Literature summary for 3.1.1.81 extracted from

Kim, M.H.; Kang, H.O.; Kang, B.S.; Kim, K.J.; Choi, W.C.; Oh, T.K.; Lee, C.H.; Lee, J.K.
Crystallization and preliminary crystallographic analysis of Bacillus thuringiensis AHL-lactonase (2005), Biochim. Biophys. Acta, 1750, 5-8.

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Cloned(Commentary)

Cloned (Comment)	Organism
gene aiiA, expression of His6-tagged maltose binding protein-fusion enzyme with the TEV protease cleavage site in Escherichia coli strain XL 1-Blue	Bacillus thuringiensis serovar kurstaki

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified detagged recombinant native and selenomethionine-labeled enzyme, sitting drop vapour diffusison method, 7 mg/ml protein in 20 mM Tris-HCl, pH 7.5, mixed with and equilibrated against the reservoir solution containing 0.1 M Tris-HCl, pH 8.0, 30% PEG 4000, and 0.2 M MgCl2, 21°C, 5 days, X-ray diffraction structure determination and analysis at 2.0 A resolution	Bacillus thuringiensis serovar kurstaki

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Bacillus thuringiensis serovar kurstaki	N-acyl homoserine lactone, AHL, quorum-sensing signals are the vital elements of bacterial quorum-sensing systems, which regulate diverse biological functions, including virulence and biofilm formation of Gram-negative bacteria, the enzyme deactivates the signaling by degradation of AHLs via lactone ring hydrolysis	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus thuringiensis serovar kurstaki	P0CJ63	gene aiiA	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged maltose binding protein-fusion enzyme from Escherichia coli strain XL 1-Blue by amylose and nickel affinity chromatography and gel filtration, the fusion tag is cleaved off by TEV protease	Bacillus thuringiensis serovar kurstaki

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	N-acyl homoserine lactone, AHL, quorum-sensing signals are the vital elements of bacterial quorum-sensing systems, which regulate diverse biological functions, including virulence and biofilm formation of Gram-negative bacteria, the enzyme deactivates the signaling by degradation of AHLs via lactone ring hydrolysis	Bacillus thuringiensis serovar kurstaki	?	-	?

Synonyms

Synonyms	Comment	Organism
AHL-degrading enzyme	-	Bacillus thuringiensis serovar kurstaki
AHL-lactonase	-	Bacillus thuringiensis serovar kurstaki

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Release 2023.1 (January 2023)