| IED ID | IndEnz0005000228 |
| Enzyme Type ID | lipase000228 |
| Protein Name |
Acyloxyacyl hydrolase EC 3.1.1.77 Cleaved into: Acyloxyacyl hydrolase small subunit; Acyloxyacyl hydrolase large subunit |
| Gene Name | AOAH |
| Organism | Oryctolagus cuniculus (Rabbit) |
| 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) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit) |
| Enzyme Sequence | MKSPWRILVVSPLLLLPLHSSTSRAHDNQPGTIRSDHYTCVGCVLVVSVIEQLAQVHNSTVQASMERLCSYLPEEWVLKTACYMMVHVFGADIIKLFDKDVNADVVCHTLEFCKQEPGQPLCHLYPLPKESWKFTLEKARHIVKQSPIMKYTRSGAGICSLPFLAKICQKIKLAIKNSVPIKDVDSDKYSIFPTLRGYHWRGRDCNDSDKTVYPGRRPDNWDAHRDSNCNGIWGVDPKDGIPYEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTVSQMSVNSFLNLPTAVTNELDWPQLSGTTGFLDSASKIKENSIYLRLRKRNRCNHRDYQNISKNGASSRNVKSLIESLSRNQLLDHPAIVIYAMIGNDVCNGRKTDPVSAMTTPEQLYANVLKMLEALNSHLPTGSHVILYGLAHGAFLWDTLHSRYHPLGQLNKDVTYTQLYSFLGCLQVSPCPGWMSANETLRALTSERAQQLSETLRKIAASKKFTNFNLFYLDFAFQEVVEEWQKMGGQPWELIEAVDGFHPNEVALLLFADQLWEKVQRQWPDVLGKENPFNPQIEEVFGDQGGH |
| Enzyme Length | 575 |
| Uniprot Accession Number | O18823 |
| 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:0000250|UniProtKB:P28039}; |
| 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). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses. In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria. {ECO:0000250|UniProtKB:O35298}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (10); Chain (2); Disulfide bond (8); Domain (1); Glycosylation (3); Helix (28); Metal binding (18); Mutagenesis (1); Propeptide (1); Region (2); Signal peptide (1); Site (2); Turn (12) |
| Keywords | 3D-structure;Calcium;Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Hydrolase;Lipid metabolism;Metal-binding;Reference proteome;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P28039}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P28039}. Note=Detected in urine. {ECO:0000250|UniProtKB:O35298}. |
| 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..25; /evidence=ECO:0000250|UniProtKB:P28039 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5W7A; 5W7B; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 65,053 |
| Kinetics | |
| Metal Binding | METAL 183; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A, ECO:0007744|PDB:5W7B"; METAL 185; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A, ECO:0007744|PDB:5W7B"; METAL 185; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A"; METAL 187; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A, ECO:0007744|PDB:5W7B"; METAL 187; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A"; METAL 189; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A, ECO:0007744|PDB:5W7B"; METAL 204; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7B"; METAL 204; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A"; METAL 206; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A"; METAL 207; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A, ECO:0007744|PDB:5W7B"; METAL 209; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A"; METAL 212; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A"; METAL 222; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A"; METAL 226; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A"; METAL 228; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A"; METAL 230; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A"; METAL 232; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A"; METAL 244; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7A" |
| Rhea ID | RHEA:12032 |
| Cross Reference Brenda |