CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.10 | Orthogonal Bundle | |
1.10.439 | Penicillin Amidohydrolase; domain 1 | |
1.10.439.10 | Penicillin Amidohydrolase, domain 1 |
Domain Context
CATH Clusters
Superfamily | Penicillin Amidohydrolase, domain 1 |
Functional Family |
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.
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UniProtKB Entries (1)
Q9I194 |
PVDQ_PSEAE
Pseudomonas aeruginosa PAO1
Acyl-homoserine lactone acylase PvdQ
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PDB Structure
PDB | 4WKU |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
n-Alkylboronic Acid Inhibitors Reveal Determinants of Ligand Specificity in the Quorum-Quenching and Siderophore Biosynthetic Enzyme PvdQ.
Biochemistry
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