ENZYME entry: EC 184.108.40.206
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|a 3-(acyloxy)acyl derivative of bacterial toxin + H2O <=> 3-hydroxyacyl derivative of bacterial toxin + a fatty acid + H(+)|
- The substrate is lipid A on the reducing end of the toxic
lipopolysaccharide (LPS) of Salmonella typhimurium and related
- 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
- It also possesses a wide range of phospholipase and acyltransferase
activities (e.g. EC 220.127.116.11, EC 18.104.22.168, EC 22.214.171.124 and
EC 126.96.36.199), hydrolyzing diacylglycerol and phosphatidyl compounds,
but not triacylglycerols.
- It has a preference for saturated C12-C16 acyl groups.
|PRIAM enzyme-specific profiles||188.8.131.52|
|KEGG Ligand Database for Enzyme Nomenclature||184.108.40.206|
|IUBMB Enzyme Nomenclature||220.127.116.11|
|MEDLINE||Find literature relating to 18.104.22.168|
|Rhea expert-curated reactions||22.214.171.124|
entries corresponding to 3.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-