CATH Classification

Domain Context

CATH Clusters

Superfamily Penicillin Amidohydrolase, domain 1
Functional Family Acyl-homoserine lactone acylase PvdQ

Enzyme Information

3.5.1.97
Acyl-homoserine-lactone acylase.
based on mapping to UniProt Q9I194
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.

UniProtKB Entries (1)

Q9I194
PVDQ_PSEAE
Pseudomonas aeruginosa PAO1
Acyl-homoserine lactone acylase PvdQ

PDB Structure

PDB 4K2G
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Identification of Inhibitors of PvdQ, an Enzyme Involved in the Synthesis of the Siderophore Pyoverdine.
Wurst, J.M., Drake, E.J., Theriault, J.R., Jewett, I.T., VerPlank, L., Perez, J.R., Dandapani, S., Palmer, M., Moskowitz, S.M., Schreiber, S.L., Munoz, B., Gulick, A.M.
Acs Chem.Biol.