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Literature summary extracted from

  • Ochiai, S.; Yasumoto, S.; Morohoshi, T.; Ikeda, T.
    AmiE, a novel N-acylhomoserine lactone acylase belonging to the amidase family, from the activated sludge isolate Acinetobacter sp. Ooi24 (2014), Appl. Environ. Microbiol., 80, 6919-6925.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.81 expressed in Escherichia coli Acinetobacter sp.
3.5.1.97 gene amiE, from genomic library, DNA and amino acid sequence determination and analysis, phylogenetic tree, sequence comparisons, amiE is transferred by a putative transposon, cloning in Escherichia coli strain DHalpha, recombinant expression in Pseudomonas aeruginosa strain PAO1 leading to reduced N-acyl-L-homoserine lactone accumulation and elastase activity Acinetobacter sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.97 additional information Acinetobacter sp. the enzyme shows a high level of degrading activity against N-acyl-L-homoserine lactones with long acyl chains but no activity against N-acyl-L-homoserine lactones with acyl chains shorter than eight carbons ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.81 Acinetobacter sp.
-
-
-
3.5.1.97 Acinetobacter sp. A0A077JIE7 activated-sludge isolate, gene amiE
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.81 N-decanoyl-L-homoserine lactone + H2O highest activity Acinetobacter sp. N-decanoyl-L-homoserine
-
 ?
3.1.1.81 N-dodecanoyl-L-homoserine lactone + H2O
-
 Acinetobacter sp. N-dodecanoyl-L-homoserine
-
 ?
3.1.1.81 N-octanoyl-L-homoserine lactone + H2O
-
 Acinetobacter sp. N-octanoyl-L-homoserine
-
 ?
3.5.1.97 additional information the enzyme shows a high level of degrading activity against N-acyl-L-homoserine lactones with long acyl chains but no activity against N-acyl-L-homoserine lactones with acyl chains shorter than eight carbons Acinetobacter sp. ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.81 AHL
-
 Acinetobacter sp.
3.1.1.81 AmiE
-
 Acinetobacter sp.
3.5.1.97 AHL acylase
-
 Acinetobacter sp.
3.5.1.97 AmiE
-
 Acinetobacter sp.
3.5.1.97 long-chain AHL acylase
-
 Acinetobacter sp.
3.5.1.97 N-acylhomoserine lactone acylase
-
 Acinetobacter sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.81 30
-
 assay at Acinetobacter sp.
3.5.1.97 30
-
 assay at Acinetobacter sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.81 7.4
-
 assay at Acinetobacter sp.
3.5.1.97 7.4
-
 assay at Acinetobacter sp.

General Information

EC Number General Information Comment Organism
3.5.1.97 evolution the enzyme belongs to the amidase family. AmiE shows homology with a member of the amidases (EC 3.5.1.4) but not with any known AHL acylase enzymes. An amino acid sequence of AmiE from Ooi24 shows greater than 99% identities with uncharacterized proteins from Acinetobacter ursingii CIP 107286 and Acinetobacter sp. strain CIP 102129, but it is not found in the draft or complete genome sequences of other Acinetobacter strains. Phylogenetic relationship between AmiE and known AHL acylases and phylogenetic tree Acinetobacter sp.
3.5.1.97 physiological function the enzyme hydrolyzes the amide bond of N-acyl-L-homoserine lactones, quorum-sensing signal molecules. The recombinant enzyme in Pseudomonas aeruginosa PAO1 reduces N-acyl-L-homoserine lactone accumulation and elastase activity, which are regulated by AHL-mediated quorum sensing Acinetobacter sp.