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Information on EC 3.1.1.47 - 1-alkyl-2-acetylglycerophosphocholine esterase and Organism(s) Rattus norvegicus and UniProt Accession O35264

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Rattus norvegicus
UNIPROT: O35264 not found.
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
lp-pla2, lipoprotein-associated phospholipase a2, paf acetylhydrolase, acetylhydrolase, plasma paf-ah, platelet-activating factor acetylhydrolase, paf-acetylhydrolase, pla2g7, lppla2, pafah, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(PAF)-acetylhydrolase
-
-
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine: acetylhydrolase
-
-
-
-
1-alkyl-2-acetylglycerophosphocholine esterase
-
-
-
-
1-alkyl-2-acetyllecithin deacetylase
-
-
-
-
2-acetyl-1-alkylglycerophosphocholine esterase
-
-
-
-
acetylhydrolase
-
-
-
-
alkylacetyl-GPC:acetylhydrolase
-
-
-
-
blood platelet-activating factor-acetyl hydrolase
-
-
-
-
deacetylase, 1-alkyl-2-acetyllecithin
-
-
-
-
HSD-PLA2
-
-
-
-
LDL-associated phospholipase A2
-
-
-
-
LDL-PLA(2)
-
-
-
-
Lissencephaly-1 protein
-
-
-
-
PAF 2-acylhydrolase
-
-
-
-
PAF acetylhydrolase
PAF acetylhydrolase I
-
PAF acetylhydrolase II
-
PAF-acetylhydrolase
PAF-AH
PAF-AH alpha
-
-
-
-
PAFAH alpha
-
-
-
-
phosphatide 2-acylhydrolase
-
-
-
-
platelet activating factor acetylhydrolase
-
-
platelet-activating factor acetylhadrolase
-
-
platelet-activating factor acetylhydrolase
platelet-activating factor acetylhydrolyase
-
-
-
-
platelet-activating factor acetylohydrolase
-
-
Serine dependent phospholipase A2
-
-
-
-
additional information
-
platelet-activating factor-dependent transacetylase, PAF-TA, and platelet-activating factor acetylhydrolase isozyme II, PAF-AH II, might be the same enzyme
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
show the reaction diagram
isozyme II of the enzyme also performs platelet-activating factor-dependent transacetylation, transfer of an acetyl group from platelet-activating factor to endogenous acceptor lipids
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
76901-00-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-hexadecyl-2-acetyl-sn-glycerol-3-phosphocholine + H2O
1-hexadecyl-sn-glycerol-3-phosphocholine + acetate
show the reaction diagram
1-hexadecyl-2-glutaryl-sn-glycero-3-phosphocholine + H2O
1-hexadecyl-glycero-3-phosphocholine + glutarate
show the reaction diagram
-
-
-
?
1-hexadecyl-2-succinyl-sn-glycero-3-phosphocholine + H2O
1-hexadecyl-glycero-3-phosphocholine + succinate
show the reaction diagram
-
-
-
?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycero-3-phosphocholine + acetate
show the reaction diagram
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
?
show the reaction diagram
-
i.e. PAF
-
-
?
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
show the reaction diagram
2-acetyl-1-hexadecyl-sn-glycero-3-phosphocholine + H2O
1-hexadecyl-sn-glycero-3-phosphocholine + acetate
show the reaction diagram
-
i.e. platelet-activation factor
-
?
2-acetyl-1-O-alkyl-sn-glycero-3-phosphoric acid + H2O
1-O-alkyl-sn-glycero-3-phosphoric acid + acetate
show the reaction diagram
-
-
-
?
2-hexadecyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-hexadecyl-sn-glycero-3-phosphocholine + acetate
show the reaction diagram
-
i.e. platelet-activation factor, substrate and enzyme play important roles in inflammation processes
-
?
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
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycero-3-phosphocholine + acetate
show the reaction diagram
regulation of platelet-activating factor, anti apoptotic protein
-
-
?
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
?
show the reaction diagram
-
i.e. PAF
-
-
?
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
show the reaction diagram
2-acetyl-1-O-alkyl-sn-glycero-3-phosphoric acid + H2O
1-O-alkyl-sn-glycero-3-phosphoric acid + acetate
show the reaction diagram
-
-
-
?
2-hexadecyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-hexadecyl-sn-glycero-3-phosphocholine + acetate
show the reaction diagram
-
i.e. platelet-activation factor, substrate and enzyme play important roles in inflammation processes
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no stimulation by Ca2+ or Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-Alkyl-2,3-diacetyl-sn-glycerol
-
slight
1-Hexadecyl-2-acetyl-sn-glycero-3-phosphoethanolamine
-
-
2-acetyl-1-acyl-glycero-sn-glycero-3-phosphocholine
-
-
3-Hexadecyl-2-acetyl-sn-glycero-1-phosphocholine
-
-
5,5'-dithiobis-2-nitrobenzoic acid
-
BN 50739
-
antagonists of lipopolysaccharides, inhibition of induction of plasma enzyme expression
Ca2+
-
18% inhibition at 10 mM
deoxycholate
-
-
diisopropyl fluorophosphates
-
diisopropylfluorophosphate
-
-
DTNB
-
69% inhibition at 2 mM
Estrogens
-
regulatory function on the enzyme form from plasma
-
lipopolysaccharides
-
regulatory function on the enzyme form from Kupffer cells, plasma, lung, liver, spleen, bile, kidney, thymus, peritoneal macrophages, and peripheral leukocytes
-
lyso-2-hexadecyl-1-alkyl-sn-glycero-3-phosphocholine
-
22% inhibition at 0.05 mM
lyso-platelet-activating factor
-
regulatory function on the enzyme form from hepatocytes
phenylmethylsulfonyl fluoride
-
-
phosphatidylcholine
-
from egg, long chain diacetyl type, slight
phosphocholine
-
25% inhibition at 0.05 mM
PMSF
-
93% inhibition at 2 mM
WEB 2170
-
antagonists of lipopolysaccharides, inhibition of induction of plasma enzyme expression
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
corticoids
-
regulatory function on the enzyme form from plasma
-
dithiothreitol
-
slightly acivating
lipopolysaccharides
-
induce plasma enzyme expression in several tissues, overview, induction is 50% inhibited by administration of antagonists BN 50739 and WEB 2170
-
platelet-activating factor
-
regulatory function on the enzyme form from hepatocytes
progestin
-
regulatory function on the enzyme form from plasma
turpentine
-
regulatory function on the enzyme form from plasma
-
zymosan
-
regulatory function on the enzyme form from plasma
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0031
1-hexadecyl-2-acetyl-sn-glycerol-3-phosphocholine
-
-
0.0049
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
-
pH 7.2, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000012
-
PAF-AH isozyme Ib alpha2 subunit, transacetylase activity
0.00028
-
PAF-AH isozyme Ib alpha1 subunit, acetylhydrolase activity
0.00236
-
PAF-AH isozyme Ib alpha2 subunit, acetylhydrolase activity
0.02
-
partially purified enzyme
0.0408
-
PAF-AH isozyme II, transacetylase activity
0.105
-
PAF-AH isozyme II, acetylhydrolase activity
0.114
-
plasma PAF-AH, transacetylase activity
0.131
-
plasma PAF-AH, acetylhydrolase activity
0.47
-
supernatant fraction
0.55
-
alveolar type II cells and 1000 x g fraction
0.77
-
macrophages
0.85
-
100000 x g fraction
1.32
-
60000 x g fraction
27.1
-
plasma
3.7
-
bronchoalveolar lavage
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
broad optimum
7.5 - 8.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.4
-
inactivation below pH 5.0, active to mild alkaline range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
plasma isozyme
Manually annotated by BRENDA team
clonal derivative of PC12 cell line
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
4 isozymes, i.e. isozyme Ia, Ib, II, and the erythrocyte form, physiological functions, overview
Manually annotated by BRENDA team
additional information
-
activity in subcellular fractions
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
glimepiride and glibenclamide reverse elevated plasma PAF-AH activity in plasma of streptozotocin-induced hyperglycemic rats, but have no effects in control rats, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LPP60_RAT
564
0
60795
Swiss-Prot
other Location (Reliability: 3)
PA1B3_RAT
232
0
25863
Swiss-Prot
other Location (Reliability: 1)
LCAT_RAT
440
1
49882
Swiss-Prot
Secretory Pathway (Reliability: 1)
PA1B2_RAT
229
0
25581
Swiss-Prot
other Location (Reliability: 1)
PAFA2_RAT
390
0
43492
Swiss-Prot
other Location (Reliability: 2)
A0A0G2JT51_RAT
383
0
42396
TrEMBL
other Location (Reliability: 2)
Q5M7T7_RAT
440
0
49491
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8I5Y241_RAT
418
0
46585
TrEMBL
other Location (Reliability: 2)
A0A8I6GE94_RAT
410
0
45930
TrEMBL
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
x * 66000, major part, + x * 37000, mino part, SDS-PAGE
40000
-
x * 40000, cytosolic and membraneous PAF-TA, SDS-PAGE, x * 43491, PAF-AH isozyme II, amino acid sequence calculation
43491
-
x * 40000, cytosolic and membraneous PAF-TA, SDS-PAGE, x * 43491, PAF-AH isozyme II, amino acid sequence calculation
66000
-
x * 66000, major part, + x * 37000, mino part, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
intracellular isozyme II, and plasma enzyme form
trimer
-
the intracellular G-protein-like isozyme Ib consists of two catalytic subunits alpha1 and alpha2 and one regulatory subunit beta
additional information
-
isozyme I exists of alpha1 and alpha2 subunits, catalytic subunits, tertiary structure, as well as of a beta-subunit, the beta-subunit is a regulatory one, isozyme II is a monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
side-chain modification
-
N-linked glycosylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C120S
-
site-directed mutagenesis, residue is involved in transacetylase reaction mechanism, mutant shows 35% reduced transacetylase activity but unaltered acetylhydrolase activity
G2A
-
site-directed mutagenesis, residue is involved in transacetylase reaction mechanism, mutant shows 50% reduced transacetylase activity but unaltered acetylhydrolase activity
G2A/C120S
-
site-directed mutagenesis, residues are involved in transacetylase reaction mechanism, mutant shows 80% reduced transacetylase activity but unaltered acetylhydrolase activity
S234C
-
site-directed mutagenesis, inactive mutant
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
30 min, stable
60
-
10 min, almost complete inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from adipocyte, 45.9fold
-
PAF-transacetylase from kidney cytosol, to homogeneity, recombinant PAF-AH isozyme II from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
PAF-AH isozyme II, DNA and amino acid sequence determination and analysis, expression of wild-type enzyme in Escherichia coli, expression of isozyme II mutant enzymes in CHO-K1 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
hyperglycemia increases in plasma PAF-AH activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Blank, M.L.; Lee, T.; Fitzgerald, V.; Snyder, F.
A specific acetylhydrolase for 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (a hypotensive and platelet-activating lipid)
J. Biol. Chem.
256
175-178
1981
Rattus norvegicus
Manually annotated by BRENDA team
Svetlov, S.; Howard, K.M.; Debuysere, M.S.; Olson, M.S.
Secretory PAF-acetylhydrolase of the rat hepatobiliary system: characterization and partial purification
Am. J. Physiol.
274
G891-G900
1998
Rattus norvegicus
Manually annotated by BRENDA team
Tjoelker, L.W.; Stafforini, D.M.
Platelet-activating factor acetylhydrolases in health and disease
Biochim. Biophys. Acta
1488
102-123
2000
Oryctolagus cuniculus, Cricetinae, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Jehle, R.; Schlame, M.; Buttner, C.; Frey, B.; Sinha, P.; Rustow, B.
Platelet-activating factor (PAF)-acetylhydrolase and PAF-like compounds in the lung: effects of hyperoxia
Biochim. Biophys. Acta
1532
60-66
2001
Rattus norvegicus
Manually annotated by BRENDA team
Arai, H.; Koizumi, H.; Aoki, J.; Inoue, K.
Platelet-activating factor acetylhydrolase (PAF-AH)
J. Biochem.
131
635-640
2002
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Howard, K.M.; Olson, M.S.
The expression and localization of plasma platelet-activating factor acetylhydrolase in endotoxemic rats
J. Biol. Chem.
275
19891-19896
2000
Rattus norvegicus
Manually annotated by BRENDA team
Bae, K.; Longobardi, L.; Karasawa, K.; Malone, B.; Inoue, T.; Aoki, J.; Arai, H.; Inoue, K.; Lee, T.
Platelet-activating factor (PAF)-dependent transacetylase and its relationship with PAF acetylhydrolases
J. Biol. Chem.
275
26704-26709
2000
Rattus norvegicus
Manually annotated by BRENDA team
Chroni, A.; Mavri-Vavayanni, M.
Characterization of a platelet activating factor acetylhydrolase from rat adipocyte
Life Sci.
67
2807-2825
2000
Rattus norvegicus
Manually annotated by BRENDA team
Bonin, F.; Ryan, S.D.; Migahed, L.; Mo, F.; Lallier, J.; Franks, D.J.; Arai, H.; Bennett, S.A.
Anti-apoptotic actions of the platelet-activating factor acetylhydrolase I alpha2 catalytic subunit
J. Biol. Chem.
279
52425-52436
2004
Rattus norvegicus (P83006)
Manually annotated by BRENDA team
Grypioti, A.D.; Mykoniatis, M.; Demopoulos, C.A.; Kostopanagiotou, G.
Recombinant platelet-activating factor-acetylhydrolase attenuates paracetamol-induced liver oxidative stress, injury, and regeneration
Digest. Dis. Sci.
52
192-199
2007
Rattus norvegicus (O35264 and O35263), Rattus norvegicus
Manually annotated by BRENDA team
Wojcicka, G.; Jamroz-Wisniewska, A.; Marciniak, A.; Lowicka, E.; Beltowski, J.
The differentiating effect of glimepiride and glibenclamide on paraoxonase 1 and platelet-activating factor acetylohydrolase activity
Life Sci.
87
126-132
2010
Rattus norvegicus
Manually annotated by BRENDA team