Literature summary for 3.1.1.81 extracted from

Liu, D.; Momb, J.; Thomas, P.W.; Moulin, A.; Petsko, G.A.; Fast, W.; Ringe, D.
Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures (2008), Biochemistry, 47, 7706-7714.

Crystallization (Commentary)

Crystallization (Comment)	Organism
lactonase AiiA bound with two different concentrations of the ring-opened product of N-hexanoyl-L-homoserine lactone, and with the ring-opened product of the non-natural N-hexanoyl-L-homocysteine thiolactone, hanging drop method, 20 mg/mL protein in 20% glycerol, v/v, 80 mM Tris-HCl, 24% w/v PEG 4000, and 160 mM MgCl2, pH 8.5, X-ray diffraction structure determination and analysis at 0.95 and 1.4 A resolution and at 1.3 A resolution, respectively, modelling	Bacillus thuringiensis

Crystallization (Comment)

Organism

lactonase AiiA bound with two different concentrations of the ring-opened product of N-hexanoyl-L-homoserine lactone, and with the ring-opened product of the non-natural N-hexanoyl-L-homocysteine thiolactone, hanging drop method, 20 mg/mL protein in 20% glycerol, v/v, 80 mM Tris-HCl, 24% w/v PEG 4000, and 160 mM MgCl2, pH 8.5, X-ray diffraction structure determination and analysis at 0.95 and 1.4 A resolution and at 1.3 A resolution, respectively, modelling

Bacillus thuringiensis

Protein Variants

Protein Variants	Comment	Organism
A206W	site-directed mutagenesis, structure and catalytic mechanism compared to the wild-type, overview	Bacillus thuringiensis
D108N	site-directed mutagenesis, structure and catalytic mechanism compared to the wild-type, overview	Bacillus thuringiensis
G207D	site-directed mutagenesis, structure and catalytic mechanism compared to the wild-type, overview	Bacillus thuringiensis
G207W	site-directed mutagenesis, structure and catalytic mechanism compared to the wild-type, overview	Bacillus thuringiensis
Y194F	site-directed mutagenesis, structure and catalytic mechanism compared to the wild-type, overview	Bacillus thuringiensis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
additional information	-	additional information	steady-state kinetics of wild-type and mutant enzymes, overview	Bacillus thuringiensis
0.09	-	N-hexanoyl-L-homoserine lactone	mutant D108N with Co2+	Bacillus thuringiensis
0.6	-	N-hexanoyl-L-homoserine thiolactone	mutant Y194F	Bacillus thuringiensis
1.3	-	N-hexanoyl-L-homoserine thiolactone	mutant D108N	Bacillus thuringiensis
1.6	-	N-hexanoyl-L-homoserine lactone	mutant D108N with Zn2+	Bacillus thuringiensis
2	-	N-hexanoyl-L-homoserine lactone	mutant Y194F with Co2+	Bacillus thuringiensis
2.1	-	N-hexanoyl-L-homoserine lactone	mutant Y194F with Zn2+	Bacillus thuringiensis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the dinuclear zinc site is required for catalysis and stability, metal coordination, overview	Bacillus thuringiensis
Zn2+	the dinuclear zinc site, zinc 1 is coordinated by residues His104, His106, and His169 along with a weaker bridging interaction to Asp191, while zinc 2 is coordinated by His109, His235, Asp108, and Asp191, overview	Bacillus thuringiensis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
N-hexanoyl-L-homoserine lactone + H2O	Bacillus thuringiensis	-	N-hexanoyl-L-homoserine	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus thuringiensis	P0CJ63	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine	catalytic mechanism of the quorum-quenching metalloenzyme, overview	Bacillus thuringiensis	a
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine	enzyme-substrate complex structure and detailed mechanism for the ring-opening hydrolysis of acyl homoserine lactone substrates as catalyzed by the AHL lactonase from Bacillus thuringiensis, overview	Bacillus thuringiensis	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	the enzyme possesses a broad substrate-binding cavity, structure, overview	Bacillus thuringiensis	?	-	?
N-hexanoyl-L-homoserine lactone + H2O	-	Bacillus thuringiensis	N-hexanoyl-L-homoserine	-	?
N-hexanoyl-L-homoserine lactone + H2O	the structures of the lactonase bound with two different concentrations of the ring-opened product of N-hexanoyl-L-homoserine lactone exhibit different product configurations, overview	Bacillus thuringiensis	N-hexanoyl-L-homoserine	-	?
N-hexanoyl-L-homoserine thiolactone + H2O	structures of the lactonase bound with the ring-opened product of N-hexanoyl-L-homoserine thiolactone, overview	Bacillus thuringiensis	?	-	?

Subunits

Subunits	Comment	Organism
More	modeling of the substrate binding orientation using the hybrid quantum mechanical/molecular mechanical method for the wild-type enzyme and the Y194F mutant, overview	Bacillus thuringiensis
More	three-dimensional structures of three enzyme-product complexes, overview	Bacillus thuringiensis

Synonyms

Synonyms	Comment	Organism
AHL lactonase	-	Bacillus thuringiensis
AiiA	-	Bacillus thuringiensis
More	the enzyme is a member of the metallo-beta-lactamase enzyme superfamily	Bacillus thuringiensis
quorum-quenching lactonase	-	Bacillus thuringiensis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
0.31	-	N-hexanoyl-L-homoserine lactone	mutant Y194F with Zn2+	Bacillus thuringiensis
1.11	-	N-hexanoyl-L-homoserine thiolactone	mutant D108N	Bacillus thuringiensis
1.4	-	N-hexanoyl-L-homoserine lactone	mutant D108N with Zn2+	Bacillus thuringiensis
3.5	-	N-hexanoyl-L-homoserine lactone	mutant D108N with Co2+	Bacillus thuringiensis
5.4	-	N-hexanoyl-L-homoserine thiolactone	mutant Y194F	Bacillus thuringiensis
16.6	-	N-hexanoyl-L-homoserine lactone	mutant Y194F with Co2+	Bacillus thuringiensis