Information on EC 3.1.1.77 - acyloxyacyl hydrolase and Organism(s) Mus musculus and UniProt Accession O35298

for references in articles please use BRENDA:EC3.1.1.77
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Mus musculus
UNIPROT: O35298
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The taxonomic range for the selected organisms is: Mus musculus

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.1.77
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RECOMMENDED NAME
GeneOntology No.
acyloxyacyl hydrolase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-O bond
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-
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CAS REGISTRY NUMBER
COMMENTARY hide
110277-64-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-(acyloxy)acyl group of bacterial toxin + H2O
3-hydroxyacyl group of bacterial toxin + a fatty acid
show the reaction diagram
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host AOAH selectively removes the secondary fatty acyl chains from bacterial lipopolysaccharides, that are required for lipopolysaccharide recognition by its mammalian signaling receptor, MD-2-TLR4. Possibility that AOAH, by inactivating bacterial lipopolysaccharide within the liver and spleen, is an important endogenous control mechanism. Recombinant AOAH restores hepatic LPS deacylation and prevented LPS-induced hepatomegaly in Aoah-/- mice
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-
?
3-(acyloxy)acyl group of bacterial toxin
3-hydroxyacyl group of bacterial toxin + a fatty acid
show the reaction diagram
3-(acyloxy)acyl group of bacterial toxin + H2O
3-hydroxyacyl group of bacterial toxin + a fatty acid
show the reaction diagram
additional information
?
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the enzyme inactivates lipopolysaccharides deacylating secondary fatty acyl chains on the lipid A moiety of lipopolysaccharide
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-(acyloxy)acyl group of bacterial toxin + H2O
3-hydroxyacyl group of bacterial toxin + a fatty acid
show the reaction diagram
-
host AOAH selectively removes the secondary fatty acyl chains from bacterial lipopolysaccharides, that are required for lipopolysaccharide recognition by its mammalian signaling receptor, MD-2-TLR4. Possibility that AOAH, by inactivating bacterial lipopolysaccharide within the liver and spleen, is an important endogenous control mechanism. Recombinant AOAH restores hepatic LPS deacylation and prevented LPS-induced hepatomegaly in Aoah-/- mice
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-
?
3-(acyloxy)acyl group of bacterial toxin
3-hydroxyacyl group of bacterial toxin + a fatty acid
show the reaction diagram
additional information
?
-
-
the enzyme inactivates lipopolysaccharides deacylating secondary fatty acyl chains on the lipid A moiety of lipopolysaccharide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005
lipopolysaccharide
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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low activity
Manually annotated by BRENDA team
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of both the colon and small intestines
Manually annotated by BRENDA team
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renal corticular tubule cells produce AOAH and secrete it into urine, where it can deacylate lipopolysaccharides
Manually annotated by BRENDA team
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low activity
Manually annotated by BRENDA team
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interleukin 17-secreting CD4+ helper T cells
Manually annotated by BRENDA team
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renal corticular tubule cells produce AOAH and secrete it into urine, where it can deacylate lipopolysaccharides
Manually annotated by BRENDA team
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renal corticular tubule cells produce AOAH and secrete it into urine, where it can deacylate lipopolysaccharides
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
Mus musculus;
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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disufide linked hetrodimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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only three glycosylation sites in large subunit; small subunit not glycosylated
proteolytic modification
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proximal tubule cells secrete the pro-enzyme, which can be taken up by bladder cells and processed to the heterodimeric, more enzymatically active, mature enzyme form
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in BHK 570 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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AOAH-deficient (Aoah-/-) mice, recovery from the tolerant state induced by Gram-negative bacteria is greatly delayed in mice that lack acyloxyacyl hydrolase (AOAH). Wild-type mice regain normal responsiveness within 14 days after they receive an intraperitoneal injection of LPS or Gram-negative bacteria, AOAH-deficient mice have greatly reduced proinflammatory responses to a second LPS injection for at least 3 weeks
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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constitutive overexpression of AOAH in vivo hasten recovery from lipopolysaccharide exposure without interfering with the normal acute inflammatory response