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CATH Superfamily 3.60.20.10

Aminohydrolase, N-terminal nucleophile (Ntn) domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:

"
Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 186: Acyl-homoserine lactone acylase PvdQ

There are 1 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Acyl-homoserine-lactone acylase. [EC: 3.5.1.97]
An N-acyl-L-homoserine lactone + H(2)O = L-homoserine lactone + a carboxylate.
  • Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing.
  • Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signaling which, in turn, initiates the expression of particular virulence genes.
  • Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL- signaling and the expression of virulence genes in quorum-sensing bacteria.
  • This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine lactone ring of AHL-dependent quorum-sensing signal molecules.
  • It has broad specificity for AHLs with side changes ranging in length from 11 to 14 carbons.
  • Substituents at the 3'-position, as found in N-(3-oxododecanoyl)-L- homoserine lactone, do not affect this activity.
 6 A0A1G5LZ86 A0A1G5LZ86 A0A454LM54 A0A454LM54 Q9I194 Q9I194
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