Literature summary for 3.1.1.81 extracted from

Liu, D.; Lepore, B.W.; Petsko, G.A.; Thomas, P.W.; Stone, E.M.; Fast, W.; Ringe, D.
Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis (2005), Proc. Natl. Acad. Sci. USA, 102, 11882-11887.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant detagged enzyme, hanging drop vapour diffusion method, 10 mg/ml protein in 20% glycerol, 80 mM Tris-HCl, pH 8.5, 24% PEG 4000, and 160 mM MgCl2, in a ratio of 4:1 mixed with well solution, room temperature, 2 weeks, X-ray diffraction structure determination and analysis at 1.6 A resolution using single-wavelength anomalous dispersion phasing, modeling	Bacillus thuringiensis serovar kurstaki

Organism

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

Reaction

Reaction	Comment	Organism	Reaction ID
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine	active site structure and substrate binding, catalytic mechanism, overview	Bacillus thuringiensis serovar kurstaki	a

Subunits

Subunits	Comment	Organism
More	enzyme secondary structure analysis and oligomeric state, overview	Bacillus thuringiensis serovar kurstaki

Synonyms

Synonyms	Comment	Organism
AHL lactonase	-	Bacillus thuringiensis serovar kurstaki
quorum-quenching N-acyl homoserine lactone hydrolase	-	Bacillus thuringiensis serovar kurstaki

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Release 2023.1 (January 2023)