词条 | Acyloxyacyl hydrolase |
释义 |
| Name = acyloxyacyl hydrolase | EC_number = 3.1.1.77 | CAS_number = | IUBMB_EC_number = 3/1/1/77 | GO_code = 0050528 | image = 5w78.jpg | width = 270 | caption = Acyloxyacyl hydrolase heterodimer, Human }} In enzymology, an acyloxyacyl hydrolase ({{EC number|3.1.1.77}}) is an enzyme that catalyzes the chemical reaction 3-(acyloxy)acyl group of bacterial lipopolysaccharide (lipid A moiety) 3-hydroxyacyl group of bacterial lipopolysaccharide + a fatty acid Hence, this enzyme has one substrate, the 3-(acyloxy)acyl groups of bacterial lipopolysaccharides, and two products, [partially deacylated lipopolysaccharide] and fatty acid. The enzyme removes from lipid A the secondary acyl chains that are needed for lipopolysaccharides to be recognized by the MD-2--TLR4 receptor on animal cells. This reaction inactivates the lipopolysaccharide (endotoxin). Acyloxyacyl hydrolase is produced by monocyte-macrophages, neutrophils, dendritic cells, and renal cortical epithelial cells. It is a protein of Mr = ~60,000 that has two disulfide-linked subunits. The smaller subunit, of Mr = ~14,000 (including glycosylation), is a member of the SAPLIP (saposin-like protein) family along with amoebopore, granulysin, acid sphingomyelinase, surfactant protein B, and the 4 sphingolipid activator proteins (saposins). The larger subunit, Mr = 50,000, contains the active site serine and the other elements of the His-Asp-Ser triad; AOAH is a GDSL lipase that has activity toward certain glycerolipids in addition to its presumed major in vivo substrate, LPS. References
2 : EC 3.1.1|Enzymes of unknown structure |
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