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Information on EC 3.1.1.77 - acyloxyacyl hydrolase and Organism(s) Homo sapiens and UniProt Accession P28039

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     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.77 acyloxyacyl hydrolase
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: P28039 not found.
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
acyloxyacyl hydrolase, AOAH, neutrophil acyloxyacyl hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
neutrophil acyloxyacyl hydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-O bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
110277-64-0
-
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
-
in vitro
-
-
?
glycerophospholipid + H2O
?
show the reaction diagram
-
in vitro
-
-
?
lysophospholipid + H2O
?
show the reaction diagram
-
in vitro
-
-
?
sn-1,2-dipalmitoylglycerol + H2O
palmitate + glycerol
show the reaction diagram
-
in vitro
-
?
sn-1,2-dipalmitoylphosphatidylcholine + H2O
palmitate + phosphatidylcholine
show the reaction diagram
-
in vitro
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
diisopropylfluorophosphate
-
-
p-bromophenacylbromide
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dimethylsulfate
-
induces enzyme activity when added to the medium
dithiothreitol
-
-
Triton X-100
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00036
diacylphosphatidylethanolamine
-
-
0.00055 - 0.00167
lipopolysaccharide
0.00026
long chain lipopolysaccharide
-
-
-
0.00031
medium chain lipopolysaccharide
-
-
-
0.00032
short chain lipopolysaccharide
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000005
-
cell lysate
1.555
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 5.5
-
-
additional information
-
from acid to neutral pH
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
acyloxyacyl hydrolase acts as one of the diverse antimicrobial peptides and proteins expressed in the placenta
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
AOAH_HUMAN
575
0
65105
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7900 - 8100
-
SDS-PAGE of deglycosylated small subunit
13800
-
small subunit, calculated from sequence of unglycosylated protein
14000 - 20000
-
small subunit, SDS-PAGE in presence of 2-mercaptoethanol
14000
-
SDS-PAGE, small subunit
47700
-
large subunit, calculated from sequence of unglycosylated protein
48000
-
SDS-PAGE of large subunit after N-glycanase treatment
50000
-
large subunit, SDS-PAGE in presence of 2-mercaptoethanol
52000 - 60000
-
native PAGE
52000
-
SDS-PAGE, large subunit
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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
-
the enzyme is induced by UV-treated Propionibacterium acnes treatment after 24 h
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
potential use in studies of LPS structure and bioactivity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Erwin, A.L.; Munford, R.S.
Deacylation of structurally diverse lipopolysaccharides by human acyloxyacyl hydrolase
J. Biol. Chem.
265
16444-16449
1990
Homo sapiens
Manually annotated by BRENDA team
Hagen, F.S.; Grant, F.J.; Kuijper, J.L.; Slaughter, C.A.; Moomaw, C.R.; Orth, K.; O'Hara, P.J.; Munford, R.S.
Expression and characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides
Biochemistry
30
8415-8423
1991
Homo sapiens
Manually annotated by BRENDA team
Munford, R.S.; Hunter, J.P.
Acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides, has phospholipase, lysophospholipase, diacylglycerollipase, and acyltransferase activities in vitro
J. Biol. Chem.
267
10116-10121
1992
Homo sapiens
Manually annotated by BRENDA team
Munford, R.S.; Hall, C.L.
Detoxification of bacterial lipopolysaccharides (endotoxins) by a human neutrophil enzyme
Science
234
203-205
1986
Homo sapiens
Manually annotated by BRENDA team
Munford, R.S.; Hall, C.L.
Purification of acyloxyacyl hydrolase, a leukocyte enzyme that removes secondary acyl chains from bacterial lipopolysaccharides
J. Biol. Chem.
264
15613-15619
1989
Homo sapiens
Manually annotated by BRENDA team
Mc Dermott, C.M.; Cullor, J.S.; Fenwick, B.W.
Intracellular and extracellular enzymatic deacylation of bacterial endotoxin during localized inflammation induced by Escherichia coli
Infect. Immun.
59
487-485
1991
Bos taurus, Homo sapiens
-
Manually annotated by BRENDA team
Munford, R.S.; Erwin, A.L.
Eukaryotic lipopolysaccharide deacylation enzyme
Methods Enzymol.
209
485-492
1992
Homo sapiens
Manually annotated by BRENDA team
Staab, J.F.; Ginkel, D.L.; Rosenberg, G.B.; Munford, R.S.
A saposin-like domain influences the intracellular localization, stability, and catalytic activity of human acyloxyacyl hydrolase
J. Biol. Chem.
269
23736-23742
1994
Homo sapiens
Manually annotated by BRENDA team
Staab, J.F.; Fosmire, S.; Zhang, M.; Varley, A.W.; Munford, R.S.
Distinctive structural features are shared by human, lapine, and murine acloxyacyl hydrolases
J. Endotoxin Res.
5
205-208
1999
Homo sapiens, Mus musculus, Oryctolagus cuniculus
-
Manually annotated by BRENDA team
Barnes, K.C.; Grant, A.; Gao, P.; Baltadjieva, D.; Berg, T.; Chi, P.; Zhang, S.; Zambelli-Weiner, A.; Ehrlich, E.; Zardkoohi, O.; Brummet, M.E.; Stockton, M.; Watkins, T.; Gao, L.; Gittens, M.; Wills-Karp, M.; Cheadle, C.; Beck, L.A.; Beaty, T.H.; Becker, K.G.; garcia, J.G.N.; Mathias, R.A.
Polymorphisms in the novel gene acyloxyacyl hydroxylase (AOAH) are associated with asthma and associated phenotypes
J. Allergy Clin. Immunol.
118
70-77
2006
Homo sapiens (P28039)
Manually annotated by BRENDA team
Gioannini, T.L.; Teghanemt, A.; Zhang, D.; Prohinar, P.; Levis, E.N.; Munford, R.S.; Weiss, J.P.
Endotoxin-binding proteins modulate the susceptibility of bacterial endotoxin to deacylation by acyloxyacyl hydrolase
J. Biol. Chem.
282
7877-7884
2007
Homo sapiens
Manually annotated by BRENDA team
Klaffenbach, D.; Friedrich, D.; Strick, R.; Strissel, P.L.; Beckmann, M.W.; Rascher, W.; Gessner, A.; Doetsch, J.; Meissner, U.; Schnare, M.
Contribution of different placental cells to the expression and stimulation of antimicrobial proteins (AMPs)
Placenta
32
830-837
2011
Homo sapiens
Manually annotated by BRENDA team
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