Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes as His-tagged maltose binding protein-fusion proteins | Bacillus thuringiensis serovar kurstaki |
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 | 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 | Comment | Organism | Structure |
---|---|---|---|
TPEN | i.e. N,N,N',N'-tetrakis-(2-pyridylmethyl)-ethylene-diamine | Bacillus thuringiensis serovar kurstaki |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus thuringiensis serovar kurstaki | P0CJ63 | HD263, gene aiiA | - |
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 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-hexanoyl-L-homoserine lactone + H2O | - |
Bacillus thuringiensis serovar kurstaki | N-hexanoyl-L-homoserine | - |
? |
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 |