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Literature summary for 3.5.1.97 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)

Cloned (Comment) Organism
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
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?

Organism

Organism UniProt Comment Textmining
Acinetobacter sp. A0A077JIE7 activated-sludge isolate, gene amiE
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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. ?
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?

Synonyms

Synonyms Comment Organism
AHL acylase
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Acinetobacter sp.
AmiE
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Acinetobacter sp.
long-chain AHL acylase
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Acinetobacter sp.
N-acylhomoserine lactone acylase
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Acinetobacter sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
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assay at Acinetobacter sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Acinetobacter sp.

General Information

General Information Comment Organism
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.
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.