CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.160 | Porin |
|
2.40.160.20 |
Domain Context
CATH Clusters
| Superfamily | 2.40.160.20 |
| Functional Family | Lipid A deacylase |
Enzyme Information
| 3.1.1.77 |
Acyloxyacyl hydrolase.
based on mapping to UniProt Q9HVD1
3-(acyloxy)acyl group of bacterial toxin = 3-hydroxyacyl group of bacterial toxin + a fatty acid.
-!- The substrate is lipid A on the reducing end of the toxic lipopolysaccharide (LPS) of Salmonella typhimurium and related organisms. -!- It consists of diglucosamine, beta-D-GlcN-(1->6)-D-GlcN, attached by glycosylation on O-6 of its non-reducing residue, phosphorylated on O-4 of this residue and on O-1 of its potentially reducing residue. -!- Both residues carry 3-(acyloxy)acyl groups on N-2 and O-3. -!- The enzyme from human leukocytes detoxifies the lipid by hydrolyzing the secondary acyl groups from O-3 of the 3-hydroxyacyl groups on the disaccharide (LPS). -!- It also possesses a wide range of phospholipase and acyltransferase activities (e.g. EC 3.1.1.4, EC 3.1.1.5, EC 3.1.1.32 and EC 3.1.1.52), hydrolyzing diacylglycerol and phosphatidyl compounds, but not triacylglycerols. -!- It has a preference for saturated C(12)-C(16) acyl groups.
|
UniProtKB Entries (1)
| Q9HVD1 |
PAGL_PSEAE
Pseudomonas aeruginosa PAO1
Lipid A deacylase PagL
|
PDB Structure
| PDB | 2ERV |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure and catalytic mechanism of the LPS 3-O-deacylase PagL from Pseudomonas aeruginosa.
Proc.Natl.Acad.Sci.USA
|
