| IED ID | IndEnz0005000398 |
| Enzyme Type ID | lipase000398 |
| Protein Name |
Acyloxyacyl hydrolase EC 3.1.1.77 Cleaved into: Acyloxyacyl hydrolase small subunit; Acyloxyacyl hydrolase large subunit |
| Gene Name | AOAH |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MQSPWKILTVAPLFLLLSLQSSASPANDDQSRPSLSNGHTCVGCVLVVSVIEQLAQVHNSTVQASMERLCSYLPEKLFLKTTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFCKQNTGQPLCHLYPLPKETWKFTLQKARQIVKKSPILKYSRSGSDICSLPVLAKICQKIKLAMEQSVPFKDVDSDKYSVFPTLRGYHWRGRDCNDSDESVYPGRRPNNWDVHQDSNCNGIWGVDPKDGVPYEKKFCEGSQPRGIILLGDSAGAHFHISPEWITASQMSLNSFINLPTALTNELDWPQLSGATGFLDSTVGIKEKSIYLRLWKRNHCNHRDYQNISRNGASSRNLKKFIESLSRNKVLDYPAIVIYAMIGNDVCSGKSDPVPAMTTPEKLYSNVMQTLKHLNSHLPNGSHVILYGLPDGTFLWDNLHNRYHPLGQLNKDMTYAQLYSFLNCLQVSPCHGWMSSNKTLRTLTSERAEQLSNTLKKIAASEKFTNFNLFYMDFAFHEIIQEWQKRGGQPWQLIEPVDGFHPNEVALLLLADHFWKKVQLQWPQILGKENPFNPQIKQVFGDQGGH |
| Enzyme Length | 575 |
| Uniprot Accession Number | P28039 |
| Absorption | |
| Active Site | ACT_SITE 263; /evidence="ECO:0000305|PubMed:29343645, ECO:0000305|PubMed:8089145" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:29343645}. |
| 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:0000269|PubMed:1883828, ECO:0000269|PubMed:29343645, ECO:0000269|PubMed:8089145}; |
| 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 (PubMed:1883828, PubMed:8089145, PubMed:29343645). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (By similarity). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (By similarity). {ECO:0000250|UniProtKB:O35298, ECO:0000269|PubMed:1883828, ECO:0000269|PubMed:29343645, ECO:0000269|PubMed:8089145}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Beta strand (13); Chain (2); Disulfide bond (8); Domain (1); Glycosylation (4); Helix (29); Metal binding (18); Mutagenesis (8); Natural variant (3); Propeptide (1); Region (2); Sequence conflict (1); Signal peptide (1); Site (1); Turn (13) |
| Keywords | 3D-structure;Alternative splicing;Calcium;Cytoplasmic vesicle;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lipid metabolism;Metal-binding;Reference proteome;Secreted;Signal;Zymogen |
| Interact With | Q15700 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8089145, ECO:0000305|PubMed:1883828}. Cytoplasmic vesicle {ECO:0000269|PubMed:8089145}. Note=Detected in urine. {ECO:0000250|UniProtKB:O35298}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved into a large and a small subunit. {ECO:0000269|PubMed:1883828, ECO:0000269|PubMed:29343645, ECO:0000269|PubMed:8089145}.; PTM: The small subunit is N-glycosylated. {ECO:0000269|PubMed:8089145}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000269|PubMed:8089145 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5W78; 5W7C; |
| Mapped Pubmed ID | 15174051; 16815140; 20237496; 20379614; 22723975; 26319989; 27888910; |
| Motif | |
| Gene Encoded By | |
| Mass | 65,105 |
| Kinetics | |
| Metal Binding | METAL 184; /note=Calcium 1; /evidence=ECO:0000269|PubMed:29343645; METAL 186; /note=Calcium 1; /evidence=ECO:0000269|PubMed:29343645; METAL 186; /note=Calcium 2; /evidence=ECO:0000269|PubMed:29343645; METAL 188; /note=Calcium 1; /evidence=ECO:0000269|PubMed:29343645; METAL 188; /note=Calcium 2; /evidence=ECO:0000269|PubMed:29343645; METAL 190; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:29343645; METAL 205; /note=Calcium 1; /evidence=ECO:0000269|PubMed:29343645; METAL 205; /note=Calcium 2; /evidence=ECO:0000269|PubMed:29343645; METAL 207; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:29343645; METAL 208; /note=Calcium 1; /evidence=ECO:0000269|PubMed:29343645; METAL 210; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:29343645; METAL 213; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:29343645; METAL 223; /note=Calcium 3; /evidence=ECO:0000269|PubMed:29343645; METAL 227; /note=Calcium 3; /evidence=ECO:0000269|PubMed:29343645; METAL 229; /note=Calcium 3; /evidence=ECO:0000269|PubMed:29343645; METAL 231; /note=Calcium 3; /evidence=ECO:0000269|PubMed:29343645; METAL 233; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:29343645; METAL 245; /note=Calcium 3; /evidence=ECO:0000269|PubMed:29343645 |
| Rhea ID | RHEA:12032 |
| Cross Reference Brenda | 3.1.1.77; |