Literature summary for 3.1.1.81 extracted from

Kim, M.H.; Choi, W.C.; Kang, H.O.; Lee, J.S.; Kang, B.S.; Kim, K.J.; Derewenda, Z.S.; Oh, T.K.; Lee, C.H.; Lee, J.K.
The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase (2005), Proc. Natl. Acad. Sci. USA, 102, 17606-17611.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes as His-tagged maltose binding protein-fusion proteins	Bacillus thuringiensis serovar kurstaki

Crystallization (Commentary)

Crystallization (Comment)	Organism
native and selenomethionine-labeled enzyme, free or in complex with L-homoserine lactone, X-ray diffraction structure determination and analysis at 1.7-2.0 A resolution, structure modeling	Bacillus thuringiensis serovar kurstaki

Protein Variants

Protein Variants	Comment	Organism
D108A	site-directed mutagenesis, the mutant enzyme shows a reduced Zn2+ content compared to the wild-type enzyme	Bacillus thuringiensis serovar kurstaki
D191A	site-directed mutagenesis, the mutant enzyme shows a reduced Zn2+ content compared to the wild-type enzyme	Bacillus thuringiensis serovar kurstaki
H109A	site-directed mutagenesis, the mutant enzyme shows a reduced Zn2+ content compared to the wild-type enzyme	Bacillus thuringiensis serovar kurstaki
H235A	site-directed mutagenesis, the mutant enzyme shows a reduced Zn2+ content compared to the wild-type enzyme	Bacillus thuringiensis serovar kurstaki

Inhibitors

Inhibitors	Comment	Organism	Structure
TPEN	i.e. N,N,N',N'-tetrakis-(2-pyridylmethyl)-ethylene-diamine	Bacillus thuringiensis serovar kurstaki

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the enzyme is a metallohydrolase and contains 2 Zn2+ ions per enzyme molecule involved in catalysis in a dinuclear zinc-binding center involving residues H104, H106, H169 for coordination of the first Zn2+, and H109, H235, and D108 for coordination of the second Zn2+, determination of metal content of wild-type and mutant enzymes, AiiA has a very high affinity for Zn2+, overview	Bacillus thuringiensis serovar kurstaki

Organism

Organism	UniProt	Comment	Textmining
Bacillus thuringiensis serovar kurstaki	P0CJ63	HD263, gene aiiA	-

Reaction

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-hexanoyl-L-homoserine lactone + H2O	-	Bacillus thuringiensis serovar kurstaki	N-hexanoyl-L-homoserine	-	?

Synonyms

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

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Release 2023.1 (January 2023)