IED Industry Enzyme Database

Detail Information for IndEnz0005000196
IED ID IndEnz0005000196
Enzyme Type ID lipase000196
Protein Name Acyloxyacyl hydrolase
EC 3.1.1.77

Cleaved into: Acyloxyacyl hydrolase small subunit; Acyloxyacyl hydrolase large subunit
Gene Name Aoah
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MKFPWKVFKTTLLLLLLSHSLASVPSEDQPGDSYSHGQSCLGCVVLVSVIEQLAEVHNSSVQVAMERLCSYLPEKLFLKTACYFLVQTFGSDIIKLLDEAMKADVVCYALEFCKRGAVQPQCHLYPLPQEAWESALEKARQVLRRSSTMKYPRSGRNICSLPFLTKICQKIELSIKKAVPFKDIDSDKHSVFPTLRGYHWRGRDCNDSDKTVYPGRRPDNWDIHQDSNCNGIWGIDPKDGIPYEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTASQMSVNSFLNLPSALTDELNWPQLSGVTGFLDSTSGIEEKSIYHRLRKRNHCNHRDYQSISKNGASSRNLKNFIESLSRNQASDHPAIVLYAMIGNDVCNSKADTVPEMTTPEQMYANVMQTLTHLNSHLPNGSHVILYGLPDGTFLWDSLHNRYHPLGQLNKDVTYAQFFSFLRCLQLNPCNGWMSSNKTLRTLTSERAEQLSNTLKKIATTETFANFDLFYVDFAFHEIIEDWQKRGGQPWQLIEPVDGFHPNEVASLLQANRVWEKIQLQWPHVLGKENPFNSQIEEVFGDQGGH
Enzyme Length 574
Uniprot Accession Number O35298
Absorption
Active Site ACT_SITE 262; /evidence=ECO:0000305|PubMed:29343645
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 3-(acyloxy)acyl derivative of bacterial toxin + H2O = 3-hydroxyacyl derivative of bacterial toxin + a fatty acid + H(+); Xref=Rhea:RHEA:12032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:136853, ChEBI:CHEBI:140675; EC=3.1.1.77; Evidence={ECO:0000305|PubMed:12810692, ECO:0000305|PubMed:15155618, ECO:0000305|PubMed:17322564, ECO:0000305|PubMed:18779055, ECO:0000305|PubMed:19860560};
DNA Binding
EC Number 3.1.1.77
Enzyme Function FUNCTION: Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS) (PubMed:12810692, PubMed:15155618, PubMed:17322564, PubMed:19860560). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (PubMed:17322564, PubMed:19860560, PubMed:28622363). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (PubMed:18779055). {ECO:0000269|PubMed:12810692, ECO:0000269|PubMed:15155618, ECO:0000269|PubMed:17322564, ECO:0000269|PubMed:18779055, ECO:0000269|PubMed:19860560, ECO:0000269|PubMed:28622363}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (10); Chain (2); Disulfide bond (9); Domain (1); Glycosylation (4); Helix (29); Metal binding (18); Mutagenesis (1); Propeptide (1); Region (2); Signal peptide (1); Site (1); Turn (13)
Keywords 3D-structure;Calcium;Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Hydrolase;Lipid metabolism;Metal-binding;Reference proteome;Secreted;Signal;Zymogen
Interact With
Induction INDUCTION: Strongly up-regulated in alveolar macrophages in response to bacterial lipopolysaccharides (LPS). {ECO:0000269|PubMed:28622363}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15155618}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P28039}. Note=Detected in urine. {ECO:0000269|PubMed:15155618}.
Modified Residue
Post Translational Modification PTM: Cleaved into a large and a small subunit. {ECO:0000250|UniProtKB:P28039}.; PTM: The small subunit is N-glycosylated. {ECO:0000250|UniProtKB:P28039}.
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000250|UniProtKB:P28039
Structure 3D X-ray crystallography (3)
Cross Reference PDB 5W7D; 5W7E; 5W7F;
Mapped Pubmed ID 11217851; 12466851; 12904583; 14610273; 16155573; 17967808; 18799693; 21267068; 21849675; 22441700; 23675296; 24344308; 25043184; 29118019; 30021797; 31017816; 32003596; 32332915; 32925915; 33250918; 34318715;
Motif
Gene Encoded By
Mass 65,155
Kinetics
Metal Binding METAL 183; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 185; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 185; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 187; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 187; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 189; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 204; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 204; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 206; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 207; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 209; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 212; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 222; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 226; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 228; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 230; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 232; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"; METAL 244; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"
Rhea ID RHEA:12032
Cross Reference Brenda 3.1.1.77;