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IUBMB CommentsAcyl-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 .
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, quorum-quenching lactonase,
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acyl homoserine degrading enzyme
auto-inducer inhibitor from Cyanobacteria
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autoinducer inactivator A
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cold-adapted N-acylhomoserine lactonase
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lactonase/phosphotriesterase
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N-acyl homoserine lactonase
N-acyl homoserine lactone hydrolase
N-acyl-homoserine lactonase
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N-acyl-homoserine lactone lactonase
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N-acyl-homoserine-lactonase
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N-acyl-L-homoserine lactone hydrolase
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N-acyl-L-homoserine lactone lactonase
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N-acylhomoserine lactonase
organophosphorus hydrolase
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phosphotriesterase-like lactonase
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quorum quenching AHL-lactonase
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quorum quenching lactonase
quorum-quenching lactonase
quorum-quenching N-acyl homoserine lactonase
quorum-quenching N-acyl homoserine lactone hydrolase
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quorum-quenching N-acyl homoserine lactone lactonase
quorum-sensing enzyme
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quorum-sensing lactonase
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AaL
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acyl homoserine degrading enzyme
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acyl homoserine degrading enzyme
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adeH
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AHL
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AHL lactonase
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AHL lactonase
Tritonibacter mobilis
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AHL lactonase
Tritonibacter mobilis YJ3
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AHL-degrading enzyme
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AHL-degrading enzyme
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AHL-degrading enzyme
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AHL-degrading enzyme
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AHL-inactivating enzyme
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AHL-inactivating enzyme
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AHL-inactivating enzyme
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AHL-inactivating enzyme
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AHL-lactonase
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AHLase
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AhlD
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AhlK
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AhlS
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AidH
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AidP
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AiiA
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AiiA lactonase
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AiiA-like protein
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AiiA-like protein
Q7B8C0, Q7B8C1, Q7B8C2, Q7B8C3, Q7B8C4, Q7B8C5, Q8KI79, Q8KTW4, Q8KTW5, Q8KTW6, Q8KTW7, Q8KTW8, Q8KTW9, Q8KTX0, Q8KTX1 -
AiiB
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AiiC
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AiiK
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AiiM
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AiiT
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AttM
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delactonase
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lactonase-like enzyme
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lactonase-like enzyme
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lactonase-like enzyme
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lactonase-like enzyme
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lactonase-like enzyme
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lactonase-like enzyme
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lactonase-like enzyme
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lactonase-like enzyme
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lactonase-like enzyme
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lactonase-like enzyme
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lactonase-like enzyme
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lactonase-like enzyme
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MomL
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N-acyl homoserine lactonase
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N-acyl homoserine lactonase
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N-acyl homoserine lactonase
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N-acyl homoserine lactonase
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N-acyl homoserine lactonase
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N-acyl homoserine lactonase
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N-acyl homoserine lactone hydrolase
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N-acyl homoserine lactone hydrolase
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N-acylhomoserine lactonase
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N-acylhomoserine lactonase
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N-acylhomoserine lactonase
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N-acylhomoserine lactonase
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N-acylhomoserine lactonase
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N-acylhomoserine lactonase
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N-acylhomoserine lactonase
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N-acylhomoserine lactonase
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N-acylhomoserine lactonase
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N-acylhomoserine lactonase
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N-acylhomoserine lactonase
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N-AHSL lactonase
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N007_09425
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POX
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QsdA
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qsdS
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quorum quenching lactonase
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quorum quenching lactonase
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quorum quenching lactonase
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quorum-quenching enzyme
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quorum-quenching enzyme
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quorum-quenching enzyme
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quorum-quenching enzyme
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quorum-quenching enzyme
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quorum-quenching lactonase
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quorum-quenching lactonase
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quorum-quenching lactonase
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quorum-quenching lactonase
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quorum-quenching lactonase
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quorum-quenching lactonase
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quorum-quenching lactonase
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quorum-quenching lactonase
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quorum-quenching lactonase
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quorum-quenching lactonase
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quorum-quenching lactonase
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quorum-quenching lactonase
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quorum-quenching lactonase
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quorum-quenching N-acyl homoserine lactonase
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quorum-quenching N-acyl homoserine lactonase
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quorum-quenching N-acyl homoserine lactonase
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quorum-quenching N-acyl homoserine lactonase
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quorum-quenching N-acyl homoserine lactone lactonase
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quorum-quenching N-acyl homoserine lactone lactonase
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RmmL
Tritonibacter mobilis
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RmmL
Tritonibacter mobilis YJ3
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SsoPox
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SsoPox
bifunctional enzyme with organophosphate hydrolase and N-acyl homoserine lactonase activities
VmoLac
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VMUT_2255
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additional information
the enzyme is a member of the metallo-beta-lactamase enzyme superfamily
additional information
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QlcA peptide belongs to the family of zinc-dependent metallohydrolases and appears to be distantly related to other NAHL-lactonases discovered in Agrobacterium, Bacillus, Photorhabdus and Rhizobium
additional information
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the enzyme belongs to the phosphotriesterase-like lactonase group of enzymes within the amidohydrolase superfamily
additional information
cf. EC 3.1.8.1 and EC 3.1.8.2
additional information
the enzyme belongs to the alpha/beta hydrolase fold family
additional information
the enzyme belongs to the alpha/beta hydrolase fold family
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additional information
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the enzyme belongs to the quorum-quenching enzymes
additional information
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QsdA is related to phosphotriesterases and constitutes the reference of a distinct class of N-AHSL degradation enzymes, QsdA belongs to the PTE family of zinc-dependent metalloproteins
additional information
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QsdA is related to phosphotriesterases and constitutes the reference of a distinct class of N-AHSL degradation enzymes, QsdA belongs to the PTE family of zinc-dependent metalloproteins
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additional information
QsdA is related to phosphotriesterases and constitutes the reference of a distinct class of N-AHSL degradation enzymes, QsdA belongs to the PTE family of zinc-dependent metalloproteins
additional information
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QsdA is related to phosphotriesterases and constitutes the reference of a distinct class of N-AHSL degradation enzymes, QsdA belongs to the PTE family of zinc-dependent metalloproteins
additional information
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QsdA is related to phosphotriesterases and constitutes the reference of a distinct class of N-AHSL degradation enzymes, QsdA belongs to the PTE family of zinc-dependent metalloproteins
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additional information
cf. EC 3.1.8.1
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an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
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an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
active site structure and substrate binding, catalytic mechanism, overview
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
hydrolysis of the lactone ring
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
hydrolysis of the lactone ring
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
residues H106, D108, and H109, as well as H169 are important for catalytic activity
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an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
substrate binding and catalytic mecanism, overview
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
catalytic mechanism of the quorum-quenching metalloenzyme, overview
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
enzyme-substrate complex structure and detailed mechanism for the ring-opening hydrolysis of acyl homoserine lactone substrates as catalyzed by the AHL lactonase from Bacillus thuringiensis, overview
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
reaction mechanism, and active site structure and function modeling, Asp108 residue, and not Tyr194, shuttles the proton during the reaction, overview
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
AiiA degrades AHLs in a tail length independent manner. The presence of the tail is required for activity. The putative oxyanion hole function of Y194 toward the substrate seem to show efficacy in stabilizing the intermediate state. Proton shuttling necessary for catalytic activity might be mediated by both water and substrate-based intra-molecular proton transfer
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an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
hydrolysis of the lactone ring
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an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
hydrolysis of the lactone ring
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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].
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-gamma-caprolactone + H2O
4-hydroxycaproate
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?
(S)-gamma-caprolactone + H2O
caproate
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?
3-oxo-dodecanoyl-L-homoserine lactone + H2O
3-oxo-dodecanoyl-L-homoserine
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?
5-thiobutyl butyrolactone + H2O
?
TBBL
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?
an N-acyl-L-homoserine lactone + H2O
an N-acyl-L-homoserine
delta valerolactone + H2O
valerate
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?
delta-decalactone + H2O
5-hydroxydecanoate
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delta-decalactone + H2O
5-hydroxydecanoic acid
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?
delta-dodecalactone + H2O
5-hydroxydodecanoic acid
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?
delta-nonalactone + H2O
5-hydroxynonanoate
delta-nonalactone + H2O
5-hydroxynonanoic acid
delta-undecalactone + H2O
5-hydroxyundecanoic acid
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?
delta-valerolactone + H2O
5-hydroxypentanoic acid
dodecanoic-delta-lactone + H2O
5-hydroxydodecanoate
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?
dodecanoic-gamma-lactone + H2O
dodecanoate
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?
epsilon-caprolactone + H2O
6-hydroxycaproate
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?
ethyl paraoxon + H2O
4-nitrophenol + diethyl phosphate
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?
gamma-butyrolactone + H2O
4-hydroxybutanoic acid
gamma-caprolactone + H2O
4-hydroxyhexanoic acid
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?
gamma-dodecalactone + H2O
4-hydroxydodecanoic acid
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?
gamma-heptalactone + H2O
4-hydroxyheptanoic acid
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?
gamma-heptanolide + H2O
4-hydroxyheptanoic acid
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?
gamma-heptanolide + H2O
?
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?
gamma-nonalactone + H2O
4-hydroxynonanoate
gamma-nonalactone + H2O
4-hydroxynonanoic acid
gamma-undecalactone + H2O
4-hydroxyundecanoic acid
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?
heptanoic-gamma-lactone + H2O
4-hydroxyheptanoate
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?
homo-L-cysteine thiolactone + H2O
homo-L-cysteine
L-homoserine lactone + H2O
L-homoserine
N-(3-hydroxy-dodecanoyl)-L-homoserine lactone + H2O
N-(3-hydroxy-dodecanoyl)-L-homoserine
relative activity: 91.9%
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-
?
N-(3-hydroxybutyryl)-L-homoserine lactone + H2O
N-(3-hydroxybutyryl)-L-homoserine
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?
N-(3-hydroxydodecanoyl)-L-homoserine lactone + H2O
N-(3-hydroxydodecanoyl)-L-homoserine
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?
N-(3-hydroxyhexanoyl)-L-homoserine lactone + H2O
N-(3-hydroxyhexanoyl)-L-homoserine
N-(3-hydroxyoctanoyl)-DL-homoserine lactone + H2O
N-(3-hydroxyoctanoyl)-L-homoserine
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?
N-(3-hydroxyoctanoyl)-L-homoserine lactone + H2O
N-(3-hydroxyoctanoyl)-L-homoserine
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?
N-(3-hydroxytetradecanoyl)-L-homoserine lactone + H2O
N-(3-hydroxytetradecanoyl)-L-homoserine
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?
N-(3-oxo-decanoyl)-L-homoserine lactone + H2O
N-(3-oxo-decanoyl)-L-homoserine
N-(3-oxo-dodecanoyl)-L-homoserine lactone + H2O
N-(3-oxo-dodecanoyl)-L-homoserine
relative activity: 83.3%
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?
N-(3-oxo-N-hexanoyl)-L-homoserine lactone + H2O
N-(3-oxo-N-hexanoyl)-L-homoserine
3.1.1.81 quorum-quenching N-acyl-homoserine lactonase
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