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Literature summary extracted from

  • Seo, M.J.; Lee, B.S.; Pyun, Y.R.; Park, H.
    Isolation and characterization of N-acylhomoserine lactonase from the Thermophilic bacterium, Geobacillus caldoxylosilyticus YS-8 (2011), Biosci. Biotechnol. Biochem., 75, 1789-1795.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.81 32000
-
x * 32000, SDS-PAGE Parageobacillus caldoxylosilyticus

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 Parageobacillus caldoxylosilyticus the AHL-degrading enzyme catalyzes the lactone ring opening of N-3-oxohexanoyl-L-homoserine lactone and N-hexanoyl-L-homoserine lactone by hydrolyzing the lactones ?
-
?
3.1.1.81 additional information Parageobacillus caldoxylosilyticus YS-8 the AHL-degrading enzyme catalyzes the lactone ring opening of N-3-oxohexanoyl-L-homoserine lactone and N-hexanoyl-L-homoserine lactone by hydrolyzing the lactones ?
-
?
3.1.1.81 N-3-oxo-dodecanoyl-L-homoserine lactone + H2O Parageobacillus caldoxylosilyticus
-
N-3-oxo-dodecanoyl-L-homoserine
-
?
3.1.1.81 N-3-oxo-hexanoyl-L-homoserine lactone + H2O Parageobacillus caldoxylosilyticus lower activity N-3-oxo-hexanoyl-L-homoserine
-
?
3.1.1.81 N-decanoyl-L-homoserine lactone + H2O Parageobacillus caldoxylosilyticus
-
N-decanoyl-L-homoserine
-
?
3.1.1.81 N-decanoyl-L-homoserine lactone + H2O Parageobacillus caldoxylosilyticus YS-8
-
N-decanoyl-L-homoserine
-
?
3.1.1.81 N-hexanoyl-L-homoserine lactone + H2O Parageobacillus caldoxylosilyticus lower activity N-hexanoyl-L-homoserine
-
?
3.1.1.81 N-hexanoyl-L-homoserine lactone + H2O Parageobacillus caldoxylosilyticus YS-8 lower activity N-hexanoyl-L-homoserine
-
?
3.1.1.81 N-octanoyl-L-homoserine lactone + H2O Parageobacillus caldoxylosilyticus lower activity N-octanoyl-L-homoserine
-
?
3.1.1.81 N-octanoyl-L-homoserine lactone + H2O Parageobacillus caldoxylosilyticus YS-8 lower activity N-octanoyl-L-homoserine
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.81 Parageobacillus caldoxylosilyticus
-
-
-
3.1.1.81 Parageobacillus caldoxylosilyticus YS-8
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.81 native enzyme 201.5fold by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, gel filtration, and another step of anion exchange chromatography Parageobacillus caldoxylosilyticus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.81 256
-
purified enzyme, substrate N-3-oxo-dodecanoyl-L-homoserine lactone, pH 6.5, 50°C Parageobacillus caldoxylosilyticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.81 additional information substrate specificity, overview Parageobacillus caldoxylosilyticus ?
-
?
3.1.1.81 additional information the AHL-degrading enzyme catalyzes the lactone ring opening of N-3-oxohexanoyl-L-homoserine lactone and N-hexanoyl-L-homoserine lactone by hydrolyzing the lactones Parageobacillus caldoxylosilyticus ?
-
?
3.1.1.81 additional information substrate specificity, overview Parageobacillus caldoxylosilyticus YS-8 ?
-
?
3.1.1.81 additional information the AHL-degrading enzyme catalyzes the lactone ring opening of N-3-oxohexanoyl-L-homoserine lactone and N-hexanoyl-L-homoserine lactone by hydrolyzing the lactones Parageobacillus caldoxylosilyticus YS-8 ?
-
?
3.1.1.81 N-3-oxo-dodecanoyl-L-homoserine lactone + H2O
-
Parageobacillus caldoxylosilyticus N-3-oxo-dodecanoyl-L-homoserine
-
?
3.1.1.81 N-3-oxo-hexanoyl-L-homoserine lactone + H2O lower activity Parageobacillus caldoxylosilyticus N-3-oxo-hexanoyl-L-homoserine
-
?
3.1.1.81 N-decanoyl-L-homoserine lactone + H2O
-
Parageobacillus caldoxylosilyticus N-decanoyl-L-homoserine
-
?
3.1.1.81 N-decanoyl-L-homoserine lactone + H2O
-
Parageobacillus caldoxylosilyticus YS-8 N-decanoyl-L-homoserine
-
?
3.1.1.81 N-hexanoyl-L-homoserine lactone + H2O lower activity Parageobacillus caldoxylosilyticus N-hexanoyl-L-homoserine
-
?
3.1.1.81 N-hexanoyl-L-homoserine lactone + H2O lower activity Parageobacillus caldoxylosilyticus YS-8 N-hexanoyl-L-homoserine
-
?
3.1.1.81 N-octanoyl-L-homoserine lactone + H2O lower activity Parageobacillus caldoxylosilyticus N-octanoyl-L-homoserine
-
?
3.1.1.81 N-octanoyl-L-homoserine lactone + H2O lower activity Parageobacillus caldoxylosilyticus YS-8 N-octanoyl-L-homoserine
-
?

Subunits

EC Number Subunits Comment Organism
3.1.1.81 ? x * 32000, SDS-PAGE Parageobacillus caldoxylosilyticus

Synonyms

EC Number Synonyms Comment Organism
3.1.1.81 AHL lactonase
-
Parageobacillus caldoxylosilyticus
3.1.1.81 AHL-degrading enzyme
-
Parageobacillus caldoxylosilyticus
3.1.1.81 N-acylhomoserine lactonase
-
Parageobacillus caldoxylosilyticus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.81 50
-
-
Parageobacillus caldoxylosilyticus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.81 30 80 activity range, 30% of maximal activity at 80°C, profile, overview Parageobacillus caldoxylosilyticus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.81 40
-
purified enzyme, 3 h, 100% of maximal activity remaining Parageobacillus caldoxylosilyticus
3.1.1.81 50
-
purified enzyme, 3 h, 80% of maximal activity remaining Parageobacillus caldoxylosilyticus
3.1.1.81 60
-
purified enzyme, 3 h, 50% of maximal activity remaining Parageobacillus caldoxylosilyticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.81 7.5
-
-
Parageobacillus caldoxylosilyticus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.81 4.5 8 activity range, profile, overview Parageobacillus caldoxylosilyticus

General Information

EC Number General Information Comment Organism
3.1.1.81 physiological function the enzyme is involved in quorum sensing, a regulatory mechanism of cell-to-cell communication in response to environmental conditions Parageobacillus caldoxylosilyticus