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Information on EC 3.1.1.47 - 1-alkyl-2-acetylglycerophosphocholine esterase and Organism(s) Bos taurus and UniProt Accession P68401

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Bos taurus
UNIPROT: P68401 not found.
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
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
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine: acetylhydrolase
-
-
-
-
1-alkyl-2-acetylglycerophosphocholine esterase
-
-
-
-
1-alkyl-2-acetyllecithin deacetylase
-
-
-
-
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetylhydrolase
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2-acetyl-1-alkylglycerophosphocholine esterase
-
-
-
-
acetylhydrolase
-
-
-
-
alkylacetyl-GPC:acetylhydrolase
-
-
-
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blood platelet-activating factor-acetyl hydrolase
-
-
-
-
deacetylase, 1-alkyl-2-acetyllecithin
-
-
-
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HSD-PLA2
-
-
-
-
LDL-associated phospholipase A2
-
-
-
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LDL-PLA(2)
-
-
-
-
Lissencephaly-1 protein
-
-
-
-
PAF 2-acylhydrolase
-
-
-
-
PAF acetylhydrolase
PAF-acetylhydrolase
PAF-AH
PAF-AH alpha
-
-
-
-
PAFAH alpha
-
-
-
-
phosphatide 2-acylhydrolase
-
-
-
-
platelet activating factor acetylhydrolase
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platelet activating factor-acetylhydrolase
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-
platelet-activating factor acetylhydrolase
platelet-activating factor acetylhydrolyase
-
-
-
-
Serine dependent phospholipase A2
-
-
-
-
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
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
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CAS REGISTRY NUMBER
COMMENTARY hide
76901-00-3
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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
-
i.e. PAF
-
?
1-hexadecyl-2-butyryl-sn-glycero-3-phosphocholine + H2O
1-hexadecyl-glycero-3-phosphocholine + butanoate
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-propionyl-sn-glycero-3-phosphocholine + H2O
1-hexadecyl-glycero-3-phosphocholine + propionate
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
1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid + H2O
1-O-alkyl-sn-glycero-3-phosphoric acid + acetate
show the reaction diagram
-
preferred substrate for the alpha1/alpha1 homodimer and the alpha1/alpha2 heterodimer
-
?
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
show the reaction diagram
acetylated platelet-activation factor + H2O
?
show the reaction diagram
-
-
-
?
oxidized phospholipids + H2O
?
show the reaction diagram
-
protection against toxic effects of oxidized phospholipids
-
-
?
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
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O
?
show the reaction diagram
2-acetyl-1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphocholine + acetate
show the reaction diagram
oxidized phospholipids + H2O
?
show the reaction diagram
-
protection against toxic effects of oxidized phospholipids
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
influences the dimerization of the enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
-
diisopropylfluorophosphate
iodoacetamide
-
NaF
-
not inhibitory
p-bromophenacyl bromide
-
intracellular enzyme form Ib from brain
p-bromophenacylbromide
-
phenylmethylsulfonyl fluoride
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0876
1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine
-
0.082 - 0.206
acetylated platelet-activation factor
-
additional information
additional information
-
kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0445
-
plasma enzyme
1.45
-
intracellular enzyme form Ib from brain
7.2
-
cytosolic isoform II from liver
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
intracellular enzyme forms from brain
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the greatest PAF-AH activity is detected on the day of parturition (day 0), after which its activity dramatically decreases and by day 5, the enzyme activity is less than 7% of the level at parturition
Manually annotated by BRENDA team
-
isozyme in endometrium is of the plasma enzyme type, enzyme activity decreases on day 20 in pregnant cows compared to cyclic cows on the same day, which show no changes in enzyme activity level
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
plasma isozyme
Manually annotated by BRENDA team
additional information
-
distribution of hetero- and homdimer of the alpha-subunit
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
brain enzyme
Manually annotated by BRENDA team
-
isozyme II
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PAFA_BOVIN
444
0
50133
Swiss-Prot
Secretory Pathway (Reliability: 1)
PA1B2_BOVIN
229
0
25569
Swiss-Prot
other Location (Reliability: 1)
PA1B3_BOVIN
232
0
25865
Swiss-Prot
other Location (Reliability: 1)
PAFA2_BOVIN
392
0
43865
Swiss-Prot
other Location (Reliability: 3)
Q1RML9_BOVIN
444
0
50151
TrEMBL
Secretory Pathway (Reliability: 1)
V6F7P3_BOVIN
229
0
25569
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
intracellular enzyme form Ib from brain, gel filtration
26000
-
isozyme Ib, 2 * 26000, subunits alpha1 and/or subunit alpha2, + 1 * 45000, beta-subunit
29000
-
1 * 45000 + 1 * 30000 + 1 * 29000, intracellular enzyme form Ib from brain, SDS-PAGE
30000
-
1 * 45000 + 1 * 30000 + 1 * 29000, intracellular enzyme form Ib from brain, SDS-PAGE
40000
43000
-
1 * 43000, SDS-PAGE
45000
60000
-
PAGE, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
isozyme II contains a myristoylation signal at the N-terminus
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
12 mg/ml purified recombinant alpha1/alpha2 heterodimer, hanging-drop vapour diffusion method, 21°C, 17% PEG-MME 2000, 0.1 M sodium acetate, pH 6.4, 10 mM CaCl2, X-ray diffraction structure determination and analysis at resolution 2.1 A
crystal structure determination and analysis of the alpha1 subunit in complex with acetate at 1.7 A resolution
-
purified recombinant R22K mutant, X-ray structure determination at 1.2 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D20N
-
site-directed mutagenesis, mutant is not efficiently expressed
D20R
-
site-directed mutagenesis, mutant is not efficiently expressed
H149R
-
brain isoform I, beta subunit, mutant has no ability to associate with the catalytic alpha-complexes
L194A
-
site-directed mutagenesis, decreased Km and Vmax compared to the wild-type enzyme
L26A
-
site-directed mutagenesis, 60% reduced activity compared to the wild-type enzyme
L48A
-
site-directed mutagenesis, decreased Km and Vmax compared to the wild-type enzyme
R22E
-
site-directed mutagenesis, mutant is not efficiently expressed
R22K
-
site-directed mutagenesis, inactive mutant
R29K
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
T103S
-
site-directed mutagenesis, decreased Km and Vmax compared to the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
stable for 24 h
47.5
-
unfolding and irreversible denaturation at pH 9.5
52.3
-
unfolding and irreversible denaturation at pH 6.5
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to several cycles of freezing and thawing
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytosolic isoform II from liver
-
from endometrium and plasma
-
from seminal plasma
-
His-tagged alpha1/alpha2 heterodimer or alpha1 homodimer as maltose-binding fusion proteins from Escherichia coli XL1-Blue, removal of tags
intracellular enzyme from brain, isoform Ib
-
isozyme II from liver, and isozyme I from brain
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
active enzyme expressed in HEK 293 cells
-
brain isoform I, expression of alpha1 and alpha2 subunits in Escherichia coli, expression of the beta subunit in Sf9 cells
-
expression of the alpha1/alpha2 heterodimer or alpha1 homodimer as His-tagged maltose-binding fusion protein in Escherichia coli XL1-Blue using a bi-citronic expression vector
expression of the catalytic subunit alpha1-homodimer and alpha1-alpha2-heterodimer in Escherichia coli as GST-fusion protein, expression of wild-type and mutant enzymes as GST-fusion proteins in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
the gene for the beta subunit of brain enzyme isoform I is identical to a causative gene for Miller-Dieker lissencephaly
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hattori, M.; Inoue, K.
Purification and characterization of bovine brain platelet-activating factor acetylhydrolase
J. Biol. Chem.
268
18748-18753
1993
Bos taurus
Manually annotated by BRENDA team
Hattori, K.; Hattori, M.; Adachi, H.; Tsujimoto, M.; Arai, H.; Inoue, K.
Purification and characterization of platelet-activating factor acetylhydrolase II from bovine liver cytosol
J. Biol. Chem.
270
22308-22313
1995
Bos taurus
Manually annotated by BRENDA team
Hough, S.R.; Parks, J.E.
Partial purification and localization of platelet-activating factor acetylhydrolase from bovine seminal plasma
J. Androl.
18
540-548
1997
Bos taurus
Manually annotated by BRENDA team
Maya, H.; Aoki, J.; Kato, H.; Ishii, J.; Hino, S.; Arai, H.; Inoue, K.
Biochemical characterization of various catalytic complexes of the brain platelet-activating factor acetylhydrolase
J. Biol. Chem.
274
31827-31832
1999
Bos taurus
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
Tiemann, U.; Tomek, W.; Schneider, F.; Wollenhaupt, K.; Kanitz, W.; Becker, F.; Pohland, R.; Alm, H.
Platelet-activating factor (PAF)-like activity, localization of PAF receptor (PAF-R) and PAF-acetylhydrolase (PAF-AH) activity in bovine endometrium at different stages of the estrous cycle and early pregnancy
Prostaglandins
65
125-141
2001
Bos taurus
Manually annotated by BRENDA team
McMullen, T.W.; Li, J.; Sheffield, P.J.; Aoki, J.; Martin, T.W.; Arai, H.; Inoue, K.; Derewenda, Z.S.
The functional implications of the dimerization of the catalytic subunits of the mammalian brain platelet-activating factor acetylhydrolase (Ib)
Protein Eng.
13
865-871
2000
Bos taurus
Manually annotated by BRENDA team
Sheffield, P.J.; McMullen, T.W.; Li, J.; Ho, Y.S.; Garrard, S.M.; Derewenda, U.; Derewenda, Z.S.
Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib
Protein Eng.
14
513-519
2001
Bos taurus (Q29460), Bos taurus
Manually annotated by BRENDA team
Lee, E.; Lee, S.J.; Lee, T.Y.; Chang, H.W.
cDNA cloning and expression of biologically active platelet activating factor-acetylhydrolase (PAF-AH) from bovine mammary gland
Biol. Pharm. Bull.
28
580-583
2005
Bos taurus
Manually annotated by BRENDA team
Moon, T.C.; Son, S.Y.; Chang, H.W.
Purification and characterization of 45 kDa PAF acetylhydrolase from bovine colostrum
Biol. Pharm. Bull.
30
1668-1673
2007
Bos taurus (Q29460 and P68401), Bos taurus
Manually annotated by BRENDA team
Turk, R.; Juretic, D.; Geres, D.; Bacic, G.; Milesevic, M.; Flegar-Mestric, Z.; Turk, N.; Svetina, A.
Bovine platelet-activating factor acetylhydrolase (PAF-AH) activity related to fertility
Anim. Reprod. Sci.
105
344-353
2008
Bos taurus
Manually annotated by BRENDA team