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Literature summary extracted from

  • Czajkowski, R.; Krzyzanowska, D.; Karczewska, J.; Atkinson, S.; Przysowa, J.; Lojkowska, E.; Williams, P.; Jafra, S.
    Inactivation of AHLs by Ochrobactrum sp. A44 depends on the activity of a novel class of AHL acylase (2011), Environ. Microbiol. Rep., 3, 59-68.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.97 expressed in Escherichia coli BL21(DE3) cells Ochrobactrum sp.
3.5.1.97 gene aiiO, DNA and amino acid sequence determination and analysis, sequence comparisons, complementation of the aiiO::Tn5 mutation with the wild-type aiiO gene, expressionin Escherichia coli strain BL21(DE3) Ochrobactrum sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.97 additional information random transposon mutagenesis, screening of the resulting mutants for the loss of AHL acylase activity. The Tn insertion in mutant A6731 is mapped to a gene termed aiiO Ochrobactrum 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 Ochrobactrum sp. N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs ?
-
 ?
3.5.1.97 additional information Ochrobactrum sp. A44 N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.97 Ochrobactrum sp.
-
-
-
3.5.1.97 Ochrobactrum sp. D8X182 soil isolate, gene aiiO
-
3.5.1.97 Ochrobactrum sp. A44
-
-
-
3.5.1.97 Ochrobactrum sp. A44 D8X182 soil isolate, gene aiiO
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.97 additional information N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs Ochrobactrum sp. ?
-
 ?
3.5.1.97 additional information N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs Ochrobactrum sp. A44 ?
-
 ?
3.5.1.97 N-(3-oxodecanoyl)-L-homoserine lactone + H2O
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 Ochrobactrum sp. L-homoserine lactone + 3-oxodecanoate
-
 ?
3.5.1.97 N-(3-oxodecanoyl)-L-homoserine lactone + H2O
-
 Ochrobactrum sp. A44 L-homoserine lactone + 3-oxodecanoate
-
 ?
3.5.1.97 N-(3-oxododecanoyl)-L-homoserine lactone + H2O
-
 Ochrobactrum sp. L-homoserine lactone + 3-oxododecanoate
-
 ?
3.5.1.97 N-(3-oxododecanoyl)-L-homoserine lactone + H2O
-
 Ochrobactrum sp. A44 L-homoserine lactone + 3-oxododecanoate
-
 ?
3.5.1.97 N-decanoyl-L-homoserine lactone + H2O
-
 Ochrobactrum sp. L-homoserine lactone + decanoate
-
 ?
3.5.1.97 N-decanoyl-L-homoserine lactone + H2O
-
 Ochrobactrum sp. A44 L-homoserine lactone + decanoate
-
 ?
3.5.1.97 N-dodecanoyl-L-homoserine lactone + H2O
-
 Ochrobactrum sp. L-homoserine lactone + dodecanoate
-
 ?
3.5.1.97 N-dodecanoyl-L-homoserine lactone + H2O
-
 Ochrobactrum sp. A44 L-homoserine lactone + dodecanoate
-
 ?
3.5.1.97 N-hexanoyl-L-homoserine lactone + H2O
-
 Ochrobactrum sp. L-homoserine lactone + hexanoate
-
 ?
3.5.1.97 N-hexanoyl-L-homoserine lactone + H2O
-
 Ochrobactrum sp. A44 L-homoserine lactone + hexanoate
-
 ?
3.5.1.97 N-tetradecanoyl-L-homoserine lactone + H2O
-
 Ochrobactrum sp. L-homoserine lactone + tetradecanoate
-
 ?
3.5.1.97 N-tetradecanoyl-L-homoserine lactone + H2O
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 Ochrobactrum sp. A44 L-homoserine lactone + tetradecanoate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.97 AHL acylase
-
 Ochrobactrum sp.
3.5.1.97 AHL amidase
-
 Ochrobactrum sp.
3.5.1.97 AiiO
-
 Ochrobactrum sp.
3.5.1.97 More the enzyme belongs to the alpha/beta hydrolase superfamily Ochrobactrum sp.
3.5.1.97 N-acyl-homoserine lactone acylase
-
 Ochrobactrum sp.

General Information

EC Number General Information Comment Organism
3.5.1.97 physiological function the organism inactivates N-acyl homoserine lactone quorum sensing signal molecules and is capable of quenching the N-acyl homoserine lactone, AHL-dependent virulence of Pectobacterium carotovorum in planta via its AHL inactivating activity Ochrobactrum sp.
3.5.1.97 physiological function the enzyme is capable of quenching the N-acyl-homoserine lactone-dependent virulence of Pectobacterium carotovorum in planta Ochrobactrum sp.