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Literature summary extracted from

  • Chen, R.; Zhou, Z.; Cao, Y.; Bai, Y.; Yao, B.
    High yield expression of an AHL-lactonase from Bacillus sp. B546 in Pichia pastoris and its application to reduce Aeromonas hydrophila mortality in aquaculture (2010), Microb. Cell Fact., 9, 39.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.81 2-mercaptoethanol 112.2% activity at 1 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 EDTA 103.6% activity at 10 mM Bacillus thuringiensis serovar kyushuensis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.81 expressed in Pichia pastoris strain GS115 Bacillus thuringiensis serovar kyushuensis

General Stability

EC Number General Stability Organism
3.1.1.81 after incubation with trypsin, subtilisin A, collagenase and proleather at 37°C for 30 or 60 min, the enzyme maintains or enhances its enzymatic activity Bacillus thuringiensis serovar kyushuensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.81 Ag+ complete inhibition at 1 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Cr3+ 29.1% residual activity at 1 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Cu2+ 68.5% residual activity at 1 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Hg2+ complete inhibition at 1 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Li+ 65.8% residual activity at 10 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Pb2+ 87.5% residual activity at 10 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 SDS complete inhibition at 10 mM Bacillus thuringiensis serovar kyushuensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.81 Ca2+ 117.5% activity at 10 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Fe3+ 104.8% activity at 1 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 K+ 109.3% activity at 10 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Li+ 115.4% activity at 1 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Mg2+ 108.4% activity at 10 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Mn2+ 108.4% activity at 10 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Na+ 109.5% activity at 1 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Ni2+ 103.4% activity at 1 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Pb2+ 108.6% activity at 1 mM Bacillus thuringiensis serovar kyushuensis
3.1.1.81 Zn2+ 109.5% activity at 10 mM Bacillus thuringiensis serovar kyushuensis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.81 28140
-
 x * 28140, calculated from amino acid sequence Bacillus thuringiensis serovar kyushuensis
3.1.1.81 31500
-
 x * 31500, deglycosylated enzyme, based on SDS-PAGE Bacillus thuringiensis serovar kyushuensis
3.1.1.81 33600
-
 x * 33600, glycosylated enzyme, based on SDS-PAGE Bacillus thuringiensis serovar kyushuensis

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.81 Bacillus thuringiensis serovar kyushuensis D8VDY4
-
-
3.1.1.81 Bacillus thuringiensis serovar kyushuensis B546 D8VDY4
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.81 glycoprotein
-
 Bacillus thuringiensis serovar kyushuensis

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.81 ammonium sulfate precipitation and anion exchange chromatography Bacillus thuringiensis serovar kyushuensis

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 2.995
-
 purified enzyme, using N-(3-oxooctanoyl)-L-homoserine lactone as the substrate, at pH 8.0 and 25°C Bacillus thuringiensis serovar kyushuensis

Storage Stability

EC Number Storage Stability Organism
3.1.1.81 0°C, purified enzyme, 3 months, 1.6% loss of activity Bacillus thuringiensis serovar kyushuensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.81 N-(3-oxohexanoyl)-L-homoserine lactone + H2O
-
 Bacillus thuringiensis serovar kyushuensis L-homoserine lactone + 3-oxohexanoate
-
 ?
3.1.1.81 N-(3-oxohexanoyl)-L-homoserine lactone + H2O
-
 Bacillus thuringiensis serovar kyushuensis B546 L-homoserine lactone + 3-oxohexanoate
-
 ?
3.1.1.81 N-(3-oxooctanoyl)-L-homoserine lactone + H2O
-
 Bacillus thuringiensis serovar kyushuensis L-homoserine lactone + 3-oxooctanoate
-
 ?
3.1.1.81 N-decanoyl-L-homoserine lactone + H2O best substrate Bacillus thuringiensis serovar kyushuensis L-homoserine lactone + decanoate
-
 ?
3.1.1.81 N-decanoyl-L-homoserine lactone + H2O best substrate Bacillus thuringiensis serovar kyushuensis B546 L-homoserine lactone + decanoate
-
 ?
3.1.1.81 N-dodecanoyl-L-homoserine lactone + H2O
-
 Bacillus thuringiensis serovar kyushuensis L-homoserine lactone + dodecanoate
-
 ?
3.1.1.81 N-dodecanoyl-L-homoserine lactone + H2O
-
 Bacillus thuringiensis serovar kyushuensis B546 L-homoserine lactone + dodecanoate
-
 ?
3.1.1.81 N-hexanoyl-L-homoserine lactone + H2O
-
 Bacillus thuringiensis serovar kyushuensis L-homoserine lactone + hexanoate
-
 ?
3.1.1.81 N-hexanoyl-L-homoserine lactone + H2O
-
 Bacillus thuringiensis serovar kyushuensis B546 L-homoserine lactone + hexanoate
-
 ?
3.1.1.81 N-octanoyl-L-homoserine lactone + H2O worst substrate Bacillus thuringiensis serovar kyushuensis L-homoserine lactone + octanoate
-
 ?
3.1.1.81 N-octanoyl-L-homoserine lactone + H2O worst substrate Bacillus thuringiensis serovar kyushuensis B546 L-homoserine lactone + octanoate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.81 ? x * 28140, calculated from amino acid sequence Bacillus thuringiensis serovar kyushuensis
3.1.1.81 ? x * 31500, deglycosylated enzyme, based on SDS-PAGE Bacillus thuringiensis serovar kyushuensis
3.1.1.81 ? x * 33600, glycosylated enzyme, based on SDS-PAGE Bacillus thuringiensis serovar kyushuensis

Synonyms

EC Number Synonyms Comment Organism
3.1.1.81 AHL-lactonase
-
 Bacillus thuringiensis serovar kyushuensis
3.1.1.81 AiiA
-
 Bacillus thuringiensis serovar kyushuensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.81 20
-
-
 Bacillus thuringiensis serovar kyushuensis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.81
-
 35 at 0°C and 20-35°C, the enzyme maintains more than 60% of the highest activity at 20°C Bacillus thuringiensis serovar kyushuensis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.81 70
-
 recombinant enzyme retains more than 80% of the initial activity after preincubation at 70°C for 30 min Bacillus thuringiensis serovar kyushuensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.81 8
-
-
 Bacillus thuringiensis serovar kyushuensis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.81 6.5 8.9 more than 73% of the maximum activity at pH 6.5-8.9 Bacillus thuringiensis serovar kyushuensis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.81 6 12 the enzyme is stable at pH 6.0-12.0, retaining more than 70% activity after pre-incubation at 37°C for 1 h Bacillus thuringiensis serovar kyushuensis