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Literature summary extracted from

  • Wang, L.H.; Weng, L.X.; Dong, Y.H.; Zhang, L.H.
    Specificity and enzyme kinetics of the quorum-quenching N-acyl homoserine lactone lactonase (AHL-lactonase) (2004), J. Biol. Chem., 279, 13645-13651.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.81 additional information enzyme is not affected by EDTA, 2,2'-bipyridine, and o-phenanthroline at 2 mM Bacillus sp. (in: Bacteria)

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.81 gene aiiA, expression of wild-type and mutant enzymes in Escherichia coli as GST-tagged proteins Bacillus sp. (in: Bacteria)

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.81 D108S site-directed mutagenesis, the mutant shows no activity, and altered secondary structure Bacillus sp. (in: Bacteria)
3.1.1.81 H106S site-directed mutagenesis, the mutant shows 53.5% of wild-type enzyme activity, and altered secondary structure Bacillus sp. (in: Bacteria)
3.1.1.81 H109S site-directed mutagenesis, the mutant shows no activity, and altered secondary structure Bacillus sp. (in: Bacteria)
3.1.1.81 H169S site-directed mutagenesis, the mutant shows 53.1% of wild-type enzyme activity, and altered secondary structure Bacillus sp. (in: Bacteria)

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.81 Ag+ complete inhibition at 0.2 mM Bacillus sp. (in: Bacteria)
3.1.1.81 Cr2+ 72% inhibition at 2 mM Bacillus sp. (in: Bacteria)
3.1.1.81 Cu2+ complete inhibition at 0.2 mM Bacillus sp. (in: Bacteria)
3.1.1.81 Fe2+ 48% inhibition at 2 mM Bacillus sp. (in: Bacteria)
3.1.1.81 additional information enzyme is not affected by EDTA, 2,2'-bipyridine, and o-phenanthroline at 2 mM Bacillus sp. (in: Bacteria)
3.1.1.81 Pb2+ 67% inhibition at 2 mM Bacillus sp. (in: Bacteria)

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.81 additional information
-
 additional information kinetics and thermodynamics Bacillus sp. (in: Bacteria)
3.1.1.81 0.0014
-
 N-3-oxodecanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 0.0023
-
 N-3-oxooctanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 0.0026
-
 N-octanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 0.003
-
 N-3-oxohexanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 0.0038
-
 N-hexanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 0.0047
-
 N-3-oxobutanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 0.0051
-
 N-butanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 0.0075
-
 N-3-hydroxybutanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.81 additional information no effect by Mg2+, Ca2+, Mn2+, Co2+, Ni2+, Zn2+, and Cd2+, the enzyme contains the putative zinc-binding motif 104HXHXDH109, but is no metallohydrolase since it does not contain and require Zn2+ or other metal ions, only trace amounts of Zn2+, the 104HXHXDH109 sequence is a catalytic motif of the AHL-lactonase Bacillus sp. (in: Bacteria)

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.81 additional information Bacillus sp. (in: Bacteria) N-acyl homoserine lactone quorum-sensing signals are the vital elements of bacterial quorum-sensing systems, which regulate diverse biological functions, including virulence ?
-
 ?
3.1.1.81 N-acyl-(S)-homoserine lactone + H2O Bacillus sp. (in: Bacteria) the enzyme AiiA inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora, acylhomoserine lactones are autoinducers of quorum-sensing signaling, mechanism N-acyl-(S)-homoserine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.81 Bacillus sp. (in: Bacteria)
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.81 recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli by glutathione affinity chromatography Bacillus sp. (in: Bacteria)

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.81 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 Bacillus sp. (in: Bacteria)
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.81 additional information
-
-
 Bacillus sp. (in: Bacteria)

Storage Stability

EC Number Storage Stability Organism
3.1.1.81 4°C or 21°C, purified recombinant enzyme, 10 days, 99% remaining activity Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.81 additional information N-acyl homoserine lactone quorum-sensing signals are the vital elements of bacterial quorum-sensing systems, which regulate diverse biological functions, including virulence Bacillus sp. (in: Bacteria) ?
-
 ?
3.1.1.81 additional information substrate specificity, poor activity with non-acyl lactones and no activity with non-cyclic esters, but strong activity with all N-acyl-(S)-homoserine lactones of different chain length and nature, the amide group and the ketone at C1 position of the substrate's acyl chain might be important for substrate-enzyme interaction, overview Bacillus sp. (in: Bacteria) ?
-
 ?
3.1.1.81 N-3-hydroxybutanoyl-L-homoserine lactone + H2O
-
 Bacillus sp. (in: Bacteria) N-3-hydroxybutanoyl-L-homoserine
-
 ?
3.1.1.81 N-3-oxobutanoyl-L-homoserine lactone + H2O
-
 Bacillus sp. (in: Bacteria) N-3-oxobutanoyl-L-homoserine
-
 ?
3.1.1.81 N-3-oxodecanoyl-L-homoserine lactone + H2O high activity Bacillus sp. (in: Bacteria) N-3-oxodecanoyl-L-homoserine
-
 ?
3.1.1.81 N-3-oxododecanoyl-L-homoserine lactone + H2O
-
 Bacillus sp. (in: Bacteria) N-3-oxododecanoyl-L-homoserine
-
 ?
3.1.1.81 N-3-oxohexanoyl-L-homoserine lactone + H2O
-
 Bacillus sp. (in: Bacteria) N-3-oxohexanoyl-L-homoserine
-
 ?
3.1.1.81 N-3-oxooctanoyl-L-homoserine lactone + H2O high activity Bacillus sp. (in: Bacteria) N-3-oxooctanoyl-L-homoserine
-
 ?
3.1.1.81 N-acyl-(S)-homoserine lactone + H2O the enzyme AiiA inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora, acylhomoserine lactones are autoinducers of quorum-sensing signaling, mechanism Bacillus sp. (in: Bacteria) N-acyl-(S)-homoserine
-
 ?
3.1.1.81 N-butanoyl-L-homoserine lactone + H2O high activity Bacillus sp. (in: Bacteria) N-butanoyl-L-homoserine
-
 ?
3.1.1.81 N-decanoyl-L-homoserine lactone + H2O high activity Bacillus sp. (in: Bacteria) N-decanoyl-L-homoserine
-
 ?
3.1.1.81 N-hexanoyl-L-homoserine lactone + H2O best substrate Bacillus sp. (in: Bacteria) N-hexanoyl-L-homoserine
-
 ?
3.1.1.81 N-octanoyl-L-homoserine lactone + H2O high activity Bacillus sp. (in: Bacteria) N-octanoyl-L-homoserine
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.81 More analysis of secondary wild-type and mutant enzyme structures, comparison, overview Bacillus sp. (in: Bacteria)

Synonyms

EC Number Synonyms Comment Organism
3.1.1.81 AHL-lactonase
-
 Bacillus sp. (in: Bacteria)
3.1.1.81 quorum-quenching enzyme
-
 Bacillus sp. (in: Bacteria)
3.1.1.81 quorum-quenching N-acyl homoserine lactone lactonase
-
 Bacillus sp. (in: Bacteria)

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.81 22
-
 assay at Bacillus sp. (in: Bacteria)

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.81 6 37
-
 Bacillus sp. (in: Bacteria)

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.81 37
-
 purified recombinant wild-type enzyme, completely stable below Bacillus sp. (in: Bacteria)
3.1.1.81 45
-
 purified recombinant wild-type enzyme, inactivation, 2 h Bacillus sp. (in: Bacteria)

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.81 20.2
-
 N-3-oxodecanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 22.2
-
 N-3-oxooctanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 22.7
-
 N-3-oxohexanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 27.5
-
 N-octanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 28.6
-
 N-3-oxobutanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 29.3
-
 N-3-hydroxybutanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 35.7
-
 N-hexanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)
3.1.1.81 37.6
-
 N-butanoyl-L-homoserine lactone pH 7.4, 22°C, recombinant wild-type enzyme Bacillus sp. (in: Bacteria)

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.81 8
-
 broad optimum of pH 7.0 to pH 9.0 Bacillus sp. (in: Bacteria)

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.81 6 9 complete loss of activity at pH 5.5 and above pH 9.0, pH-profile Bacillus sp. (in: Bacteria)

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.1.81 Bacillus sp. (in: Bacteria)
-
-
 4.7