Information on EC 3.1.1.77 - acyloxyacyl hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.1.77
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RECOMMENDED NAME
GeneOntology No.
acyloxyacyl hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-(acyloxy)acyl group of bacterial toxin + H2O = 3-hydroxyacyl group of bacterial toxin + a fatty acid
show the reaction diagram
The substrate is lipid A on the reducing end of the toxic lipopolysaccharide, LPS of Salmonella typhimurium and related organisms. It consists of diglucosamine, beta-D-GlcN-(1- 6)-D-GlcN, attached by glycosylation on O-6 of its non-reducing residue, phosphorylated on O-4 of this residue and on O-1 of ist potentially reducing residue. Both residues carry 3-(acyloxy)acyl groups on N-2 and O-3. The enzyme from human leucocytes detoxifies the lipid by hydrolysing the secondary acyl groups from O-3 of the 3-hydroxyacyl groups on the disaccharide, LPS. It also possesses a wide range of phospholipase and acyltransferase activities, e.g. EC 3.1.1.4, phospholipase A2, EC 3.1.1.5, lysophospholipase, EC 3.1.1.32, phospholipase A1 and EC 3.1.1.52, phosphatidylinositol deacylase, hydrolysing diacylglycerol and phosphatidyl compounds, but not triacylglycerols. It has a preference for saturated C12-C16 acyl groups
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-O bond
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CAS REGISTRY NUMBER
COMMENTARY hide
110277-64-0
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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
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
diacylglycerol + H2O
?
show the reaction diagram
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in vitro
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-
?
glycerophospholipid + H2O
?
show the reaction diagram
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in vitro
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-
?
lysophospholipid + H2O
?
show the reaction diagram
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in vitro
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-
?
sn-1,2-dipalmitoylglycerol + H2O
palmitate + glycerol
show the reaction diagram
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in vitro
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?
sn-1,2-dipalmitoylphosphatidylcholine + H2O
palmitate + phosphatidylcholine
show the reaction diagram
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in vitro
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?
additional information
?
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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
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
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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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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
diisopropylfluorophosphate
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p-bromophenacylbromide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dimethylsulfate
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induces enzyme activity when added to the medium
dithiothreitol
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Triton X-100
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00036
diacylphosphatidylethanolamine
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0.0005 - 0.00167
lipopolysaccharide
0.00026
long chain lipopolysaccharide
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0.00031
medium chain lipopolysaccharide
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0.00032
short chain lipopolysaccharide
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000005
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cell lysate
1.555
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 5
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7.2
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
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4.5 - 5.5
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additional information
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from acid to neutral pH
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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cell free
Manually annotated by BRENDA team
blood neutrophil
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7900 - 8100
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SDS-PAGE of deglycosylated small subunit
13800
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small subunit, calculated from sequence of unglycosylated protein
14000 - 20000
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small subunit, SDS-PAGE in presence of 2-mercaptoethanol
14000
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SDS-PAGE, small subunit
47700
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large subunit, calculated from sequence of unglycosylated protein
48000
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SDS-PAGE of large subunit after N-glycanase treatment
50000
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large subunit, SDS-PAGE in presence of 2-mercaptoethanol
52000 - 60000
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native PAGE
52000
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SDS-PAGE, large subunit
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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10 min causes complete inactivation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in BHK 570 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
slight downregulation of enzyme expression by treatment during 24 h lipopolysaccharide or UV-treated group B streptococci, overview
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the enzyme is induced by UV-treated Propionibacterium acnes treatment after 24 h
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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
analysis
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potential use in studies of LPS structure and bioactivity
medicine
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constitutive overexpression of AOAH in vivo hasten recovery from lipopolysaccharide exposure without interfering with the normal acute inflammatory response
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