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Information on EC 3.1.1.81 - quorum-quenching N-acyl-homoserine lactonase

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.81 quorum-quenching N-acyl-homoserine lactonase
IUBMB 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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UNIPROT: I7HB71
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Word Map
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
quorum-quenching lactonase
-
quorum-sensing enzyme
-
-
-
-
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 hide
389867-43-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-3-oxooctanoyl-L-homoserine lactone + H2O
N-3-oxooctanoyl-L-homoserine
show the reaction diagram
-
-
-
?
N-butyryl-L-homoserine lactone + H2O
N-butyryl-L-homoserine
show the reaction diagram
-
-
-
?
N-decanoyl-L-homoserine lactone + H2O
N-decanoyl-L-homoserine
show the reaction diagram
-
-
-
?
N-dodecanoyl-L-homoserine lactone + H2O
N-dodecanoyl-L-homoserine
show the reaction diagram
-
-
-
?
N-heptanoyl-L-homoserine lactone + H2O
N-heptanoyl-L-homoserine
show the reaction diagram
-
-
-
?
N-hexanoyl-L-homoserine lactone + H2O
N-hexanoyl-L-homoserine
show the reaction diagram
-
-
-
?
N-octanoyl-L-homoserine lactone + H2O
N-octanoyl-L-homoserine
show the reaction diagram
-
-
-
?
N-pentanoyl-L-homoserine lactone + H2O
N-pentanoyl-L-homoserine
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
AidC preparation contains 1.2 equiv of zinc ions per AidC monomer
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13
N-3-oxooctanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
0.47
N-butyryl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
0.012
N-decanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
0.007
N-dodecanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
0.047
N-heptanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
0.061
N-hexanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
0.083
N-octanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
0.13
N-pentanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 8
N-3-oxooctanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
39
N-butyryl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
5.2
N-decanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
0.4
N-dodecanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
80
N-heptanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
59
N-hexanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
45
N-octanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
57
N-pentanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
220
N-3-oxooctanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
83
N-butyryl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
430
N-decanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
57
N-dodecanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
1700
N-heptanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
970
N-hexanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
540
N-octanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
440
N-pentanoyl-L-homoserine lactone
pH 7.5, temperature not specified in the publication
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
20°C: about 85% of maximal activity, 60°C: about 60% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
I7HB71_9FLAO
330
0
37134
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray crystal structures ofAidC alone and with the product N-hexanoyl-L-homoserine are determined at resolutions of 1.09 and 1.67 A, respectively
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
10 min, AHL lactonase activity is almost completely lost
60
10 min, AHL lactonase activity is almost completely lost
70
10 min, AHL lactonase activity is almost completely lost
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant maltose binding protein (MBP)-AiiT fusion protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mascarenhas, R.; Thomas, P.W.; Wu, C.X.; Nocek, B.P.; Hoang, Q.Q.; Liu, D.; Fast, W.
Structural and biochemical characterization of AidC, a quorum-quenching lactonase with atypical selectivity
Biochemistry
54
4342-4353
2015
Chryseobacterium sp. StRB126 (I7HB71)
Manually annotated by BRENDA team
Morohoshi, T.; Tominaga, Y.; Someya, N.; Ikeda, T.
Characterization of a novel thermostable N-acylhomoserine lactonase from the thermophilic bacterium Thermaerobacter marianensis
J. Biosci. Bioeng.
120
1-5
2015
Bacillus cereus, Thermaerobacter marianensis, Thermaerobacter nagasakiensis (A0A060NR36), Thermaerobacter nagasakiensis, Thermaerobacter composti (A0A060NTE1), Solibacillus silvestris (F8WSM9), Solibacillus silvestris, Chryseobacterium sp. StRB126 (I7HB71), Bacillus cereus ATCC 14579, Solibacillus silvestris StLB046 (F8WSM9), Thermaerobacter nagasakiensis JCM 11223 (A0A060NR36), Thermaerobacter marianensis JCM 10246, Thermaerobacter composti JCM 15650 (A0A060NTE1)
Manually annotated by BRENDA team