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
ahl acylase, quorum quenching enzyme, pa0305, papva, slpva, acyl-hsl acylase, pvdq acylase, pa2385, n-acylhomoserine lactone acylase, aptm01, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl-homoserine lactone acylase
AHL acylase
AHL amidase
AHL-acylase
AiiC
AiiD
AiiO
AmiE
APTM01
FaGL1422
HacA
HacB
N-acyl-homoserine lactone acylase
N-acylhomoserine lactone acylase
N-acylhomoserine lactone-acylase
pfmA
PvdQ
PvdQ acylase
QuiP
quorum quenching enzyme
quorum-quenching N-acylhomoserine lactone acylase
SlPVA
additional information
N-acyl-homoserine lactone acylase
-
encoded by the aac gene, a probable aculeacin A aclyase is a N-acyl-homoserine lactone acylase with quorum-quenching activity
quorum-quenching N-acylhomoserine lactone acylase
-
additional information
the enzyme belongs to the alpha/beta hydrolase superfamily
additional information
the enzyme belongs to the alpha/beta hydrolase superfamily
-
additional information
-
the enzyme belongs to the N-terminal nucleophile hydrolase superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an N-acyl-L-homoserine lactone + H2O = L-homoserine lactone + a carboxylate
-
-
-
-
an N-acyl-L-homoserine lactone + H2O = L-homoserine lactone + a carboxylate
AHL-acylase is a quorum quenching enzyme and degrades N-acylhomoserine lactones (AHLs) by removing the fatty acid side chain from the homoserine lactone ring of AHLs. This blocks AHL accumulation and pathogenic phenotypes in quorum sensing bacteria
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
N-acyl-L-homoserine-lactone amidohydrolase
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. This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine lactone ring of AHL-dependent quorum-sensing signal molecules. It has broad specificity for AHLs with side changes ranging in length from 11 to 14 carbons. Substituents at the 3'-position, as found in N-(3-oxododecanoyl)-L-homoserine lactone, do not affect this activity.
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CAS REGISTRY NUMBER
COMMENTARY
857396-91-9
-
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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-oxohexanoyl)-DL-homoserine lactone + H2O
homoserine lactone + 3-oxohexanoate
0.5 microM, assay at 28°C, pH 7.0, 1 h
-
-
?
N-(3-oxohexanoyl)-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoate
-
-
-
-
?
N-(3-oxooctanoyl)-DL-homoserine lactone + H2O
homoserine lactone + 3-oxooctanoate
0.5 microM, assay at 28°C, pH 7.0, 1 h
-
-
?
N-(3-oxooctanoyl)-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoate
-
-
-
-
?
N-(3-oxotetradecanoyl)-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxotetradecanoate
-
-
-
-
?
N-3-oxo-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxotetradecanoate
N-3-oxododecanoyl-(S)-homoserine lactone + H2O
(S)-homoserine + 3-oxododecanoic acid
-
-
-
-
?
N-3-oxooctanoyl-DL-homoserine lactone + H2O
homoserine lactone + 3-oxooctanoate
0.5 microM, assay at 28°C, pH 7.0, 3 h
-
-
?
N-3-oxotetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxotetradecanoic acid
N-butanoyl-L-homoserine lactone + H2O
L-homoserine lactone + butanoic acid
-
-
-
-
?
N-butyryl homoserine lactone + H2O
homoserine lactone + butanoate
0.5 microM, assay at 28°C, pH 7.0, 1 h
-
-
?
N-decanoyl-DL-homoserine lactone + H2O
DL-homoserine lactone + decanoate
-
-
-
-
?
N-dodecanoyl-(S)-homoserine lactone + H2O
(S)-homoserine + dodecanoic acid
-
-
-
-
?
N-dodecanoyl-DL-homoserine lactone + H2O
DL-homoserine lactone + dodecanoate
-
-
-
-
?
N-heptanoyl-(S)-homoserine lactone + H2O
(S)-homoserine + heptanoic acid
-
-
-
-
?
N-heptanoyl-DL-homoserine lactone + H2O
DL-homoserine lactone + heptanoate
-
-
-
-
?
N-hexanoyl-DL-homoserine lactone + H2O
homoserine lactone + hexanoate
0.5 microM, assay at 28°C, pH 7.0, 1 h
-
-
?
N-octanoyl-(S)-homoserine lactone + H2O
(S)-homoserine + octanoic acid
-
-
-
-
?
N-octanoyl-DL-homoserine lactone + H2O
DL-homoserine lactone + octanoate
-
-
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + N-octanoic acid
-
-
-
-
?
N-tetradecanoyl-(S)-homoserine lactone + H2O
(S)-homoserine + tetradecanoic acid
-
-
-
-
?
N-tetradecanoyl-DL-homoserine lactone + H2O
DL-homoserine lactone + tetradecanoate
-
-
-
-
?
N-undecanoyl-(S)-homoserine lactone + H2O
(S)-homoserine + undecanoic acid
-
-
-
-
?
N-(3-oxodecanoyl)-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoate
-
-
-
?
N-(3-oxodecanoyl)-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoate
-
-
-
?
N-(3-oxodecanoyl)-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoate
-
-
-
-
?
N-(3-oxododecanoyl)-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoate
-
-
-
?
N-(3-oxododecanoyl)-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoate
-
-
-
?
N-(3-oxododecanoyl)-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoate
-
-
-
-
?
N-(3-oxohexanoyl)-L-homoserine lactone + H2O
homoserine lactone + 3-oxohexanoate
-
rapid degradation (more than 40% after 15 min)
-
-
?
N-(3-oxohexanoyl)-L-homoserine lactone + H2O
homoserine lactone + 3-oxohexanoate
-
rapid degradation (more than 40% after 15 min)
-
-
?
N-(3-oxooctanoyl)-L-homoserine lactone + H2O
homoserine lactone + 3-oxooctanoate
-
rapid degradation (more than 40% after 15 min, completely degraded after 120 min)
-
-
?
N-(3-oxooctanoyl)-L-homoserine lactone + H2O
homoserine lactone + 3-oxooctanoate
-
rapid degradation (more than 40% after 15 min, completely degraded after 120 min)
-
-
?
N-3-oxo-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoate
-
-
-
-
?
N-3-oxo-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoate
-
-
-
?
N-3-oxo-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoate
-
-
-
-
?
N-3-oxo-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoate
-
-
-
?
N-3-oxo-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoate
-
-
-
?
N-3-oxo-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoate
-
-
-
?
N-3-oxo-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoate
-
-
-
-
?
N-3-oxo-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoate
-
-
-
-
?
N-3-oxo-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxo-octanoate
-
-
-
-
?
N-3-oxo-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxo-octanoate
-
-
-
-
?
N-3-oxo-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxotetradecanoate
-
-
-
-
?
N-3-oxo-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxotetradecanoate
-
-
-
?
N-3-oxobutanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxobutanoic acid
-
-
-
-
?
N-3-oxobutanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxobutanoic acid
-
-
-
-
?
N-3-oxobutanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxobutanoic acid
-
-
-
?
N-3-oxodecanoyl-(S)-homoserine lactone + H2O
(S)-homoserine lactone + 3-oxodecanoic acid
-
-
-
-
?
N-3-oxodecanoyl-(S)-homoserine lactone + H2O
(S)-homoserine lactone + 3-oxodecanoic acid
-
hydrolysis of the amide bond
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
Pseudomonas syringae B728a
-
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
-
?
N-3-oxodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoic acid
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
Pseudomonas syringae B728a
-
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
-
?
N-3-oxododecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoic acid
-
-
-
?
N-3-oxoheptanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxoheptanoic acid
-
-
-
?
N-3-oxoheptanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxoheptanoic acid
-
-
-
?
N-3-oxohexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoic acid
-
-
-
-
?
N-3-oxohexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoic acid
-
-
-
-
?
N-3-oxohexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoic acid
-
-
-
-
?
N-3-oxohexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoic acid
-
-
-
-
?
N-3-oxohexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoic acid
-
-
-
-
?
N-3-oxohexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoic acid
Pseudomonas syringae B728a
-
-
-
-
?
N-3-oxohexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoic acid
-
-
-
-
?
N-3-oxohexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoic acid
-
-
-
-
?
N-3-oxohexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoic acid
-
-
-
-
?
N-3-oxohexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoic acid
Variovorax paradoxus VAI-C
-
-
-
-
?
N-3-oxohexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoic acid
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
-
?
N-3-oxooctanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxooctanoic acid
-
-
-
?
N-3-oxotetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxotetradecanoic acid
-
-
-
-
?
N-3-oxotetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxotetradecanoic acid
-
-
-
-
?
N-3-oxotetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxotetradecanoic acid
-
-
-
?
N-3-oxotetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxotetradecanoic acid
-
-
-
?
N-3-oxotetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxotetradecanoic acid
-
-
-
?
N-acyl-(S)-homoserine lactone + H2O
(S)-homoserine lactone + carboxylic acid
-
-
-
-
?
N-acyl-(S)-homoserine lactone + H2O
(S)-homoserine lactone + carboxylic acid
-
-
-
-
?
N-acyl-(S)-homoserine lactone + H2O
(S)-homoserine lactone + carboxylic acid
-
specificity for the degradation of long-acyl-chain acyl-homoserine-lactones
-
-
?
N-acyl-(S)-homoserine lactone + H2O
(S)-homoserine lactone + carboxylic acid
-
inactivation of N-acylhomoserine lactone signaling in regulation of infection and virulence functions
-
-
?
N-butanoyl-L-homoserine lactone + H2O
L-homoserine lactone + butanoate
10 microM, assay at 30°C, shaking, reaction stopped by incubation at 95°C for 5 min
-
-
?
N-butanoyl-L-homoserine lactone + H2O
L-homoserine lactone + butanoate
10 microM, assay at 30°C, shaking, reaction stopped by incubation at 95°C for 5 min
-
-
?
N-butyryl-L-homoserine lactone + H2O
L-homoserine lactone + butyric acid
-
-
-
-
?
N-butyryl-L-homoserine lactone + H2O
L-homoserine lactone + butyric acid
Variovorax paradoxus VAI-C
-
-
-
-
?
N-decanoyl-DL-homoserine lactone + H2O
homoserine lactone + decanoate
0.5 microM, assay at 28°C, pH 7.0, 1 h
-
-
?
N-decanoyl-DL-homoserine lactone + H2O
homoserine lactone + decanoate
0.5 microM, assay at 28°C, pH 7.0, 3 h
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
10 microM, assay at 30°C, shaking, reaction stopped by incubation at 95°C for 5 min
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
10 microM, assay at 30°C, shaking, reaction stopped by incubation at 95°C for 5 min
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
Pseudomonas syringae B728a
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
Tenacibaculum maritimum NCIMB 2154(T)
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoic acid
Variovorax paradoxus VAI-C
-
-
-
-
?
N-dodecanoyl-DL-homoserine lactone + H2O
homoserine lactone + dodecanoate
0.5 microM, assay at 28°C, pH 7.0, 1 h
-
-
?
N-dodecanoyl-DL-homoserine lactone + H2O
homoserine lactone + dodecanoate
0.5 microM, assay at 28°C, pH 7.0, 3 h
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
-
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
10 microM, assay at 30°C, shaking, reaction stopped by incubation at 95°C for 5 min
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
10 microM, assay at 30°C, shaking, reaction stopped by incubation at 95°C for 5 min
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoic acid
-
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoic acid
-
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoic acid
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoic acid
-
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoic acid
Pseudomonas syringae B728a
-
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoic acid
-
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoic acid
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoic acid
-
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoic acid
Variovorax paradoxus VAI-C
-
-
-
-
?
N-heptanoyl-L-homoserine lactone + H2O
L-homoserine lactone + heptanoic acid
-
-
-
?
N-heptanoyl-L-homoserine lactone + H2O
L-homoserine lactone + heptanoic acid
-
-
determined by ESI-MS analysis
-
?
N-heptanoyl-L-homoserine lactone + H2O
L-homoserine lactone + heptanoic acid
-
-
-
-
?
N-heptanoyl-L-homoserine lactone + H2O
L-homoserine lactone + heptanoic acid
-
-
-
-
?
N-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + hexanoate
-
-
-
-
?
N-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + hexanoate
-
-
-
-
?
N-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + hexanoate
-
-
-
?
N-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + hexanoate
-
-
-
?
N-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + hexanoate
10 microM, assay at 30°C, shaking, reaction stopped by incubation at 95°C for 5 min
-
-
?
N-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + hexanoate
10 microM, assay at 30°C, shaking, reaction stopped by incubation at 95°C for 5 min
-
-
?
N-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + hexanoic acid
-
-
-
?
N-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + hexanoic acid
-
-
-
-
?
N-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + hexanoic acid
-
-
-
-
?
N-octanoyl-DL-homoserine lactone + H2O
homoserine lactone + octanoate
0.5 microM, assay at 28°C, pH 7.0, 1 h
-
-
?
N-octanoyl-DL-homoserine lactone + H2O
homoserine lactone + octanoate
0.5 microM, assay at 28°C, pH 7.0, 3 h
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoate
-
-
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoate
-
-
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoate
10 microM, assay at 30°C, shaking, reaction stopped by incubation at 95°C for 5 min
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoate
10 microM, assay at 30°C, shaking, reaction stopped by incubation at 95°C for 5 min
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoic acid
-
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoic acid
-
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoic acid
-
-
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoic acid
-
-
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoic acid
-
-
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoic acid
-
-
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoic acid
-
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoic acid
-
-
-
-
?
N-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + octanoic acid
Variovorax paradoxus VAI-C
-
-
-
-
?
N-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + tetradecanoate
-
-
-
?
N-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + tetradecanoate
-
-
-
?
N-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + tetradecanoate
-
-
-
?
N-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + tetradecanoate
-
-
-
?
N-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + tetradecanoic acid
-
-
-
?
N-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + tetradecanoic acid
-
-
-
-
?
N-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + tetradecanoic acid
-
-
-
-
?
additional information
?
-
-
enzyme MacQ has the bifunctional capacity to degrade both AHL and beta-lactam antibiotics by deacylation activity (cf. EC 3.5.2.6). MacQ is able to inactivate a variety of beta-lactams, including penicillin derivatives (penicillin G, ampicillin, amoxicillin, and carbenicillin) and cephalosporin derivatives (cephalexin and cefadroxil)
-
-
-
additional information
?
-
-
the enzyme is also active with substrate penicillin G and able to inactivate a variety of beta-lactams, including penicillin derivatives (penicillin G, ampicillin, amoxicillin, and carbenicillin) and cephalosporin derivatives (cephalexin and cefadroxil). Enzyme reaction metabolites identification using gas chromatography. MacQ show a much broader substrate specificity than two AHL acylases (AhlM and KcPGA) known to degrade penicillin G, overview
-
-
-
additional information
?
-
the enzyme shows a high level of degrading activity against N-acyl-L-homoserine lactones with long acyl chains but no activity against N-acyl-L-homoserine lactones with acyl chains shorter than eight carbons
-
-
?
additional information
?
-
-
the enzyme shows a high level of degrading activity against N-acyl-L-homoserine lactones with long acyl chains but no activity against N-acyl-L-homoserine lactones with acyl chains shorter than eight carbons
-
-
?
additional information
?
-
-
screening for the AHL-degrading properties in AHL-bioassay with biosensor strain Chromobacterium violaceum CV026
-
-
-
additional information
?
-
-
N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs
-
-
?
additional information
?
-
N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs
-
-
?
additional information
?
-
-
N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs
-
-
?
additional information
?
-
N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs
-
-
?
additional information
?
-
the marine bacterium Pseudoalteromonas flavipulchra strain JG1 can degrade N-acylhomoserine lactones (AHLs). PfmA can degrade ampicillin but not penicillin G. The concentration of AHLs in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1 is reduced when 0.01 mg/ml PfmA is present
-
-
-
additional information
?
-
-
the marine bacterium Pseudoalteromonas flavipulchra strain JG1 can degrade N-acylhomoserine lactones (AHLs). PfmA can degrade ampicillin but not penicillin G. The concentration of AHLs in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1 is reduced when 0.01 mg/ml PfmA is present
-
-
-
additional information
?
-
enzyme AHL acylase PfmA can degrade N-acylhomoserine lactones (AHLs) with acyl chains longer than 10 carbons. PfmA can degrade ampicillin but not penicillin G. No activity with N-hexanoyl-L-homoserine lactone, N-3-oxo-hexanoyl-L-homoserine lactone, N-octanoyl-L-homoserine lactone, and N-3-oxo-octanoyl-L-homoserine lactone
-
-
-
additional information
?
-
-
enzyme AHL acylase PfmA can degrade N-acylhomoserine lactones (AHLs) with acyl chains longer than 10 carbons. PfmA can degrade ampicillin but not penicillin G. No activity with N-hexanoyl-L-homoserine lactone, N-3-oxo-hexanoyl-L-homoserine lactone, N-octanoyl-L-homoserine lactone, and N-3-oxo-octanoyl-L-homoserine lactone
-
-
-
additional information
?
-
the marine bacterium Pseudoalteromonas flavipulchra strain JG1 can degrade N-acylhomoserine lactones (AHLs). PfmA can degrade ampicillin but not penicillin G. The concentration of AHLs in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1 is reduced when 0.01 mg/ml PfmA is present
-
-
-
additional information
?
-
-
the marine bacterium Pseudoalteromonas flavipulchra strain JG1 can degrade N-acylhomoserine lactones (AHLs). PfmA can degrade ampicillin but not penicillin G. The concentration of AHLs in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1 is reduced when 0.01 mg/ml PfmA is present
-
-
-
additional information
?
-
enzyme AHL acylase PfmA can degrade N-acylhomoserine lactones (AHLs) with acyl chains longer than 10 carbons. PfmA can degrade ampicillin but not penicillin G. No activity with N-hexanoyl-L-homoserine lactone, N-3-oxo-hexanoyl-L-homoserine lactone, N-octanoyl-L-homoserine lactone, and N-3-oxo-octanoyl-L-homoserine lactone
-
-
-
additional information
?
-
-
enzyme AHL acylase PfmA can degrade N-acylhomoserine lactones (AHLs) with acyl chains longer than 10 carbons. PfmA can degrade ampicillin but not penicillin G. No activity with N-hexanoyl-L-homoserine lactone, N-3-oxo-hexanoyl-L-homoserine lactone, N-octanoyl-L-homoserine lactone, and N-3-oxo-octanoyl-L-homoserine lactone
-
-
-
additional information
?
-
no activity with N-3-oxo-octanoyl-L-homoserine lactone, and N-3-oxo-decanoyl-L-homoserine lactone, N-hexanoyl-L-homoserine lactone is a poor substrate
-
-
-
additional information
?
-
-
no activity with N-3-oxo-octanoyl-L-homoserine lactone, and N-3-oxo-decanoyl-L-homoserine lactone, N-hexanoyl-L-homoserine lactone is a poor substrate
-
-
-
additional information
?
-
no activity with N-3-oxo-octanoyl-L-homoserine lactone, and N-3-oxo-decanoyl-L-homoserine lactone, N-hexanoyl-L-homoserine lactone is a poor substrate
-
-
-
additional information
?
-
-
virulence of the opportunistic human pathogen is controlled by the N-acyl-homoserine lactone, AHL-dependent quorum-sensing system, the enzyme inactivates AHLs by hydrolysis of the carboxylic side chain with side chain ranging from 11 to 14 C-atoms with broad range specificity, addition of the purified enzyme to cell cultures results in complete inhibition of N-3-oxododecanoyl-(S)-homoserine lactone accumulation and production of the signal molecule 2-heptyl-3-hydroxy-4(1H)-quinolone, as well as reduced production of virulence factors elastase and procyanin
-
-
?
additional information
?
-
-
N-acyl-homoserine lactone substrate specificity, no activity with N-butanoyl-(S)-homoserine lactone, N-hexanoyl-(S)-homoserine lactone, and N-3-oxohexanoyl-(S)-homoserine lactone, overview
-
-
?
additional information
?
-
-
no activity towards N-butanoyl-DL-homoserine lactone
-
-
?
additional information
?
-
-
PA0305 degrades N-acyl-homoserine lactones with acyl side chains ranging in length from 6 to 14 carbons
-
-
?
additional information
?
-
-
a modified homoserine lactone-o-phthaldialdehyde (HSL-OPA) assay is used to quantify the recombinant AHL acylase activity. No activity is observed with short chain N-acylhomoserine lactones (AHLs), i.e. N-butanoyl-L-homoserine lactone, N-hexanoyl-L-homoserine, or N-(3-oxohexanoyl)-L-homoserine lactone. AHLs of more than ten carbon-acyl chains, i.e. N-decanoyl-L-homoserine lactone and N-dodecanoyl-L-homoserine lactone can not be determined due to their poor solubility
-
-
?
additional information
?
-
-
since the aac gene is predicted as a probable aculeacin A acylase aculeacin A is tested as substrate. The possible products i.e. palmatic acid is not found in the ESI-MS analysis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-oxo-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxodecanoate
-
-
-
?
N-3-oxo-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxohexanoate
-
-
-
-
?
N-3-oxo-octanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxo-octanoate
-
-
-
-
?
N-3-oxo-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxotetradecanoate
-
-
-
?
N-3-oxododecanoyl-(S)-homoserine lactone + H2O
(S)-homoserine + 3-oxododecanoic acid
-
-
-
-
?
N-acyl-(S)-homoserine lactone + H2O
(S)-homoserine lactone + carboxylic acid
-
inactivation of N-acylhomoserine lactone signaling in regulation of infection and virulence functions
-
-
?
N-dodecanoyl-(S)-homoserine lactone + H2O
(S)-homoserine + dodecanoic acid
-
-
-
-
?
N-hexanoyl-L-homoserine lactone + H2O
L-homoserine lactone + hexanoate
-
-
-
-
?
N-tetradecanoyl-(S)-homoserine lactone + H2O
(S)-homoserine + tetradecanoic acid
-
-
-
-
?
N-undecanoyl-(S)-homoserine lactone + H2O
(S)-homoserine + undecanoic acid
-
-
-
-
?
N-3-oxo-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoate
-
-
-
?
N-3-oxo-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoate
-
-
-
?
N-3-oxo-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + 3-oxododecanoate
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
L-homoserine lactone + decanoate
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + dodecanoate
-
-
-
?
N-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + tetradecanoate
-
-
-
?
N-tetradecanoyl-L-homoserine lactone + H2O
L-homoserine lactone + tetradecanoate
-
-
-
?
additional information
?
-
-
enzyme MacQ has the bifunctional capacity to degrade both AHL and beta-lactam antibiotics by deacylation activity (cf. EC 3.5.2.6). MacQ is able to inactivate a variety of beta-lactams, including penicillin derivatives (penicillin G, ampicillin, amoxicillin, and carbenicillin) and cephalosporin derivatives (cephalexin and cefadroxil)
-
-
-
additional information
?
-
the enzyme shows a high level of degrading activity against N-acyl-L-homoserine lactones with long acyl chains but no activity against N-acyl-L-homoserine lactones with acyl chains shorter than eight carbons
-
-
?
additional information
?
-
-
the enzyme shows a high level of degrading activity against N-acyl-L-homoserine lactones with long acyl chains but no activity against N-acyl-L-homoserine lactones with acyl chains shorter than eight carbons
-
-
?
additional information
?
-
-
N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs
-
-
?
additional information
?
-
N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs
-
-
?
additional information
?
-
-
N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs
-
-
?
additional information
?
-
N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs
-
-
?
additional information
?
-
the marine bacterium Pseudoalteromonas flavipulchra strain JG1 can degrade N-acylhomoserine lactones (AHLs). PfmA can degrade ampicillin but not penicillin G. The concentration of AHLs in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1 is reduced when 0.01 mg/ml PfmA is present
-
-
-
additional information
?
-
-
the marine bacterium Pseudoalteromonas flavipulchra strain JG1 can degrade N-acylhomoserine lactones (AHLs). PfmA can degrade ampicillin but not penicillin G. The concentration of AHLs in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1 is reduced when 0.01 mg/ml PfmA is present
-
-
-
additional information
?
-
the marine bacterium Pseudoalteromonas flavipulchra strain JG1 can degrade N-acylhomoserine lactones (AHLs). PfmA can degrade ampicillin but not penicillin G. The concentration of AHLs in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1 is reduced when 0.01 mg/ml PfmA is present
-
-
-
additional information
?
-
-
the marine bacterium Pseudoalteromonas flavipulchra strain JG1 can degrade N-acylhomoserine lactones (AHLs). PfmA can degrade ampicillin but not penicillin G. The concentration of AHLs in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1 is reduced when 0.01 mg/ml PfmA is present
-
-
-
additional information
?
-
-
virulence of the opportunistic human pathogen is controlled by the N-acyl-homoserine lactone, AHL-dependent quorum-sensing system, the enzyme inactivates AHLs by hydrolysis of the carboxylic side chain with side chain ranging from 11 to 14 C-atoms with broad range specificity, addition of the purified enzyme to cell cultures results in complete inhibition of N-3-oxododecanoyl-(S)-homoserine lactone accumulation and production of the signal molecule 2-heptyl-3-hydroxy-4(1H)-quinolone, as well as reduced production of virulence factors elastase and procyanin
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
no effect on enzyme activity by 2 mM of Na+, K+, Mg2+, and Ca2+
additional information
Na+, K+, Ca2+, Fe3+, and Cu2+ show no or poor effects on AHL acylase activity at 1 mM
additional information
-
Na+, K+, Ca2+, Fe3+, and Cu2+ show no or poor effects on AHL acylase activity at 1 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cataract
Prediction of postoperative complications of pediatric cataract patients using data mining.
Infections
Marine-Source Quorum Quenching Enzyme YtnP to Improve Hygiene Quality in Dental Units.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics and thermodynamics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
78
N-(3-oxododecanoyl)-L-homoserine lactone
-
in 0.1 M phosphate buffer pH 7.4, at 30°C
1.4
N-octanoyl-L-homoserine lactone
-
in 0.1 M phosphate buffer pH 7.4, at 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
over 50% of maximal activity at pH 5.0-11.0, 40% at pH 4.0, profile overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 80
over 40% of maximal activity at 20-80°C, profile overview
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from activated sludge in a penicillin G production wastewater treatment system
-
-
brenda
the virulence of Pseudomonas aeruginosa PAO1 is analyzed in a Caenorhabditis elegans infection model
-
-
brenda
an important soil-borne plant pathogen with an extensive host range
-
-
brenda
strain B728a, strain BHSL, strain HacA-, strain HacB-, strain HacA-B-
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
the culture medium pH of Delftia sp. strain VM4 increases from pH 7.2 to pH 7.8 within 6 h
brenda
additional information
-
in the Caenorhabditis elegans infection model it is observed that larval stage 1 to 3 benefit much more from the protection by PvdQ than larval stage 4 worms
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the first 24 residues of MacQ are predicted to be a signal sequence
-
brenda
PfmA lacks an N-terminal signal peptide and no activity is found in the cell medium
brenda
-
PfmA lacks an N-terminal signal peptide and no activity is found in the cell medium
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
-
virulence gene expression in many Gram-negative pathogens generally is under quorum sensing control. In particular, quorum-sensing plays an important role in the regulation of virulence genes (mainly plant cell wall degrading enzymes, PCWDEs, production) in phytopathogenic soft rot causing Pectobacterium species. Also the N-acylhomoserine lactone (AHL) based quorum sensing in soft rot Pectobacterium species tightly regulates the activities implicated in microbial competition and host-pathogen interaction. These activities require various microbial functions such as biofilm formation, expression of virulence factors, antibiotic production etc.
physiological function
additional information
evolution
the enzyme belongs to the amidase family. AmiE shows homology with a member of the amidases (EC 3.5.1.4) but not with any known AHL acylase enzymes. An amino acid sequence of AmiE from Ooi24 shows greater than 99% identities with uncharacterized proteins from Acinetobacter ursingii CIP 107286 and Acinetobacter sp. strain CIP 102129, but it is not found in the draft or complete genome sequences of other Acinetobacter strains. Phylogenetic relationship between AmiE and known AHL acylases and phylogenetic tree
evolution
enzyme PfmA belongs to the N-terminal nucleophile (Ntn) hydrolase superfamily and shows homology to a member of penicillin amidases, but PfmA can degrade ampicillin but not penicillin G
evolution
the acylase gene APTM01 from the strain MQS005 belongs to PvdQ type on sub-branch in phylogenetic tree
evolution
-
the enzyme shows an AHL acylase type mode of action. It possesses similarity with an alpha/beta-hydrolase fold protein, which makes it unique among the known AHL acylases with domains of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Phylogenetic analysis of isolate VM4 within the genus Delftia
evolution
-
enzyme PfmA belongs to the N-terminal nucleophile (Ntn) hydrolase superfamily and shows homology to a member of penicillin amidases, but PfmA can degrade ampicillin but not penicillin G
-
evolution
-
the acylase gene APTM01 from the strain MQS005 belongs to PvdQ type on sub-branch in phylogenetic tree
-
physiological function
-
PvdQ functions as a quorum quencher in vitro. Purified PvdQ is added to Caenorhabditis elegans worms infected with wild-type PAO1 and this results in reduced pathogenicity and increases the life span of the nematodes. PvdQ might be a strong candidate for antibacterial therapy against Pseudomonas infections
physiological function
the organism inactivates N-acyl homoserine lactone quorum sensing signal molecules and is capable of quenching the N-acyl homoserine lactone, AHL-dependent virulence of Pectobacterium carotovorum in planta via its AHL inactivating activity
physiological function
the enzyme is capable of quenching the N-acyl-homoserine lactone-dependent virulence of Pectobacterium carotovorum in planta
physiological function
the enzyme hydrolyzes the amide bond of N-acyl-L-homoserine lactones, quorum-sensing signal molecules. The recombinant enzyme in Pseudomonas aeruginosa PAO1 reduces N-acyl-L-homoserine lactone accumulation and elastase activity, which are regulated by AHL-mediated quorum sensing
physiological function
-
Delftia sp. VM4 can degrade exogenous N-acyl homoserine lactone (AHL), hence it effectively attenuates the virulence of bacterial soft rot pathogen Pectobacterium carotovorum subsp. carotovorum strain BR1 (Pcc BR1) as a consequence of quorum sensing inhibition. Interference of quorum sensing by Delftia sp. VM4 depends on the activity of the N-acylhomoserine lactone-acylase. Delftia sp. VM4 interferes with quorum-sensing signaling of Pcc BR1 when they live commensally in vitro, and such signal interruption causes drastic attenuation of Pcc BR1 virulence determinants. Delftia sp. VM4 cells do not produce an antibiotic-like material to hinder the growth of Pcc BR1
physiological function
enzyme PfmA reduces N-acylhomoserine lactone (AHL) accumulation and the production of virulence factors in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1, and attenuates the virulence of Pseudomonas aeruginosa to increase Artemia survival, which suggests that PfmA can be considered as a therapeutic agent to control AHL-mediated pathogenicity. N-acylhomoserine lactone acylase is a quorum-quenching enzyme. Quorum sensing (QS) is a cell-to-cell communication mechanism dependent on cell density, which allows bacterial populations to regulate the expression of genes responsible for a wide range of biological behaviours, such as the production of pigments, biofilm formation, antibiotic production, motility, adhesion, bioluminescence and secretion of virulence factors
physiological function
-
MacQ is a bifunctional enzyme that confers both quorum quenching and antibiotic resistance on strain MRS7. Enzyme N-acylhomoserine lactone acylase (AHL acylase) is responsible for disrupting cell-cell communication (quorum sensing) in bacteria. AHL-mediated virulence factor production in a plant pathogen, Pectobacterium carotovorum, is dramatically attenuated by coculture with MacQ-overexpressing Escherichia coli Origami 2(DE3), whereas Escherichia coli with an empty vector is unable to quench the pathogenicity. MacQ acts as a quorum-quenching enzyme and disrupts the quorum-sensing system in the pathogen. Recombinant MacQ confers multiple beta-lactam antibiotic resistance on an Escherichia coli host strain by hydrolyzing beta-lactam antibiotics
physiological function
the marine bacteria of Pseudoalteromonas has wide activity of degrading AHLs as a type of signal molecule associated with quorum sensing
physiological function
-
the enzyme is capable of quenching the N-acyl-homoserine lactone-dependent virulence of Pectobacterium carotovorum in planta
-
physiological function
-
the organism inactivates N-acyl homoserine lactone quorum sensing signal molecules and is capable of quenching the N-acyl homoserine lactone, AHL-dependent virulence of Pectobacterium carotovorum in planta via its AHL inactivating activity
-
physiological function
-
enzyme PfmA reduces N-acylhomoserine lactone (AHL) accumulation and the production of virulence factors in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1, and attenuates the virulence of Pseudomonas aeruginosa to increase Artemia survival, which suggests that PfmA can be considered as a therapeutic agent to control AHL-mediated pathogenicity. N-acylhomoserine lactone acylase is a quorum-quenching enzyme. Quorum sensing (QS) is a cell-to-cell communication mechanism dependent on cell density, which allows bacterial populations to regulate the expression of genes responsible for a wide range of biological behaviours, such as the production of pigments, biofilm formation, antibiotic production, motility, adhesion, bioluminescence and secretion of virulence factors
-
physiological function
-
the marine bacteria of Pseudoalteromonas has wide activity of degrading AHLs as a type of signal molecule associated with quorum sensing
-
additional information
-
Delftia sp. VM4 enzyme structure model of alpha/beta-hydrolase fold protein, overview
additional information
residue Ser256 in PfmA is the active site residue and residues Arg528, Asn324, His278 and Leu279 also play important roles in the catalytic process. Ser356 is also the first amino acid of the beta-subunit
additional information
-
residue Ser256 in PfmA is the active site residue and residues Arg528, Asn324, His278 and Leu279 also play important roles in the catalytic process. Ser356 is also the first amino acid of the beta-subunit
additional information
-
residue Ser256 in PfmA is the active site residue and residues Arg528, Asn324, His278 and Leu279 also play important roles in the catalytic process. Ser356 is also the first amino acid of the beta-subunit
-
Show AA Sequence and Transmembrane Helices (839 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
-
1 * 26000 (C-terminally processed alpha-subunit) + 1 * 60000 (beta-subunit), SDS-PAGE
60000
60000
-
1 * 26000 (C-terminally processed alpha-subunit) + 1 * 60000 (beta-subunit), SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
additional information
heterodimer
-
1 * 20000, alpha-subunit, + 1 * 62000, beta-subunit, SDS-PAGE, recombinant enzyme
heterodimer
1 * 26000, alpha-subunit, + 1 * 68000, beta-subunit, His6-tagged recombinant enzyme, SDS-PAGE
heterodimer
-
1 * 26000, alpha-subunit, + 1 * 68000, beta-subunit, His6-tagged recombinant enzyme, SDS-PAGE
-
heterodimer
-
1 * 26000 (C-terminally processed alpha-subunit) + 1 * 60000 (beta-subunit), SDS-PAGE
additional information
-
peptide mass fingerprinting analysis of the active protein band (from native PAGE) possessing AHL degrading activity, peptide sequence comparisons, overview
additional information
second-structure analysis of PfmA shows that the protein includes an alpha subunit, a spacer sequence, and a beta subunit. The alpha subunit of PfmA is predicted to have seven alpha helices, two beta folds and three random coils, while the beta subunit is predicted to have 12 alpha helices, 19 beta folds and eight random coils
additional information
-
second-structure analysis of PfmA shows that the protein includes an alpha subunit, a spacer sequence, and a beta subunit. The alpha subunit of PfmA is predicted to have seven alpha helices, two beta folds and three random coils, while the beta subunit is predicted to have 12 alpha helices, 19 beta folds and eight random coils
additional information
-
second-structure analysis of PfmA shows that the protein includes an alpha subunit, a spacer sequence, and a beta subunit. The alpha subunit of PfmA is predicted to have seven alpha helices, two beta folds and three random coils, while the beta subunit is predicted to have 12 alpha helices, 19 beta folds and eight random coils
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
post-translational modification is performed prior to PfmA becoming an active enzyme
proteolytic modification
-
post-translational modification is performed prior to PfmA becoming an active enzyme
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.8 A resolution. PvdQ has a typical alpha/beta heterodimeric Ntn-hydrolase fold. It has a large, hydrophobic binding pocket, ideally suited to recognize C12 fatty acid-like chains of N-acylhomoserine lactones. Binding of a C12 fatty acid or a 3-oxo-C12 fatty acid induces subtle conformational changes to accommodate the aliphatic chain. PvdQ is the first structurally characterized Ntn-hydrolase within this family to have any disulfide bridges. The disulfides are located in both the alpha- and beta-chain on the periphery of the protein
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H278S
site-directed mutagenesis, the mutant shows 80% reduced activity compared to wild-type
L279S
site-directed mutagenesis, the mutant shows 74% reduced activity compared to wild-type
H278S
-
site-directed mutagenesis, the mutant shows 80% reduced activity compared to wild-type
-
L279S
-
site-directed mutagenesis, the mutant shows 74% reduced activity compared to wild-type
-
additional information
additional information
-
AHL-mediated virulence factor production in a plant pathogen, Pectobacterium carotovorum, is dramatically attenuated by coculture with MacQ-overexpressing Escherichia coli Origami 2(DE3), whereas Escherichia coli with an empty vector is unable to quench the pathogenicity
additional information
-
random transposon mutagenesis, screening of the resulting mutants for the loss of AHL acylase activity. The Tn insertion in mutant A6731 is mapped to a gene termed aiiO
additional information
random transposon mutagenesis, screening of the resulting mutants for the loss of AHL acylase activity. The Tn insertion in mutant A6731 is mapped to a gene termed aiiO
additional information
-
random transposon mutagenesis, screening of the resulting mutants for the loss of AHL acylase activity. The Tn insertion in mutant A6731 is mapped to a gene termed aiiO
-
additional information
-
the strain PAO1-DELTApvd is shown to be more virulent than the wild-type strain, confirming the role of PvdQ as a virulence-reducing agent
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 30
purified recombinant enzyme, completely stable at
40
purified recombinant enzyme, 40% activity remaining
50
purified recombinant enzyme, 30% activity remaining
60
purified recombinant enzyme, 10% activity remaining
70
purified recombinant enzyme, 5% activity remaining
80
purified recombinant enzyme, no activity remaining
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a two-step purification protocol, anion exchange chromatography and hydrophobic interaction chromatography
-
gene macQ, recombinant His-tagged enzyme from Escherichia coli strain Origami 2(DE3) by nickel affinity chromatography
-
native enzyme 155.8fold from strain VM4 by ammonium sulfate fractionation, dialysis, anion exchange chromatography, ultrafiltration, and gel filtration
-
recombinant enzyme from Escherichia coli strain DH10B by several chromatographic steps
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli strain BL21 and in Vibrio anguillarum strain TB0008
gene aiiD, DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain DH5alpha, expression of AiiD in Pseudomonas aeruginosa strain PAO1 without showing catalytic function, but reducing the ability of the bacterium to exhibit quorum-regulated swarming motility, the bacterium is attenuated in nematode killing
-
gene aiiO, DNA and amino acid sequence determination and analysis, sequence comparisons, complementation of the aiiO::Tn5 mutation with the wild-type aiiO gene, expressionin Escherichia coli strain BL21(DE3)
gene amiE, from genomic library, DNA and amino acid sequence determination and analysis, phylogenetic tree, sequence comparisons, amiE is transferred by a putative transposon, cloning in Escherichia coli strain DHalpha, recombinant expression in Pseudomonas aeruginosa strain PAO1 leading to reduced N-acyl-L-homoserine lactone accumulation and elastase activity
gene macQ, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic and analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain Origami 2(DE3). Recombinant plasmid (pMQ28) confers 2 to 16fold higher MIC values toward all six beta-lactam antibiotics in Escherichia coli Origami 2(DE3) than the strain with a control vector. This indicates that MacQ confers multiple beta-lactam antibiotic resistance on a host strain by hydrolyzing beta-lactam antibiotics
-
gene pfmA, sequence comparisons, cloning of PfmA and recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene pvdQ, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree, genetic structure analysis, recombinant expression in Escherichia coli strain BL21
expression in Escherichia coli strain BL21 and in Vibrio anguillarum strain TB0008
expression in Escherichia coli strain BL21 and in Vibrio anguillarum strain TB0008
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
drug development
medicine
pharmacology
additional information
agriculture
effective in quenching quorum sensing of fish pathogens
agriculture
may be used to degrade pathogenic biofilms in fish intestines
drug development
therapeutic efficacy of PvdQ acylase as a quorum quenching agent during Pseudomonas aeruginosa infection (mouse model of pulmonary Pseudomonas aeruginosa infection)
drug development
-
therapeutic efficacy of PvdQ acylase as a quorum quenching agent during Pseudomonas aeruginosa infection (mouse model of pulmonary Pseudomonas aeruginosa infection)
-
medicine
therapeutic efficacy of PvdQ acylase as a quorum quenching agent during Pseudomonas aeruginosa infection (mouse model of pulmonary Pseudomonas aeruginosa infection)
medicine
-
therapeutic efficacy of PvdQ acylase as a quorum quenching agent during Pseudomonas aeruginosa infection (mouse model of pulmonary Pseudomonas aeruginosa infection)
-
pharmacology
therapeutic efficacy of PvdQ acylase as a quorum quenching agent during Pseudomonas aeruginosa infection (mouse model of pulmonary Pseudomonas aeruginosa infection)
pharmacology
-
therapeutic efficacy of PvdQ acylase as a quorum quenching agent during Pseudomonas aeruginosa infection (mouse model of pulmonary Pseudomonas aeruginosa infection)
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, J.J.; Petersen, A.; Whiteley, M.; Leadbetter, J.R.
Identification of QuiP, the product of gene PA1032, as the second acyl-homoserine lactone acylase of Pseudomonas aeruginosa PAO1
Appl. Environ. Microbiol.
72
1190-1197
2006
Pseudomonas aeruginosa
brenda
Sio, C.F.; Otten, L.G.; Cool, R.H.; Diggle, S.P.; Braun, P.G.; Bos, R.; Daykin, M.; Camara, M.; Williams, P.; Quax, W.J.
Quorum quenching by an N-acyl-homoserine lactone acylase from Pseudomonas aeruginosa PAO1
Infect. Immun.
74
1673-1682
2006
Pseudomonas aeruginosa
brenda
Lin, Y.H.; Xu, J.L.; Hu, J.; Wang, L.H.; Ong, S.L.; Leadbetter, J.R.; Zhang, L.H.
Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes
Mol. Microbiol.
47
849-860
2003
Ralstonia sp.
brenda
Romero, M.; Diggle, S.P.; Heeb, S.; Camara, M.; Otero, A.
Quorum quenching activity in Anabaena sp. PCC 7120: identification of AiiC, a novel AHL-acylase
FEMS Microbiol. Lett.
280
73-80
2008
Anabaena sp.
brenda
Shepherd, R.W.; Lindow, S.E.
Two dissimilar N-acyl-homoserine lactone acylases of Pseudomonas syringae influence colony and biofilm morphology
Appl. Environ. Microbiol.
75
45-53
2009
Pseudomonas syringae (Q4ZV08), Pseudomonas syringae
brenda
Morohoshi, T.; Nakazawa, S.; Ebata, A.; Kato, N.; Ikeda, T.
Identification and characterization of N-acylhomoserine lactone-acylase from the fish intestinal Shewanella sp. strain MIB015
Biosci. Biotechnol. Biochem.
72
1887-1893
2008
Shewanella sp. MIB015 (A9CPH6), Shewanella oneidensis MR-1 (Q8EIC5), Shewanella oneidensis MR-1
brenda
Papaioannou, E.; Wahjudi, M.; Nadal-Jimenez, P.; Koch, G.; Setroikromo, R.; Quax, W.J.
Quorum-quenching acylase reduces the virulence of Pseudomonas aeruginosa in a Caenorhabditis elegans infection model
Antimicrob. Agents Chemother.
53
4891-4897
2009
Pseudomonas aeruginosa PAO1
brenda
Chen, C.N.; Chen, C.J.; Liao, C.T.; Lee, C.Y.
A probable aculeacin A acylase from the Ralstonia solanacearum GMI1000 is N-acyl-homoserine lactone acylase with quorum-quenching activity
BMC Microbiol.
9
89
2009
Ralstonia solanacearum GMI1000
brenda
Bokhove, M.; Nadal Jimenez, P.; Quax, W.J.; Dijkstra, B.W.
The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket
Proc. Natl. Acad. Sci. USA
107
686-691
2010
Pseudomonas aeruginosa (Q9I194), Pseudomonas aeruginosa
brenda
Czajkowski, R.; Krzyzanowska, D.; Karczewska, J.; Atkinson, S.; Przysowa, J.; Lojkowska, E.; Williams, P.; Jafra, S.
Inactivation of AHLs by Ochrobactrum sp. A44 depends on the activity of a novel class of AHL acylase
Environ. Microbiol. Rep.
3
59-68
2011
Ochrobactrum sp., Ochrobactrum sp. (D8X182), Ochrobactrum sp. A44, Ochrobactrum sp. A44 (D8X182)
brenda
Chan, K.G.; Wong, C.S.; Yin, W.F.; Sam, C.K.; Koh, C.L.
Rapid degradation of N-3-oxo-acylhomoserine lactones by a Bacillus cereus isolate from Malaysian rainforest soil
Antonie van Leeuwenhoek
98
299-305
2010
Bacillus cereus, Bacillus cereus KM1S
brenda
Wahjudi, M.; Papaioannou, E.; Hendrawati, O.; van Assen, A.H.; van Merkerk, R.; Cool, R.H.; Poelarends, G.J.; Quax, W.J.
PA0305 of Pseudomonas aeruginosa is a quorum quenching acylhomoserine lactone acylase belonging to the Ntn hydrolase superfamily
Microbiology
157
2042-2055
2011
Pseudomonas aeruginosa
brenda
Ochiai, S.; Yasumoto, S.; Morohoshi, T.; Ikeda, T.
AmiE, a novel N-acylhomoserine lactone acylase belonging to the amidase family, from the activated sludge isolate Acinetobacter sp. Ooi24
Appl. Environ. Microbiol.
80
6919-6925
2014
Acinetobacter sp. (A0A077JIE7), Acinetobacter sp.
brenda
Utari, P.; Setroikromo, R.; Melgert, B.; Quax, W.
PvdQ quorum quenching acylase attenuates Pseudomonas aeruginosa virulence in a mouse model of pulmonary infection
Front. Cell. Infect. Microbiol.
8
119
2018
Pseudomonas aeruginosa (Q9I194), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9I194)
brenda
Utari, P.; Vogel, J.; Quax, W.
Deciphering physiological functions of AHL quorum quenching acylases
Front. Microbiol.
8
1123
2017
Agrobacterium tumefaciens, Variovorax paradoxus, Brucella melitensis, Deinococcus radiodurans, Kluyvera cryocrescens, Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9I194), Pseudomonas aeruginosa (Q9I4U2), Pseudomonas syringae, Rhodococcus erythropolis, Shewanella sp., Nostoc sp. PCC 7120 = FACHB-418, Pectobacterium atrosepticum, Comamonas sp. D1, Ralstonia mannitolilytica, Ralstonia sp. XJ12B, Tenacibaculum maritimum, Acinetobacter sp. Ooi24 (A0A077JIE7), [Ochrobactrum] quorumnocens (D8X182), Streptomyces sp. M664 (Q50H45), Ralstonia solanacearum (Q8XWC7), Rhodococcus erythropolis W2, Tenacibaculum maritimum NCIMB 2154(T), Pseudomonas aeruginosa DSM 22644 (Q9I194), Pseudomonas aeruginosa DSM 22644 (Q9I4U2), Pseudomonas syringae B728a, Variovorax paradoxus VAI-C, Ralstonia mannitolilytica SDV
brenda
Kusada, H.; Tamaki, H.; Kamagata, Y.; Hanada, S.; Kimura, N.
A novel quorum-quenching N-acylhomoserine lactone acylase from Acidovorax sp. strain MR-S7 mediates antibiotic resistance
Appl. Environ. Microbiol.
83
e00080-17
2017
Acidovorax sp. MR-S7
brenda
Pan, Y.; Wang, Y.; Yan, X.; Liu, C.; Wu, B.; He, X.; Liang, Y.
Quorum quenching enzyme APTM01, an acylhomoserine-lactone acylase from marine bacterium of Pseudoalteromonas tetraodonis strain MQS005
Curr. Microbiol.
76
1387-1397
2019
Pseudoalteromonas tetraodonis (A0A290TM55), Pseudoalteromonas tetraodonis, Pseudoalteromonas tetraodonis MQS005 (A0A290TM55)
brenda
Liu, N.; Yu, M.; Zhao, Y.; Cheng, J.; An, K.; Zhang, X.H.
PfmA, a novel quorum-quenching N-acylhomoserine lactone acylase from Pseudoalteromonas flavipulchra
Microbiology
163
1389-1398
2017
Pseudoalteromonas flavipulchra (A0A223AMX9), Pseudoalteromonas flavipulchra, Pseudoalteromonas flavipulchra JG1 (A0A223AMX9), Pseudoalteromonas flavipulchra JG1
brenda
Maisuria, V.B.; Nerurkar, A.S.
Interference of quorum sensing by Delftia sp. VM4 depends on the activity of a novel N-acylhomoserine lactone-acylase
PLoS ONE
10
e0138034
2015
Delftia sp. VM4
brenda
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