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(2R)-3-{[(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-({12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodecanoyl}oxy)propyl tetradecanoate + H2O
ethanolamine + (2R)-2-({12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodecanoyl}oxy)-3-(phosphonooxy)propyl tetradecanoate
-
-
-
-
?
(7R)-4-hydroxy-N,N,N-trimethyl-7-({12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodecanoyl}oxy)-10-oxo-3,5,9-trioxa-4-phosphatricosan-1-aminium 4-oxide + H2O
choline + (2R)-2-({12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodecanoyl}oxy)-3-(phosphonooxy)propyl tetradecanoate
-
-
-
-
?
1,2-dibutyl-sn-glycero-3-phosphocholine + H2O
choline + ?
-
-
?
1,2-dihexanoyl-sn-glycero-3-phosphocholine + H2O
1,2-dihexanoyl-sn-glycero-3-phosphatidate + choline
-
-
-
-
?
1,2-dioleoyl-sn-glycero-3-phosphocholine + glycerol
1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol + 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol + choline
1,2-dioleoyl-sn-glycerophosphocholine + 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)-1,3-propanediol
choline + 1,2-dioleoyl-sn-glycerophospho-2-[bis(2-hydroxyethyl)imino]-2-(hydroxymethyl)-1,3-propanediol
-
with BisTris as acceptor alcohol two regioisomeric forms of phosphatidyl-BisTris are obtained, product yield: 19.6% (regioisomer I), 3,1% (regioisomer II), purity of product: 98% (regioisomer I), 97% (regioisomer I)
-
-
?
1,2-dioleoyl-sn-glycerophosphocholine + diethanolamine
choline + 1,2-dioleoyl-sn-glycerophospho-diethanolamine
1,2-dioleoyl-sn-glycerophosphocholine + H2O
choline + 1,2-dioleoyl-sn-glycero-3-phosphatidic acid
-
-
-
-
?
1,2-dioleoyl-sn-glycerophosphocholine + serinol
choline + 1,2-dioleoyl-sn-glycerophospho-serinol
1,2-dioleoyl-sn-glycerophosphocholine + triethanolamine
choline + 1,2-dioleoyl-sn-glycerophospho-triethanolamine
1,2-dioleoyl-sn-glycerophosphocholine + tris(hydroxymethyl)-aminomethane
choline + 1,2-dioleoyl-sn-glycerophospho-tris(hydroxymethyl)-aminomethane
-
product yield: 31.6%, purity of product: 95%
-
-
?
1,2-dioleoylphosphatidylcholine + inositol
1,2-dioleoylphosphatidylinositol + choline
-
-
-
?
1-hexadecanoyl-2-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)aminohexanoyl]-sn-glycero-3-phosphocholine + H2O
?
-
fluorescent substrate
-
-
?
1-myristoyl-2-hydroxy-sn-glycero-3-phosphoethanolamine + H2O
[(4R)-2-hydroxy-2-oxido-1,3,2-dioxaphospholan-4-yl]methyl tetradecanoate + ethanolamine
-
-
-
?
1-O-(6-(p-methyl red)-amino-hexanoyl)-2-O-(12-(p-methyl red)-amino-dodecanoyl)-sn-glyceryl-N-(3-(5-BODIPY-pentanoyl)-amino-propyl)-N,Ndimethyl-phosphatidylethanolamine + H2O
?
1-O-alkyl-2-lyso-phosphatidylcholine + H2O
choline + 1-O-alkyl-2-lyso-phosphatidate
-
-
-
-
?
1-O-octadecyl-sn-glycero-3-phosphocholine + H2O
1-O-octadecyl-sn-glycero-3-phosphatidate + choline
-
-
-
-
?
1-oleoyl-2-stearoylphosphatidylethanolamine + H2O
ethanolamine + 1-oleoyl-2-stearoyl-sn-glycero-3-phosphatidic acid
-
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphate + choline
the enzyme hydrolyzes 98.4% of mixed micelle 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine in 1 h
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidate + choline
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidic acid + choline
2 1,2-dioleoyl-sn-glycerophosphocholine + diethanolamine
2 choline + bis(1,2-dioleoyl-sn-glycerophospho)-diethanolamine
-
-
-
-
?
2 1,2-dioleoyl-sn-glycerophosphocholine + serinol
2 choline + bis(1,2-dioleoyl-sn-glycerophospho)-serinol
-
-
-
-
?
2 1,2-dioleoyl-sn-glycerophosphocholine + triethanolamine
2 choline + bis(1,2-dioleoyl-sn-glycerophospho)-triethanolamine
-
-
-
-
?
2 1,2-dioleoyl-sn-glycerophosphocholine + tris(hydroxymethyl)-aminomethane
2 choline + bis(1,2-dioleoyl-sn-glycerophospho)-tris(hydroxymethyl)-aminomethane
-
-
-
-
?
2-(13'-hydroperoxy-octadecadienoyl)-1-palmitoylglycero-phosphocholine + N,N,N-triethyl-N-2-hydroxyethylammonium bromide
?
-
a synthetic phosphatidyl acceptor and substrate in transphosphatidylation reaction
-
-
?
2-(13'-hydroxy-octadecadienoyl)-1-palmitoylglycero-phosphocholine + N,N,N-triethyl-N-2-hydroxyethylammonium bromide
?
-
a synthetic phosphatidyl acceptor and substrate in transphosphatidylation reaction
-
-
?
2-(13'-oxo-octadecadienoyl)-1-palmitoylglycero-phosphocholine + N,N,N-triethyl-N-2-hydroxyethylammonium bromide
?
-
a synthetic phosphatidyl acceptor and substrate in transphosphatidylation reaction
-
-
?
2-decanoyl-1-(O-[(11-(4,4-difluoro-5,7-dimethyl)-4-bora-3a,4a-diaza-s-indacene-3-propionyl)amino]-undecyl)-phosphatidylcholine + H2O
2-decanoyl-1-(O-[(11-(4,4-difluoro-5,7-dimethyl)-4-bora-3a,4a-diaza-s-indacene-3-propionyl)amino]-undecyl)-phosphatidic acid + choline
-
BODIPY-fluorophor-phosphatidylcholine as substrate
-
-
?
bis(4-nitrophenyl)phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
bis(p-nitrophenyl)phosphate + H2O
?
-
-
-
?
cardiolipin + H2O
sn-glycero-1-phosphate + diacylglycerophosphate
choline plasmalogen + H2O
?
substrate of EC 3.1.4.3
-
-
?
dibutyroylphosphatidylcholine + H2O
dibutyroylglycerophosphate + choline
-
-
-
-
?
diheptanoylphosphatidylcholine + H2O
diheptanoylglycerophosphate + choline
-
-
-
-
?
dihexanoylphosphatidylcholine + H2O
dihexanoylglycerophosphate + choline
-
-
-
-
?
dioleoyl-phosphatidylcholine + cyclohexane-1,2,3-triol
choline + dioleoyl-phosphatidylcyclohexane-2,3-diol
in the cases of 1,2-diols, triols, and myo-inositol mutant W187F/Y191R generates the corresponding transphosphatidylated products more efficiently than wild-type
-
-
?
dioleoyl-phosphatidylcholine + cyclohexane-1,2,5-triol
choline + dioleoyl-phosphatidylcyclohexane-2,5-diol
in the cases of 1,2-diols, triols, and myo-inositol mutant W187F/Y191R generates the corresponding transphosphatidylated products more efficiently than wild-type
-
-
?
dioleoyl-phosphatidylcholine + cyclohexane-1,2-diol
choline + dioleoyl-phosphatidylcyclohexane-2-ol
in the cases of 1,2-diols, triols, and myo-inositol mutant W187F/Y191R generates the corresponding transphosphatidylated products more efficiently than wild-type
-
-
?
dioleoyl-phosphatidylcholine + cyclohexane-1,3-diol
choline + dioleoyl-phosphatidylcyclohexane-3-ol
in the cases of 1,2-diols, triols, and myo-inositol mutant W187F/Y191R generates the corresponding transphosphatidylated products more efficiently than wild-type
-
-
?
dioleoyl-phosphatidylcholine + cyclohexane-1,4-diol
choline + dioleoyl-phosphatidylcyclohexane-4-ol
-
-
-
?
dioleoyl-phosphatidylcholine + cyclohexanol
choline + dioleoyl-phosphatidylcyclohexane
in the cases of cyclohexanol and of cyclohexane-1,4-diol, the wild-type enzyme generates the corresponding transphosphatidylated products more efficiently than the mutant W187F/Y191R
-
-
?
dioleoyl-phosphatidylcholine + H2O
choline + dioleoyl-phosphatidate
-
-
-
?
dioleoyl-phosphatidylcholine + myo-inositol
?
in the cases of 1,2-diols, triols, and myo-inositol mutant W187F/Y191R generates the corresponding transphosphatidylated products more efficiently than wild-type
-
-
?
dioleoyl-phosphatidylcholine + myo-inositol
phosphatidylinositol + choline
dioleoylphosphatidylcholine + H2O
choline + 1,2-dioleoyl-sn-glycero-3-phosphatidic acid
-
-
-
-
?
dioleoylphosphatidylcholine + myo-inositol
choline + dioleoylphosphatidylinositol
transphosphatidylation activity of mutant W187D/Y191Y/Y385R enzyme
-
-
?
dioleoylphosphatidylethanolamine + H2O
ethanolamine + 1,2-dioleoyl-sn-glycero-3-phosphatidic acid
-
-
-
-
?
dipalmitoyl phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerophosphate + choline
dipalmitoylphosphatidylcholine + H2O
choline + dipalmitoylphosphatidate
dipalmitoylphosphatidylcholine + H2O
dipalmitoylglycerophosphate + choline
DNA + H2O
smaller DNA fragments
docosahexanoylphosphatidylcholine + D-serine
docosahexanoylphosphatidylserine + choline
doxorubicin + phosphatidate
phosphatidyl-doxorubicin + H2O
-
-
-
?
glycerophospho-(N-palmitoyl)ethanolamine + H2O
N-palmitoylethanolamine + ?
-
-
1% of the activity with N-palmitoyl-phosphatidylethanolamine
-
?
glycosylinositol phosphoceramide + H2O
phytoceramide-1-phosphate + glycosylinositol
L-alpha-lysophosphatidylcholine + H2O
?
substrate of EC 3.1.4.3
-
-
?
lysophosphatidylcholine + glycerol
?
-
-
-
?
lysophosphatidylcholine + H2O
choline + lysophosphatidate
-
about 20 times slower than reaction of phosphatidylcholine
-
?
lysophosphatidylcholine + H2O
choline + lysophosphatidic acid
-
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerophosphate + choline
N-acyl-phosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
N-acylphosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
-
-
-
-
?
N-arachidonoyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-arachidonoylethanolamine
-
-
-
?
n-butanol + phosphatidylcholine
phosphatidylbutanol + choline
-
-
-
-
?
N-lauroyl-D-erythrosphingosylphosphoethanolamine + H2O
N-[(4R,5S)-2-hydroxy-2-oxido-4-[(1E)-pentadec-1-en-1-yl]-1,3,2-dioxaphosphinan-5-yl]dodecanamide + ethanolamine
-
-
-
?
N-lauroyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-lauroylethanolamine
N-palmitoyl-lyso-phosphatidylethanolamine + H2O
N-palmitoylethanolamine + sn-glycerol 3-phosphate
-
-
4% of the activity with N-palmitoyl-phosphatidylethanolamine
-
?
N-palmitoyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-palmitoylethanolamine
octadecylphosphocholine + L-serine
octadecylphospho-L-serine + choline
oleoyllysophosphatidylethanolamine + H2O
ethanolamine + 1,2-dioleoyl-sn-glycero-3-phosphatidic acid
-
-
-
-
?
p-nitrophenylphosphorylcholine + H2O
?
-
-
-
?
phosphatidyl-doxorubicin + H2O
doxorubicin + phosphatidate
-
-
-
-
?
phosphatidyl-p-nitrophenol + H2O
phosphatidate + p-nitrophenol
phosphatidyl-p-nitrophenol + H2O
phosphatidic acid + p-nitrophenol
phosphatidylcholine + butanol
phosphatidylbutanol + choline
phosphatidylcholine + D-arabinose
phosphatidylarabinose + choline
-
-
-
-
?
phosphatidylcholine + D-fructose
phosphatidylfructose + choline
-
-
-
-
?
phosphatidylcholine + D-galactose
phosphatidylgalactose + choline
-
-
-
-
?
phosphatidylcholine + D-glucose
phosphatidylglucose + choline
-
-
-
-
?
phosphatidylcholine + D-mannose
phosphatidylmannose + choline
-
-
-
-
?
phosphatidylcholine + D-serine
phosphatidylserine + choline
phosphatidylcholine + D-xylose
phosphatidylxylose + choline
-
-
-
-
?
phosphatidylcholine + diethyleneglycol
phosphatidyldiethyleneglycol + choline
-
-
-
-
?
phosphatidylcholine + diethyleneglycol monomethyl ester
diethyleneglycol dimethyl phosphatidic acid + choline
-
-
-
-
?
phosphatidylcholine + ethanol
choline + phosphatidyl ethanol
-
PLD also performs transphosphatidylation using ethanol as phosphatidyl acceptor
-
-
?
phosphatidylcholine + ethanol
choline + phosphatidylethanol
phosphatidylcholine + ethanol
phosphatidylethanol + choline
phosphatidylcholine + ethanolamine
phosphatidylethanolamine + choline
phosphatidylcholine + ethyleneglycol
phosphatidylethyleneglycol + choline
-
-
-
-
?
phosphatidylcholine + ethyleneglycol monomethyl ester
ethyleneglycol monomethyl phosphatidic acid + choline
-
-
-
-
?
phosphatidylcholine + glycerol
?
-
-
-
?
phosphatidylcholine + glycerol
phosphatidylglycerol + choline
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
phosphatidylcholine + H2O
choline + ?
phosphatidylcholine + H2O
choline + a phosphatidate
phosphatidylcholine + H2O
choline + phosphatidate
phosphatidylcholine + H2O
choline + phosphatidic acid
phosphatidylcholine + H2O
phosphatidate + choline
phosphatidylcholine + H2O
phosphatidic acid + choline
phosphatidylcholine + heptanol
phosphatidylheptanol + choline
-
-
-
-
?
phosphatidylcholine + hexanol
phosphatidylhexanol + choline
-
-
-
-
?
phosphatidylcholine + inositol
phosphatidylinositol + choline
phosphatidylcholine + L-serine
phosphatidyl-L-serine + choline
-
-
-
?
phosphatidylcholine + L-serine
phosphatidylserine + choline
phosphatidylcholine + L-sorbose
phosphatidylsorbose + choline
-
-
-
-
?
phosphatidylcholine + methanol
phosphatidylmethanol + choline
phosphatidylcholine + myo-inositol
phosphatidylinositol + choline
the wild-type enzyme is capable of synthesizing phosphatidylinositol by transphosphatidylation. Increase in phosphatidylinositol yield is possible by providing excess of solvated myo-inositol, which is achievable at high temperatures due to its highly temperature-dependent solubility, especially by enzyme variants with increased thermostability, e.g. mutant W187D/Y191Y/Y385R
-
-
?
phosphatidylcholine + N,N,N-triethyl-N-2-hydroxyethylammonium bromide
choline + ?
-
a synthetic phosphatidyl acceptor in transphosphatidylation reaction
-
-
?
phosphatidylcholine + pentanol
phosphatidylpentanol + choline
-
-
-
-
?
phosphatidylcholine + propanol
phosphatidylpropanol + choline
-
-
-
-
?
phosphatidylcholine + triethyleneglycol
phosphatidyltriethyleneglycol + choline
-
-
-
-
?
phosphatidylcholine + triethyleneglycol monomethyl ester
triethyleneglycol trimethyl phosphatidic acid + choline
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
phosphatidylethanolamine + H2O
ethanolamine + phosphatidate
phosphatidylethanolamine + H2O
ethanolamine + phosphatidic acid
phosphatidylethanolamine + H2O
phosphatidate + ethanolamine
phosphatidylglycerol + H2O
?
-
-
-
?
phosphatidylglycerol + H2O
glycerol + 1,2-diacylglycerophosphate
phosphatidylglycerol + H2O
glycerol + diacylglycerophosphate
phosphatidylglycerol + H2O
glycerol + phosphatidate
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
phosphatidylglycerol + H2O
phosphatidate + glycerol
phosphatidylinositol + H2O
1,2-diacylglycerophosphate + inositol
phosphatidylinositol + H2O
phosphatidate + inositol
phosphatidylserine + H2O
1,2-diacylglycerophosphate + serine
phosphatidylserine + H2O
L-serine + phosphatidate
phosphatidylserine + H2O
phosphatidate + serine
phosphatidylserine + H2O
serine + phosphatidic acid
phospholipid + alcohol
phospholipid + alcohol
phospholipid + H2O
phosphatidic acid + alcohol
sphingomyelin + H2O
N-acylsphingosylphosphate + choline
additional information
?
-
1,2-dioleoyl-sn-glycero-3-phosphocholine + glycerol
1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol + 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol + choline
-
stereoselectivity of the enzyme towards the two primary hydroxyl groups of prochiral glycerol is significantly influenced by reaction temperature
the proportion of 1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol (R,R-configuration) to 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol (R,S configuration) is 50:50 at 50-60°C and 70:30 at 0°C
-
?
1,2-dioleoyl-sn-glycero-3-phosphocholine + glycerol
1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol + 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol + choline
-
no effect of temperature on stereoselectivity
almost equimolar mixture of 1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol (R,R-configuration) and 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol in the range from 0°C to 40°C
-
?
1,2-dioleoyl-sn-glycero-3-phosphocholine + glycerol
1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol + 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol + choline
-
little effect of temperature on stereoselectivity
the proportion of 1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol (R,R-configuration) to 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol (R,S configuration) is 65-69:31-35 in the temperature range 60°C to 10°C
-
?
1,2-dioleoyl-sn-glycero-3-phosphocholine + glycerol
1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol + 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol + choline
-
little effect of temperature on stereoselectivity
the proportion of 1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol (R,R-configuration) to 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol (R,S configuration) is 65-69:31-35 in the temperature range 60°C to 10°C
-
?
1,2-dioleoyl-sn-glycero-3-phosphocholine + glycerol
1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol + 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol + choline
-
stereoselectivity of the enzyme towards the two primary hydroxyl groups of prochiral glycerol is significantly influenced by reaction temperature
the proportion of 1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol (R,R-configuration) to 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol (R,S configuration) is 50:50 at 50-60°C and 70:30 at 0°C
-
?
1,2-dioleoyl-sn-glycero-3-phosphocholine + glycerol
1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol + 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol + choline
-
stereoselectivity of the enzyme towards the two primary hydroxyl groups of prochiral glycerol is significantly influenced by reaction temperature
the proportion of 1,2-dioleoyl-sn-glycero-3-phospho-3'-sn-glycerol (R,R-configuration) to 1,2-dioleoyl-sn-glycero-3-phospho-1'-sn-glycerol (R,S configuration) is 50:50 at 50-60°C and 70:30 at 0°C
-
?
1,2-dioleoyl-sn-glycerophosphocholine + diethanolamine
choline + 1,2-dioleoyl-sn-glycerophospho-diethanolamine
-
product yield: 44.1%, purity of product: 97.0%
-
-
?
1,2-dioleoyl-sn-glycerophosphocholine + diethanolamine
choline + 1,2-dioleoyl-sn-glycerophospho-diethanolamine
-
product yield: 47.2%, purity of product: 81.5%
-
-
?
1,2-dioleoyl-sn-glycerophosphocholine + serinol
choline + 1,2-dioleoyl-sn-glycerophospho-serinol
-
product yield: 39.5%, purity of product: 99.8%
-
-
?
1,2-dioleoyl-sn-glycerophosphocholine + serinol
choline + 1,2-dioleoyl-sn-glycerophospho-serinol
-
product yield: 45.8%, purity of product: 68%
-
-
?
1,2-dioleoyl-sn-glycerophosphocholine + triethanolamine
choline + 1,2-dioleoyl-sn-glycerophospho-triethanolamine
-
product yield: 22.6%, purity of product: 99.5%
-
-
?
1,2-dioleoyl-sn-glycerophosphocholine + triethanolamine
choline + 1,2-dioleoyl-sn-glycerophospho-triethanolamine
-
product yield: 33.7%, purity of product: 65.4%
-
-
?
1-O-(6-(p-methyl red)-amino-hexanoyl)-2-O-(12-(p-methyl red)-amino-dodecanoyl)-sn-glyceryl-N-(3-(5-BODIPY-pentanoyl)-amino-propyl)-N,Ndimethyl-phosphatidylethanolamine + H2O
?
-
fluorogenic analogue of phosphatidylcholine, direct substrate for real-time measurement of enzyme activity
-
-
?
1-O-(6-(p-methyl red)-amino-hexanoyl)-2-O-(12-(p-methyl red)-amino-dodecanoyl)-sn-glyceryl-N-(3-(5-BODIPY-pentanoyl)-amino-propyl)-N,Ndimethyl-phosphatidylethanolamine + H2O
?
-
fluorogenic analogue of phosphatidylcholine, direct substrate for real-time measurement of enzyme activity
-
-
?
1-O-(6-(p-methyl red)-amino-hexanoyl)-2-O-(12-(p-methyl red)-amino-dodecanoyl)-sn-glyceryl-N-(3-(5-BODIPY-pentanoyl)-amino-propyl)-N,Ndimethyl-phosphatidylethanolamine + H2O
?
-
fluorogenic analogue of phosphatidylcholine, direct substrate for real-time measurement of enzyme activity
-
-
?
1-O-(6-(p-methyl red)-amino-hexanoyl)-2-O-(12-(p-methyl red)-amino-dodecanoyl)-sn-glyceryl-N-(3-(5-BODIPY-pentanoyl)-amino-propyl)-N,Ndimethyl-phosphatidylethanolamine + H2O
?
-
fluorogenic analogue of phosphatidylcholine, direct substrate for real-time measurement of enzyme activity
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidic acid + choline
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidic acid + choline
-
-
phosphatidic acid is negatively charged
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidic acid + choline
-
-
phosphatidic acid is negatively charged
?
cardiolipin + H2O
sn-glycero-1-phosphate + diacylglycerophosphate
-
-
-
-
?
cardiolipin + H2O
sn-glycero-1-phosphate + diacylglycerophosphate
-
-
-
-
?
dioleoyl-phosphatidylcholine + myo-inositol
phosphatidylinositol + choline
-
-
the 187H/191Y/385R mutant generates 1-phosphatidylinositol more than 3-phosphatidylinositol, whereas 187T/191Y/385R generates 1-phosphatidylinositol less than 3-phosphatidylinositol
-
?
dioleoyl-phosphatidylcholine + myo-inositol
phosphatidylinositol + choline
-
the FRY mutant generates 1(3)-phosphatidylinositol and 4(6)-phosphatidylinositol, but not 2-phosphatidylinositol and 5-phosphatidylinositol
-
?
dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerophosphate + choline
-
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerophosphate + choline
-
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
choline + dipalmitoylphosphatidate
-
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
choline + dipalmitoylphosphatidate
-
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
dipalmitoylglycerophosphate + choline
-
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
dipalmitoylglycerophosphate + choline
-
-
-
-
?
DNA + H2O
smaller DNA fragments
-
double and single stranded DNA
-
-
?
DNA + H2O
smaller DNA fragments
-
endonuclease
-
-
?
docosahexanoylphosphatidylcholine + D-serine
docosahexanoylphosphatidylserine + choline
-
-
-
-
?
docosahexanoylphosphatidylcholine + D-serine
docosahexanoylphosphatidylserine + choline
-
-
-
-
?
glycosylinositol phosphoceramide + H2O
phytoceramide-1-phosphate + glycosylinositol
-
-
phytoceramide-1-phosphate with an alpha-hydroxy fatty acid
-
?
glycosylinositol phosphoceramide + H2O
phytoceramide-1-phosphate + glycosylinositol
-
-
phytoceramide-1-phosphate with an alpha-hydroxy fatty acid
-
?
glycosylinositol phosphoceramide + H2O
phytoceramide-1-phosphate + glycosylinositol
-
-
phytoceramide-1-phosphate with an alpha-hydroxy fatty acid
-
?
lysophosphatidylcholine + H2O
monoacylglycerophosphate + choline
-
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerophosphate + choline
-
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerophosphate + choline
-
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerophosphate + choline
-
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerophosphate + choline
-
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerophosphate + choline
-
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerophosphate + choline
-
-
-
-
?
N-acyl-phosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
-
high specificity for N-acyl-phosphatidylethanolamines without selectivity for long chain or medium chain N-acyl species
-
-
?
N-acyl-phosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
-
high specificity for N-acyl-phosphatidylethanolamines without selectivity for long chain or medium chain N-acyl species
-
-
?
N-lauroyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-lauroylethanolamine
-
-
-
-
?
N-lauroyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-lauroylethanolamine
-
-
-
-
?
N-palmitoyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-palmitoylethanolamine
-
-
-
-
?
N-palmitoyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-palmitoylethanolamine
-
-
-
-
?
N-palmitoyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-palmitoylethanolamine
-
-
-
?
N-palmitoyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-palmitoylethanolamine
-
-
-
-
?
octadecylphosphocholine + L-serine
octadecylphospho-L-serine + choline
-
-
-
?
octadecylphosphocholine + L-serine
octadecylphospho-L-serine + choline
-
-
-
?
phosphatidyl-p-nitrophenol + H2O
phosphatidate + p-nitrophenol
-
the N-terminal HKD motif contains the catalytic nucleophile, which attacks the phosphatidyl group of the substrate
-
-
?
phosphatidyl-p-nitrophenol + H2O
phosphatidate + p-nitrophenol
-
the N-terminal HKD motif contains the catalytic nucleophile, which attacks the phosphatidyl group of the substrate
-
-
?
phosphatidyl-p-nitrophenol + H2O
phosphatidic acid + p-nitrophenol
-
-
-
?
phosphatidyl-p-nitrophenol + H2O
phosphatidic acid + p-nitrophenol
-
-
-
?
phosphatidyl-p-nitrophenol + H2O
phosphatidic acid + p-nitrophenol
-
-
-
-
?
phosphatidyl-p-nitrophenol + H2O
phosphatidic acid + p-nitrophenol
-
-
-
-
?
phosphatidylcholine + butanol
phosphatidylbutanol + choline
-
-
-
-
?
phosphatidylcholine + butanol
phosphatidylbutanol + choline
-
-
-
-
?
phosphatidylcholine + D-serine
phosphatidylserine + choline
-
-
-
-
?
phosphatidylcholine + D-serine
phosphatidylserine + choline
-
-
-
-
?
phosphatidylcholine + D-serine
phosphatidylserine + choline
for L- and D-serine a stereoselectivity of PLD is observed
-
-
?
phosphatidylcholine + D-serine
phosphatidylserine + choline
for L- and D-serine a stereoselectivity of PLD is observed
-
-
?
phosphatidylcholine + ethanol
choline + phosphatidylethanol
-
-
-
?
phosphatidylcholine + ethanol
choline + phosphatidylethanol
-
-
-
?
phosphatidylcholine + ethanol
phosphatidylethanol + choline
-
enzyme shows also transphosphatidylation activity
-
-
?
phosphatidylcholine + ethanol
phosphatidylethanol + choline
-
-
-
-
?
phosphatidylcholine + ethanol
phosphatidylethanol + choline
-
-
-
-
?
phosphatidylcholine + ethanol
phosphatidylethanol + choline
-
-
-
-
?
phosphatidylcholine + ethanol
phosphatidylethanol + choline
-
-
-
-
?
phosphatidylcholine + ethanol
phosphatidylethanol + choline
-
-
-
-
?
phosphatidylcholine + ethanolamine
phosphatidylethanolamine + choline
-
-
-
-
?
phosphatidylcholine + ethanolamine
phosphatidylethanolamine + choline
-
-
-
-
?
phosphatidylcholine + ethanolamine
phosphatidylethanolamine + choline
-
transferase activity in presence of 4% ethanolamine
-
-
?
phosphatidylcholine + ethanolamine
phosphatidylethanolamine + choline
preference of acceptor alcohols in transphosphatidylation of phosphatidylcholine: ethanolamine higher than glycerol higher than L-Ser
-
-
?
phosphatidylcholine + ethanolamine
phosphatidylethanolamine + choline
preference of acceptor alcohols in transphosphatidylation of phosphatidylcholine: ethanolamine higher than glycerol higher than L-serine
-
-
?
phosphatidylcholine + ethanolamine
phosphatidylethanolamine + choline
-
-
-
-
?
phosphatidylcholine + ethanolamine
phosphatidylethanolamine + choline
-
-
-
-
?
phosphatidylcholine + ethanolamine
phosphatidylethanolamine + choline
preference of acceptor alcohols in transphosphatidylation of phosphatidylcholine: ethanolamine higher than glycerol
-
-
?
phosphatidylcholine + ethanolamine
phosphatidylethanolamine + choline
preference of acceptor alcohols in transphosphatidylation of phosphatidylcholine: ethanolamine higher than glycerol higher than L-serine
-
-
?
phosphatidylcholine + ethanolamine
phosphatidylethanolamine + choline
-
-
-
-
?
phosphatidylcholine + glycerol
phosphatidylglycerol + choline
preference of acceptor alcohols in transphosphatidylation of phosphatidylcholine: ethanolamine higher than glycerol higher than L-Ser
-
-
?
phosphatidylcholine + glycerol
phosphatidylglycerol + choline
preference of acceptor alcohols in transphosphatidylation of phosphatidylcholine: ethanolamine higher than glycerol higher than L-serine
-
-
?
phosphatidylcholine + glycerol
phosphatidylglycerol + choline
preference of acceptor alcohols in transphosphatidylation of phosphatidylcholine: ethanolamine higher than glycerol
-
-
?
phosphatidylcholine + glycerol
phosphatidylglycerol + choline
preference of acceptor alcohols in transphosphatidylation of phosphatidylcholine: ethanolamine higher than glycerol higher than L-serine
-
-
?
phosphatidylcholine + glycerol
phosphatidylglycerol + choline
-
-
-
-
?
phosphatidylcholine + glycerol
phosphatidylglycerol + choline
-
-
-
-
?
phosphatidylcholine + glycerol
phosphatidylglycerol + choline
-
-
-
-
?
phosphatidylcholine + glycerol
phosphatidylglycerol + choline
-
catalyzes the transphosphatidylation of glycerol, but not that of L-serine, myo-inositol or ethanolamine
-
-
?
phosphatidylcholine + glycerol
phosphatidylglycerol + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
presence of phosphatidylinositol 4,5-bisphosphate and phosphatidylethanol is required
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
ratio in rates of hydrolysis phosphatidylcholine:phosphatidylglycerol:phosphatidylserine:phosphatidylinositol is 1:0.5:0.3:0.1, isoenzyme PLD-A
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
ratio in rates of hydrolysis phosphatidylcholine:phosphatidylglycerol:phosphatidylserine:phosphatidylinositol is 1:0.5:0.3:0.1, isoenzyme PLD-B
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
both phosphatidylcholine and phosphatidylethanolamine are substrates for phospholipase D in UMR-106 osteoblastic cells and can therefore be sources of phospholipid hydrolysis products for downstream signaling in osteoblast
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
high activity to the non-micelle form of phosphatidylcholine in an aequeous solution containing methanol, ethanol, isopropanol, or n-propanol. In absence of alcohol, hydrolytic activity is weak, and no transphosphatidylation activity is detected
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
hydrolytic and transphosphatylation activity
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
?
phosphatidylcholine + H2O
choline + ?
-
-
-
?
phosphatidylcholine + H2O
choline + ?
-
-
-
?
phosphatidylcholine + H2O
choline + a phosphatidate
-
substrate soybean lecithin
-
-
?
phosphatidylcholine + H2O
choline + a phosphatidate
phosphatidylcholine hydrolysis
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
from egg yolk
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
Regulation and effectors of phospholipase D and phosphatidic acid on the Golgi apparatus, overview
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
egg yolk lecithin
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
egg yolk lecithin
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
catalyzes both hydrolysis of phosphoric ester and transphosphatidylation
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
phosphatidic acid binds to ABI1, a PP2C, which functions as a negative regulator in abscisic acid signalling in stomata closure. Phosphatidic acid stimulated NADPH oxidase activity and reactive oxygen species production in wild-type and PLDalpha1-deficient cells, cellular and physiological effects of phosphatidic acid, overview
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
707069, 707481, 707549, 707551, 707572, 708012, 708430, 709222, 709597, 709606, 709924, 710407 -
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
phosphatidic acid has unique bioactive properties and can modify both the physical and signalling properties of lipid bilayers. Perturbation of phosphatidic metabolism can alter membrane dynamics with consequences on cell viability, phosphatidic acid functions, overview
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
phosphatidic acid induces upregulation of MMP-2 mediated by protein kinase C, protein kinase A, nuclear factor-kappaB, and Sp1. Phosphatidic acid induces nuclear localization and the transactivation of NF-kappaB in glioma cells.
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
phosphatidic acid plays a regulatory role in important cellular processes such as secretion, cellular shape change, and movement
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
hydrolysis of phosphatidylcholine by phospholipase D leads to the generation of phosphatidic acid, which is itself a source of diacylglycerol. PLD2 emerges as an early player upstream of the Ras-MAPK-IL-2 pathway in T-cells via phosphatidic acid and diacylglycerol production
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
the basal activity of PLD1 is lower than that of isozyme PLD2
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
hydrolysis of phosphatidylcholine by phospholipase D leads to the generation of phosphatidic acid, PA, which is itself a source of diacylglycerol. PLD2 emerges as an early player upstream of the Ras-MAPK-IL-2 pathway in T-cells via PA and DAG production
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
phosphatidic acid activates the production of and promotes accumulation of silymarin, overview
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
phosphatidic acid acts as a second messenger in phosphorylation cascades
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
essential role for catalysis of histidines 167 and 440 and lysines 169 and 442 of the two highly conserved HKD domains. H167 acts as the nucleophile by attacking the phosphorus atom of the phospholipidic substrates, while the conserved histidine of the C-terminal HKD domain, H440, plays a complementary role in the catalytic mechanism
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
phosphatidate + choline
-
-
-
-
?
phosphatidylcholine + H2O
phosphatidate + choline
-
-
-
?
phosphatidylcholine + H2O
phosphatidate + choline
enzyme shows the highest activity toward phosphatidylcholine and the lowest toward phosphatidylserine
-
-
?
phosphatidylcholine + H2O
phosphatidate + choline
the order of substrates in the rates of hydrolysis is: phosphatidylcholine higher than phosphatidylglycerol equal to phosphatidylethanolamine higher than phosphatidylinositol higher than phosphatidylserine
-
-
?
phosphatidylcholine + H2O
phosphatidate + choline
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylglycerol equal to phosphatidylcholine higher than phosphatidylinositol higher than phosphatidylserine
-
-
?
phosphatidylcholine + H2O
phosphatidate + choline
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylcholine higher than phosphatidylglycerol higher than phosphatidylinositol
-
-
?
phosphatidylcholine + H2O
phosphatidate + choline
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylglycerol higher than phosphatidylcholine higher than phosphatidylserine higher than phosphatidylinositol
-
-
?
phosphatidylcholine + H2O
phosphatidate + choline
-
-
-
?
phosphatidylcholine + H2O
phosphatidic acid + choline
-
a phospholipid transphosphatidylation reaction
-
-
?
phosphatidylcholine + H2O
phosphatidic acid + choline
-
a phospholipid transphosphatidylation reaction
-
-
?
phosphatidylcholine + inositol
phosphatidylinositol + choline
-
-
-
-
?
phosphatidylcholine + inositol
phosphatidylinositol + choline
-
-
-
-
?
phosphatidylcholine + L-serine
phosphatidylserine + choline
for L- and D-serine a stereoselectivity of PLD is observed, preference of acceptor alcohols in transphosphatidylation of phosphatidylcholine: ethanolamine higher than glycerol higher than L-serine
-
-
?
phosphatidylcholine + L-serine
phosphatidylserine + choline
preference of acceptor alcohols in transphosphatidylation of phosphatidylcholine: ethanolamine higher than glycerol higher than L-Ser
-
-
?
phosphatidylcholine + L-serine
phosphatidylserine + choline
for L- and D-serine a stereoselectivity of PLD is observed, preference of acceptor alcohols in transphosphatidylation of phosphatidylcholine: ethanolamine higher than glycerol higher than L-serine
-
-
?
phosphatidylcholine + L-serine
phosphatidylserine + choline
-
-
-
-
?
phosphatidylcholine + L-serine
phosphatidylserine + choline
phosphatidylcholine transphosphatidylation
-
-
?
phosphatidylcholine + L-serine
phosphatidylserine + choline
-
-
-
-
?
phosphatidylcholine + L-serine
phosphatidylserine + choline
-
-
-
-
?
phosphatidylcholine + methanol
phosphatidylmethanol + choline
-
-
-
-
?
phosphatidylcholine + methanol
phosphatidylmethanol + choline
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
parathyroid hormone stimulates phosphatidylethanolamine hydrolysis by phospholipase D in osteoblastic cells. Both phosphatidylcholine and phosphatidylethanolamine are substrates for phospholipase D in UMR-106 osteoblastic cells and can therefore be sources of phospholipid hydrolysis products for downstream signaling in osteoblast
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
-
-
-
r
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
-
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidate
-
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidate
-
-
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidate
-
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidate
-
-
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidic acid
-
-
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidic acid
-
-
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidic acid
-
-
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidic acid
-
-
-
-
?
phosphatidylethanolamine + H2O
phosphatidate + ethanolamine
the order of substrates in the rates of hydrolysis is: phosphatidylcholine higher than phosphatidylglycerol equal to phosphatidylethanolamine higher than phosphatidylinositol higher than phosphatidylserine
-
-
?
phosphatidylethanolamine + H2O
phosphatidate + ethanolamine
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylcholine higher than phosphatidylglycerol higher than phosphatidylinositol higher than phosphatidylserine
-
-
?
phosphatidylethanolamine + H2O
phosphatidate + ethanolamine
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylcholine higher than phosphatidylglycerol higher than phosphatidylinositol
-
-
?
phosphatidylethanolamine + H2O
phosphatidate + ethanolamine
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylglycerol higher than phosphatidylcholine higher than phosphatidylserine higher than phosphatidylinositol
-
-
?
phosphatidylglycerol + H2O
glycerol + 1,2-diacylglycerophosphate
-
ratio in rates of hydrolysis phosphatidylcholine:phosphatidylglycerol:phosphatidylserine:phosphatidylinositol is 1:0.5:0.3:0.1, isoenzyme PLD-A
-
-
?
phosphatidylglycerol + H2O
glycerol + 1,2-diacylglycerophosphate
-
ratio in rates of hydrolysis phosphatidylcholine:phosphatidylglycerol:phosphatidylserine:phosphatidylinositol is 1:0.5:0.3:0.1, isoenzyme PLD-B
-
-
?
phosphatidylglycerol + H2O
glycerol + diacylglycerophosphate
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + diacylglycerophosphate
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidate
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidate
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidate
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
?
phosphatidylglycerol + H2O
phosphatidate + glycerol
enzyme shows the highest activity toward phosphatidylcholine and the lowest toward phosphatidylserine
-
-
?
phosphatidylglycerol + H2O
phosphatidate + glycerol
the order of substrates in the rates of hydrolysis is: phosphatidylcholine higher than phosphatidylglycerol equal to phosphatidylethanolamine higher than phosphatidylinositol higher than phosphatidylserine
-
-
?
phosphatidylglycerol + H2O
phosphatidate + glycerol
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylglycerol equal to phosphatidylcholine higher than phosphatidylinositol higher than phosphatidylserine
-
-
?
phosphatidylglycerol + H2O
phosphatidate + glycerol
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylcholine higher than phosphatidylglycerol higher than phosphatidylinositol
-
-
?
phosphatidylglycerol + H2O
phosphatidate + glycerol
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylglycerol higher than phosphatidylcholine higher than phosphatidylserine higher than phosphatidylinositol
-
-
?
phosphatidylinositol + H2O
1,2-diacylglycerophosphate + inositol
-
-
-
-
?
phosphatidylinositol + H2O
1,2-diacylglycerophosphate + inositol
-
-
-
-
?
phosphatidylinositol + H2O
1,2-diacylglycerophosphate + inositol
-
ratio in rates of hydrolysis phosphatidylcholine:phosphatidylglycerol:phosphatidylserine:phosphatidylinositol is 1:0.5:0.3:0.1, isoenzyme PLD-A
-
-
?
phosphatidylinositol + H2O
1,2-diacylglycerophosphate + inositol
-
ratio in rates of hydrolysis phosphatidylcholine:phosphatidylglycerol:phosphatidylserine:phosphatidylinositol is 1:0.5:0.3:0.1, isoenzyme PLD-B
-
-
?
phosphatidylinositol + H2O
1,2-diacylglycerophosphate + inositol
-
-
-
-
?
phosphatidylinositol + H2O
phosphatidate + inositol
the order of substrates in the rates of hydrolysis is: phosphatidylcholine higher than phosphatidylglycerol equal to phosphatidylethanolamine higher than phosphatidylinositol higher than phosphatidylserine
-
-
?
phosphatidylinositol + H2O
phosphatidate + inositol
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylcholine higher than phosphatidylglycerol higher than phosphatidylinositol higher than phosphatidylserine
-
-
?
phosphatidylinositol + H2O
phosphatidate + inositol
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylcholine higher than phosphatidylglycerol higher than phosphatidylinositol
-
-
?
phosphatidylinositol + H2O
phosphatidate + inositol
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylglycerol higher than phosphatidylcholine higher than phosphatidylserine higher than phosphatidylinositol
-
-
?
phosphatidylserine + H2O
1,2-diacylglycerophosphate + serine
-
-
-
-
?
phosphatidylserine + H2O
1,2-diacylglycerophosphate + serine
-
-
-
-
?
phosphatidylserine + H2O
1,2-diacylglycerophosphate + serine
-
-
-
-
?
phosphatidylserine + H2O
1,2-diacylglycerophosphate + serine
-
-
-
-
?
phosphatidylserine + H2O
L-serine + phosphatidate
-
ratio in rates of hydrolysis phosphatidylcholine:phosphatidylglycerol:phosphatidylserine:phosphatidylinositol is 1:0.5:0.3:0.1, isoenzyme PLD-A
-
-
?
phosphatidylserine + H2O
L-serine + phosphatidate
-
ratio in rates of hydrolysis phosphatidylcholine:phosphatidylglycerol:phosphatidylserine:phosphatidylinositol is 1:0.5:0.3:0.1, isoenzyme PLD-B
-
-
?
phosphatidylserine + H2O
L-serine + phosphatidate
-
-
-
?
phosphatidylserine + H2O
phosphatidate + serine
enzyme shows the highest activity toward phosphatidylcholine and the lowest toward phosphatidylserine
-
-
?
phosphatidylserine + H2O
phosphatidate + serine
the order of substrates in the rates of hydrolysis is: phosphatidylcholine higher than phosphatidylglycerol equal to phosphatidylethanolamine higher than phosphatidylinositol higher than phosphatidylserine
-
-
?
phosphatidylserine + H2O
phosphatidate + serine
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylcholine higher than phosphatidylglycerol higher than phosphatidylinositol higher than phosphatidylserine
-
-
?
phosphatidylserine + H2O
phosphatidate + serine
the order of substrates in the rates of hydrolysis is: phosphatidylethanolamine higher than phosphatidylglycerol higher than phosphatidylcholine higher than phosphatidylserine higher than phosphatidylinositol
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
-
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
sphingomyelin + H2O
N-acylsphingosylphosphate + choline
-
-
-
?
sphingomyelin + H2O
N-acylsphingosylphosphate + choline
-
-
-
-
?
sphingomyelin + H2O
N-acylsphingosylphosphate + choline
-
-
-
-
?
sphingomyelin + H2O
N-acylsphingosylphosphate + choline
-
-
-
-
?
sphingomyelin + H2O
N-acylsphingosylphosphate + choline
-
-
-
-
?
additional information
?
-
-
enzyme displays high transphosphatidylation activity and no hydrolysis activity. In the PLD-catalyzed synthesis process (12 h), both the transphosphatidylation conversion rate and selectivity of phosphatidylserine and docosahexaenoic acid-phosphatidylserine are about 100%
-
-
?
additional information
?
-
-
enzyme displays high transphosphatidylation activity and no hydrolysis activity. In the PLD-catalyzed synthesis process (12 h), both the transphosphatidylation conversion rate and selectivity of phosphatidylserine and docosahexaenoic acid-phosphatidylserine are about 100%
-
-
?
additional information
?
-
-
PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, the latter with a primary alcohol, both pathway share a common intermediate, mechanism, overview
-
-
?
additional information
?
-
-
PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, the latter with a primary alcohol. Development of an transphosphatidylation assay method with a combination of unnatural phosphatidyl acceptor and tandem electrospray ionization mass spectrometry for tracing phospholipase D activity, overview
-
-
?
additional information
?
-
-
transphosphatidylation reaction is typically carried out in a bi-phase system consisting of a water-immiscible organic solvent (e.g., diethylether, ethylacetate) containing phospholipids and an aqueous solution of enzyme and acceptor compounds (e.g., ethanolamine, glycerol, serine)
-
-
?
additional information
?
-
-
transphosphatidylation reaction is typically carried out in a bi-phase system consisting of a water-immiscible organic solvent (e.g., diethylether, ethylacetate) containing phospholipids and an aqueous solution of enzyme and acceptor compounds (e.g., ethanolamine, glycerol, serine)
-
-
?
additional information
?
-
-
phospholipid acyl composition in wild type and enzyme-suppressed mutants
-
?
additional information
?
-
-
involved in wound-induced metabolism of polyunsaturated fatty acids
-
?
additional information
?
-
-
hydrolysis of phosphatidylcholine by enzyme isoforms PLDzeta1 and PLDzeta2 during phosphorus starvation contributes to the supply of inorganic phosphorus for cell metabolism and diacylglycerol moieties for galactolipid synthesis
-
-
?
additional information
?
-
-
incubation of Arabidopsis thaliana cell suspensions with primary alcohols inhibit the induction of two salicylic acid-responsive genes, PR1 and WRKY38, in a dose dependent manner. This inhibitory effect is more pronounced when the primary alcohols are more hydrophobic. Secondary or tertiary alcohols have no inhibitory effect. These results show that PLD activity is upstream of the induction of these genes by salicylic acid. A detailed analysis of the regulation of salicylic acid-responsive genes show that PLD can act both positively and negatively, either on gene induction or gene repression
-
-
?
additional information
?
-
-
PLDalpha1 interacts with the Galpha1 subunit of the heterotrimeric G protein to inhibit stomatal opening
-
-
?
additional information
?
-
-
the different PLDs exhibit distinguishable reaction conditions, substrate preferences and subcellular localization, overview. PLDalpha1 interacts with Galpha protein, a heterotrimeric Galpha protein to prevent closed stomata from opening
-
-
?
additional information
?
-
-
in presence of primary alcohols, such as 1-butanol or ethanol, PLD also has a unique ability to transfer phosphatidyl group to a primary alcohol to form phosphatidylalcohol at the expense of phosphatidic acid
-
-
?
additional information
?
-
-
isozyme PLDalpha3 hydrolyzes multiple substrates with distinguishable preferences
-
-
?
additional information
?
-
-
PLDepsilon is active under a broad range of reaction conditions
-
-
?
additional information
?
-
-
the enzyme hydrolyzes glycosylinositol phosphoceramide specifically, but not glycerophospholipids, phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, or sphingomyelin, MALDI-TOF mass spectrometry product identification, overview
-
-
?
additional information
?
-
Peanut PLD may be involved in drought sensitivity and tolerance responses. PLD gene expression is induced faster by drought stress in the drought-sensitive lines than in the drought tolerant lines. Cultivated peanut has multiple copies (3 to 5 copies) of the PLD gene
-
-
?
additional information
?
-
-
Peanut PLD may be involved in drought sensitivity and tolerance responses. PLD gene expression is induced faster by drought stress in the drought-sensitive lines than in the drought tolerant lines. Cultivated peanut has multiple copies (3 to 5 copies) of the PLD gene
-
-
?
additional information
?
-
-
regulation of phospholipase D activity by light and phytohormones. abscisic acid manifests a short-term stimulating effect on phospholipase D activity in the green seedlings and inhibits phospholipase D activity in the etiolated plants. Kinetin inhibits enzyme activity in the etiolated seedlings and does not affect its activity in light. gibberellic acid does not markedly affect phospholipase D activity in the etiolated plant and activates this enzyme in the green seedling
-
-
?
additional information
?
-
-
white and red light exposure inhibits enzyme activity in etiolated seedlings. Phospholipase D activity is regulated by light with involvement of phytochrome photoreceptor and associated with photosynthesis process
-
-
?
additional information
?
-
-
crosstalk between protein kinase A and C regulates phospholipase D and F-actin formation during sperm capacitation
-
-
?
additional information
?
-
-
vitamin C at pharmacological doses activates PLD in the lung microvascular endothelial cells through oxidative stress and activation of mitogen-activated protein kinase
-
-
?
additional information
?
-
-
PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor
-
-
?
additional information
?
-
-
PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor, the transphosphatidylation reaction is an index of PLD activity in intact cells
-
-
?
additional information
?
-
phosphatidylcholines with short-chain fatty acids are better substrates than phosphatidylcholines with long fatty acid chains. Lysophosphatidylcholine is not accepted as substrate
-
-
?
additional information
?
-
-
spectrophotometric determination of phosphatidic acid via iron(III) complexation in presence of salicylate for simply assaying phospholipase D activity, method evaluation and optimization, overview
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze glycosylinositol phosphoceramide
-
-
?
additional information
?
-
-
the enzyme hydrolyzes glycosylinositol phosphoceramide specifically, but not glycerophospholipids, phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, or sphingomyelin, MALDI-TOF mass spectrometry product identification, overview
-
-
?
additional information
?
-
transphosphatidylation reaction is typically carried out in a bi-phase system consisting of a water-immiscible organic solvent (e.g., diethylether, ethylacetate) containing phospholipids and an aqueous solution of enzyme and acceptor compounds (e.g., ethanolamine, glycerol, serine). Transphosphatidylation with L-serine gives phosphatidyl-L-serine, no activity with D-serine
-
-
?
additional information
?
-
-
the enzyme hydrolyzes glycosylinositol phosphoceramide specifically, but not glycerophospholipids, phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, or sphingomyelin, MALDI-TOF mass spectrometry product identification, overview
-
-
?
additional information
?
-
-
increase in local membrane monomeric tubulin concentration inhibits PLD2 activity. The PLD2 regulating mechanism via tubulin exists in endogeneous muscarinic receptor possessing cells
-
-
?
additional information
?
-
-
phorbol 12-myristate 13-acetate induces PLD2 activation via the involvement of protein kinase Calpha. PLD2 becomes phosphorylated on both Ser and Thr residues. Interaction rather than phosphorylation underscores the activation of PLD2 by protein kinase Calpha in vivo. Phosphorylation may contribute to the inactivation of the enzyme
-
-
?
additional information
?
-
-
PLD is also active in a transphosphatidylation assay with substrate 1-butanol resulting in production of phosphatidylbutanol
-
-
?
additional information
?
-
-
phospholipase D activity is essential for actin localization and actin-based motility
-
-
?
additional information
?
-
-
phospholipase D facilitates phototransduction by maintaining adequate levels of phosphatidylinositol 4,5-bisphosphate and by protecting the visual system from metarhodopsin-induced, low light degeneration
-
-
?
additional information
?
-
-
enzyme is required for cellularization, i.e. A form of cytokinesis in which polarized membrane extension proceeds in part through incorporation of new membrane via fusion of apically-translocated Golgi-derived vesicles. Loss of enzyme activity frequently leads to early embryonic developmental arrest
-
-
?
additional information
?
-
-
phospholipase D alpha is a key enzyme involved in membrane deterioration that occurs during fruit ripening and senescence
-
-
?
additional information
?
-
-
phospholipase D alpha is a key enzyme involved in membrane deterioration that occurs during fruit ripening and senescence
-
-
?
additional information
?
-
-
purified PLDalpha is inactive in vitro on bilamellar substrates. It is fully active on mixed micelles made with phospholipids and a mixture of Triton-X100 and SDS at equal concentrations. Ca2+ interacts with the SDS contained in the mixed micelles thus leading to an aggregated form of the substrate which is more easily hydrolyzed by PLDalpha
-
-
?
additional information
?
-
-
activation of phospholipase D by 8-Br-cAMP occurs through a pathway involving Src, Ras, and ERK in human endometrial stromal cells
-
-
?
additional information
?
-
-
lysophosphatidic acid increases phospholipase D activity in neutrophils
-
-
?
additional information
?
-
-
Munc-18-1 is a potent negative regulator of basal PLD activity. EGF stimulation abolishes this interaction
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additional information
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PLD is actived by the chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine. PLD2, but not PLD1, contributes to PLD activity mediated by N-formyl-methionyl-leucyl-phenylalanine. Extracellular signal-regulated kinase/PLD2 pathway contributes to N-formyl-methionyl-leucyl-phenylalanine-mediated oxidant production
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additional information
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PLD1 is required for normal organization of the actin cytoskeleton and for cell motility. PLD1 is a critical factor in the organization of the actin-based cytoskeleton, with regard to cell adhesion and migration
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additional information
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PLD1 plays a role in the induction of gene expression of Cox-2 and IL-8
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additional information
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priming is a critical regulator of PLD activation
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additional information
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protein casein kinase II stimulates basal phospholipase D (PLD1 and PLD2) activity as well as PMA-induced phospholipase D activation in human U87 astroglioma cells
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additional information
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protein casein kinase II stimulates basal phospholipase D (PLD1 and PLD2) activity as well as PMA-induced phospholipase D activation in human U87 astroglioma cells
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additional information
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protein casein kinase II stimulates basal phospholipase D (PLD1 and PLD2) activity as well as PMA-induced phospholipase D activation in human U87 astroglioma cells
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additional information
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stimulation of PLD activity and its mRNA expression by lipopolysaccharides might be required for IL-2 R expression and a sustained PKC dependent intracellular pH elevation but not for secretion of IL-2 or IL-4 in T cells
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additional information
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the enzyme plays an essential role in the swelling-induced vesicle cycling and in the activation of volume-sensitive anion channels
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additional information
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the PLD gene undergoes qualitative changes in transcription regulation during granulocytic differentiation
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additional information
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the PLD gene undergoes qualitative changes in transcription regulation during granulocytic differentiation
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additional information
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endocytotic trafficking of my-opioid receptor MOR1, delta-opioid receptor DOR and cannabinoid receptor isoform CB1 are mediated by an isoform PLD2 dependent pathway
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additional information
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enzyme is activated downstream of ERK1/2 kinases upon chemokine receptor CCR5 activation and plays a major role in promoting HIV-1 LTR transactivation and virus replication
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additional information
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enzyme isoform PLD1 and PLD2 are closely related with Bcl-2 expression together with phospholipase A2, but not with phosphatidic acid phosphohydrolase, during taxotere-induced apoptosis in SNU 484 cells
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additional information
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isoform PLD1 isassociated with cell polarity and directionality concomitantly with adhesion and F-actin polymerization in response to IL-8
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additional information
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isoform PLD1 isassociated with cell polarity and directionality concomitantly with adhesion and F-actin polymerization in response to IL-8
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additional information
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isoform PLD1 plays a crucial role in collagen type I production through mTOR signaling in dermal fibroblast
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additional information
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isoform PLD2 is associated with cell polarity and directionality concomitantly with adhesion and F-actin polymerization in response to IL-8
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additional information
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isoform PLD2 is associated with cell polarity and directionality concomitantly with adhesion and F-actin polymerization in response to IL-8
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additional information
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phospholipase D functions as a GTPase activating protein through the phox homology domain, which directly activates the GTPase domain of dynamin. Enzyme increases epidermal growth factor receptor endocytosis at physiological concentrations of epidermal growth factor
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additional information
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up-regulation of beta-defensin-2 by cell wall extract of Fusobacterium nucleatum or phorbol 12-myristate 13-acetate is mediated by phospholipase D
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additional information
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PLD product phosphatidic acid acts as a membrane anchor of Rac1. The C-terminal polybasic motif of Rac1 is responsible for direct interaction with phosphatidic acid. It is shown that phosphatidic acid induces dissociation of Rho-guanine nucleotide dissociation inhibitor from Rac1 and that phosphatidic acid-mediated Rac1 localization is important for integrin-mediated lamellipodia formation, cell spreading, and migration
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additional information
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PLD product phosphatidic acid acts as a membrane anchor of Rac1. The C-terminal polybasic motif of Rac1 is responsible for direct interaction with phosphatidic acid. It is shown that phosphatidic acid induces dissociation of Rho-guanine nucleotide dissociation inhibitor from Rac1 and that phosphatidic acid-mediated Rac1 localization is important for integrin-mediated lamellipodia formation, cell spreading, and migration
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additional information
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PLD product phosphatidic acid acts as a membrane anchor of Rac1. The C-terminal polybasic motif of Rac1 is responsible for direct interaction with phosphatidic acid. Phosphatidic acid induces dissociation of Rho-guanine nucleotide dissociation inhibitor from Rac1 and that phosphatidic acid-mediated Rac1 localization is important for integrin-mediated lamellipodia formation, cell spreading, and migration
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additional information
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PLD product phosphatidic acid acts as a membrane anchor of Rac1. The C-terminal polybasic motif of Rac1 is responsible for direct interaction with phosphatidic acid. Phosphatidic acid induces dissociation of Rho-guanine nucleotide dissociation inhibitor from Rac1 and that phosphatidic acid-mediated Rac1 localization is important for integrin-mediated lamellipodia formation, cell spreading, and migration
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additional information
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effects of active and inactive phospholipase D2 on signal transduction, adhesion, migration, invasion, and metastasis in EL4 lymphoma cells, overview
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additional information
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isozymes PLD1 and PLD2 share aboout 50% homology, but are regulated and localized differently in the cell. In vitro, PLD2 has a higher basal activity than PLD1, but overall cellular activity of PLD is low
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additional information
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isozymes PLD1 and PLD2 share aboout 50% homology, but are regulated and localized differently in the cell. In vitro, PLD2 has a higher basal activity than PLD1, but overall cellular activity of PLD is low
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additional information
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NF-kappaB and transcription factor Sp1 are essential transcriptional factors linking PLD to MMP-2 upregulation
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additional information
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PLD isozymes are cleaved by caspase 3, cleavage site determination, isozyme PLD2alpha contains two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S between the PLD domains, mutational analysis, overview
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additional information
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PLD isozymes are cleaved by caspase 3, cleavage site determination, isozyme PLD2alpha contains two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S between the PLD domains, mutational analysis, overview
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additional information
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PLD isozymes are cleaved by caspase 3, cleavage site determination, isozyme PLD2alpha contains two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S between the PLD domains, mutational analysis, overview
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additional information
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PLD isozymes are cleaved by caspase 3, cleavage site determination, isozymes PLD1beta and PLD2alpha contain each two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S and DFID631R between the PLD domains, respectively, mutational analysis, overview
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additional information
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PLD isozymes are cleaved by caspase 3, cleavage site determination, isozymes PLD1beta and PLD2alpha contain each two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S and DFID631R between the PLD domains, respectively, mutational analysis, overview
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additional information
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PLD isozymes are cleaved by caspase 3, cleavage site determination, isozymes PLD1beta and PLD2alpha contain each two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S and DFID631R between the PLD domains, respectively, mutational analysis, overview
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additional information
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PLD1 mediates the reactive oxygen species-induced increase in diacylglycerol, which facilitates PKD1 localization to the mitochondria and its activation. Diacylglycerol, to which PKD1 is recruited, is formed downstream of phospholipase D1 and is required for PKD1 localization in the mitochondria and well as activation under oxidative stress, overview. Role for PLD1-induced DAG as a competent second messenger at the mitochondria that relays ROS to PKD1-mediated mitochondria-to-nucleus signaling
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additional information
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during PLD stimulation of phosphatidylcholine hydrolysis, primary alcohols can replace water in the transphosphatidylation reaction forming phosphatidylbutanol instead of phosphatidic acid
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additional information
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except for PLD2c, all PLD1 and PLD2 isozymes contain the catalytic core regions comprised of highly conserved domain I-IV. In domains II and IV, the enzymes contain two HxKxxxxD sequences designated HKD motifs, which are essential for enzymatic catalysis
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additional information
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PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor leading to formation of phosphatidylbutan-1-ol
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additional information
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PLD also performs transphosphatidylation using ethanol as phosphatidyl acceptor
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additional information
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PLD also shows transphosphatidylation activity with 1-butanol resulting in formation of phosphatidylbutanol
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additional information
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PLD also shows transphosphatidylation activity with 1-butanol resulting in formation of phosphatidylbutanol
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additional information
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PLD also shows transphosphatidylation activity with 1-butanol resulting in formation of phosphatidylbutanol
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additional information
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PLD assay on whole hematopoietic cells
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additional information
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the enzyme also performs transphosphatidylation transferring phosphatidic acid to a primary alcohol
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additional information
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transphosphatidylation reaction is typically carried out in a bi-phase system consisting of a water-immiscible organic solvent (e.g., diethylether, ethylacetate) containing phospholipids and an aqueous solution of enzyme and acceptor compounds (e.g., ethanolamine, glycerol, serine)
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additional information
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enzyme evokes inflammatory reactions following injections into rabbit skin. Enzyme has a small hemolytic effect
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additional information
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enzyme evokes inflammatory reactions following injections into rabbit skin. Enzyme has a small hemolytic effect
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additional information
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enzyme evokes inflammatory reactions following injections into rabbit skin. Enzyme has a small hemolytic effect
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additional information
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enzyme evokes inflammatory reactions following injections into rabbit skin. Treatment of Madin-Darby canine kidney cells results in appearance of cytoplasmic vacuolization, altered cellular spreading and cell-cell adhesion. Enzyme causes a high degree of hemolysis
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additional information
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enzyme evokes inflammatory reactions following injections into rabbit skin. Treatment of Madin-Darby canine kidney cells results in appearance of cytoplasmic vacuolization, altered cellular spreading and cell-cell adhesion. Enzyme causes a high degree of hemolysis
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additional information
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enzyme evokes inflammatory reactions following injections into rabbit skin. Treatment of Madin-Darby canine kidney cells results in appearance of cytoplasmic vacuolization, altered cellular spreading and cell-cell adhesion. Enzyme causes a high degree of hemolysis
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additional information
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enzyme shows dermonbecrotic properties. Enzyme causes massive inflammatory response in rabbit skin dermis, evokes platelet aggregation, increases vascular permeability, causes edema and death in mice
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additional information
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down-regulation of melanogenesis is mediated by phospholipase D2 but not by phospholipase D1 through turbiquitin proteasome-mediated degradation of tyrosinase. PLD2 may play an important role in regulating pigmentation in vivo
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additional information
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essential role for phospholipase D in activation of protein kinase C and degranulation in mast cells. Production of phosphatidic acid by PLD facilitates activation of protein kinase C and, in turn, degranulation, although additional PLD-dependent processes appear to be critical for antigen-mediated degranulation
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additional information
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mechanical stimuli activate mTOR (mammalian target of rapamycin) signaling through a phospholipase D-dependent increase in phosphatidic acid
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additional information
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PLD might be implicated in core protein-induced transformation
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additional information
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sphingosine significantly stimulates phospholipase D activity in mouse C2c12 myoblasts via phosphorylation to sphingosine 1-phosphate
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additional information
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survival signals generated by PLD attenuate expression of Egr-1 by activation of phosphatidylinositol 3-kinase signaling pathway and induction of PTEN by early growth response-1, which confers resistance to apoptosis
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additional information
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the PLD2 PX domain enables PLD1 to mediate signal transduction via ERK1/2 by providing a direct binding site for phosphatidylinositol 3,4,5-triphosphate and by activating PLD1
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additional information
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mechanical stimuli activate signaling by mTOR, i.e. mammalian target of rapamycin, in skeletal muscle through an enzyme-dependent increase in phosphatidic acid
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additional information
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PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor
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additional information
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PLD2 is regulated by phosphorylation-dephosphorylation, detailed overview
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additional information
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except for PLD2c, all PLD1 and PLD2 isozymes contain the catalytic core regions comprised of highly conserved domain I-IV. In domains II and IV, the enzymes contain two HxKxxxxD sequences designated HKD motifs, which are essential for enzymatic catalysis
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additional information
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PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor leading to formation of phosphatidylbutan-1-ol
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additional information
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PLD assay on whole haematopoietic cells
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additional information
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the catalytic activity of PLD is not required for PLD-mediated CKII inhibition, possible inhibition mechanism, overview
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additional information
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enzyme augments gonococcus invasion of cervical epithelia by interacting with Akt kinase in a hosphatidylinositol-(3,4,5)-trisphosphate-independent manner, resulting in subversion of normal cervical cell signaling
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additional information
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PLD activity is constitutive during pollen tube growth. Hypoosmotic stress stimulates PLD activity, hyperosmotic stress attenuates PLD activity
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additional information
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ability of PLD-generated phosphatidic acid to control actin polymerization and the reciprocal ability of actin to specifically modulate PIP2-dependent PLD, PLDbeta, activity through direct interaction
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additional information
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ability of PLD-generated phosphatidic acid to control actin polymerization and the reciprocal ability of actin to specifically modulate PIP2-dependent PLD, PLDbeta, activity through direct interaction
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additional information
?
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ability of PLD-generated phosphatidic acid to control actin polymerization and the reciprocal ability of actin to specifically modulate PIP2-dependent PLD, PLDbeta, activity through direct interaction
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additional information
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ability of PLD-generated phosphatidic acid to control actin polymerization and the reciprocal ability of actin to specifically modulate PIP2-dependent PLD, PLDbeta, activity through direct interaction
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additional information
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enhanced binding of isozyme PLDbeta1 to actin is mediated by amino acid residues Asn323 and Thr382
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additional information
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enhanced binding of isozyme PLDbeta1 to actin is mediated by amino acid residues Asn323 and Thr382
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additional information
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enhanced binding of isozyme PLDbeta1 to actin is mediated by amino acid residues Asn323 and Thr382
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additional information
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enhanced binding of isozyme PLDbeta1 to actin is mediated by amino acid residues Asn323 and Thr382
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additional information
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constitutive cation channel activity in ear artery myocytes is mediated by diacylglycerol which is generated by phosphatidylcholine-phospholipase D via phosphatidic acid which represents a novel activation pathway of cation channels in vascular myocytes
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additional information
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PLD is activated by H2O2. The activation by H2O2 enhances phytoalexin biosynthesis in rice cells
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additional information
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isoform PLDbeta1 stimulates abscisic acid signaling by activating SAP kinase, thus repressing GAmyb expression and inhibiting seed germination
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additional information
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isoform PLDbeta1 stimulates abscisic acid signaling by activating SAP kinase, thus repressing GAmyb expression and inhibiting seed germination
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additional information
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isoenzyme PLD-A does not catalyze head group exchange and is inactive towards phosphatidylethanolamine
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additional information
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isoenzyme PLD-B is inactive towards phosphatidylethanolamine. Pld-B shows high transphosphorylation potential in the conversion of phosphatidylcholine into phosphatidylglycerol and phosphatidylethanolamine. The enzyme also catalyzes the transesterification of octadecylphosphocholine into octadecylphosphoglycerol or octadecylphosphoethanolamine
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additional information
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PldA contributes to the ability of Pseudomonas aeruginosa PAO1 to persist in a chronic pulmonary infection model in rats
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additional information
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PldA is capable of using methanol, ethanol, and butanol to produce transphosphatidylation products
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additional information
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5-[4-acridin-[9-ylamino]phenyl]-5-methyl-3-methylenedihydrofuran-2-one inhibits the formyl-Met-Leu-Phe-stimulated phospholipase D activity, mainly through the blockade of RhoA activation and degranulation
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additional information
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alpha-adrenoreceptor activation increases phospholipase D activity
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additional information
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dependency of activation of protein kinase D on phospholipase D, phospholipase D could be a key molecule that links Rho/protein kinase C signaling to diacylglycerol for protein kinase D activation
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additional information
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interaction of the PLD1 PX domain with phosphatidylinositol 3,4,5-trisphosphate and/or phosphatidic acid (or phosphatidylserine) may be an important factor in the spatiotemporal regulation and activation of PLD1
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additional information
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lysophosphatidic acid activates protein translation through the action of PLD1-generated phosphatidic acid on mTOR and the phosphoinositide 3-kinase/Akt pathway
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additional information
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Munc-18-1 is a potent negative regulator of basal PLD activity. EGF stimulation abolishes this interaction
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additional information
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phospholipase D elevates the level of MDM2 and suppresses DNA damage-induced increase in p53
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additional information
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phospholipase D plays an important role in the regulation of beta-hexosaminidase release in actively sensitized rat peritoneal mast cells
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additional information
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PLD1 is a signaling node, in which integration of convergent signals occurs within discrete locales of the cellular membrane
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additional information
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PLD2 may be involved in early developmental processes of some neuronal progenitors
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additional information
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prolonged elevation of PLD activity is required for myogenic differentiation
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additional information
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the enzyme participates in myogenesis through phosphatidic acid- and phosphatidylinositol bisphosphate-dependent actin fiber formation
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additional information
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thyrotrophin-releasing hormone increases phospholipase D activity through stimulation of protein kinase C in GH3 cells
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additional information
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no substrate: N-palmitoylethanolamine phosphate, phosphatidylcholine, phosphatidylserine, phosphatidylinositol
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additional information
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phospholipase D activates native TRPC3 cation channels after stimulation of G-protein-coupled type I glutamate receptors in the cerebellum. Small GTPases might be involved in the activation mechanism of TRPC3 in rat cerebellar Purkinje cells, overview
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additional information
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PLD catalyzes the hydrolysis of phospholipids resulting in the generation of phosphatidic acid and the release of the polar head group. The enzyme also catalyzes a transphosphatidylation reaction, in which the aliphatic chain of the primary alcohol is transferred to the phosphatidyl moiety of the phosphatidic acid product
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additional information
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PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, 1-butanol serves as acceptor in the transphosphatidylation reaction, while 2-butanol does not. PLD-catalysed PtdOH formation may be necessary for EGF-induced macropinocytosis
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additional information
?
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except for PLD2c, all PLD1 and PLD2 isozymes contain the catalytic core regions comprised of highly conserved domain I-IV. In domains II and IV, the enzymes contain two HxKxxxxD sequences designated HKD motifs, which are essential for enzymatic catalysis
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?
additional information
?
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PLD also performs transphosphatidylation using ethanol as phosphatidyl acceptor
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additional information
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does not catalyze transphosphatidylation reaction with primary short-chain alcohols
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?
additional information
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the Arf-GTPase-activating protein Gsc1p is essential for sporulation and positively regulates the phospholipase D Spo14p
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additional information
?
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transphosphatidylation reaction is typically carried out in a bi-phase system consisting of a water-immiscible organic solvent (e.g., diethylether, ethylacetate) containing phospholipids and an aqueous solution of enzyme and acceptor compounds (e.g., ethanolamine, glycerol, serine)
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additional information
?
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transphosphatidylation reaction is typically carried out in a bi-phase system consisting of a water-immiscible organic solvent (e.g., diethylether, ethylacetate) containing phospholipids and an aqueous solution of enzyme and acceptor compounds (e.g., ethanolamine, glycerol, serine)
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additional information
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enzyme exhibits a ratio of hydrolytic activity to transphosphatidylation of 2.5
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additional information
?
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enzyme shows a strong preference for ethanolamine over choline substrates. Very poor substrate: N-hexanoyl-D-erythrosphingosylphosphorylcholine
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additional information
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enzyme shows a strong preference for ethanolamine over choline substrates. Very poor substrate: N-hexanoyl-D-erythrosphingosylphosphorylcholine
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?
additional information
?
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silymarin secretion and its elicitation by methyl jasmonate in cell cultures of Silybum marianum is mediated by phospholipase D-phosphatidic acid, overview
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?
additional information
?
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expression of LePLDbeta1 is increased upon treatment with xylanase. Possible involvement of LePLDbeta1 in plant defense response
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?
additional information
?
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interaction of PLDalpha C2 domain with synthetic unilamellar vesicles shows maximum affinity towards phosphatidic acid, and virtually no binding with phosphatidylcholine. Electrostatic, rather than a hydrophobic mode of interaction between C2 domain and the phospholipid vesicles. The binding towards phosphoinositides is reduced with increasing degree of phosphorylation
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additional information
?
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in the presence of n-butanol, PLD specifically catalyses the formation of phosphatidyl-butanol by transferring the phosphatidyl group of its substrate to n-butanol instead of water. Water and n-butanol compete as substrates for PLD
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?
additional information
?
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PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, the latter with a primary alcohol, both pathway share a common intermediate, mechanism, overview
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?
additional information
?
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transphosphatidylation reaction is typically carried out in a bi-phase system consisting of a water-immiscible organic solvent (e.g., diethylether, ethylacetate) containing phospholipids and an aqueous solution of enzyme and acceptor compounds (e.g., ethanolamine, glycerol, serine). Transphosphatidylation with L- and D-serine gives phosphatidyl-L- and D-serine, respectively. Synthesis of phosphatidylinositol by bacterial enzyme is unsuccessful is likely the low affinity of the enzyme toward myo-inositol, a bulky molecule causing steric hindrances in the active site
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additional information
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use of monlayers of pure dipalmitoylphosphatidylcholine, equimolar mixtures of dipalmitoylphosphatidylcholineand n-hexadecanol and of dipalmitoylphosphatidylcholine and dipalmitoylglycerol as model substrate systems. Activity of enzyme exhibits different dependencies on surface pressure and is correlated to the phase state of the monlayers. Self-regulating mechanism for the concentration of the second messenger phosphatidic acid within biological membranes
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?
additional information
?
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analysis of structure of PLD-treated subtrate egg yolk in an oil-in-water emulsion using circular dichroism and scanning electron microscopy, overview
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?
additional information
?
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transphosphatidylation reaction is typically carried out in a bi-phase system consisting of a water-immiscible organic solvent (e.g., diethylether, ethylacetate) containing phospholipids and an aqueous solution of enzyme and acceptor compounds (e.g., ethanolamine, glycerol, serine). Transphosphatidylation with L- and D-serine gives phosphatidyl-L- and D-serine, respectively. Synthesis of phosphatidylinositol by bacterial enzyme is unsuccessful is likely the low affinity of the enzyme toward myo-inositol, a bulky molecule causing steric hindrances in the active site
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?
additional information
?
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PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, the latter with a primary alcohol, both pathway share a common intermediate, mechanism, overview
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-
?
additional information
?
-
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transphosphatidylation reaction is typically carried out in a bi-phase system consisting of a water-immiscible organic solvent (e.g., diethylether, ethylacetate) containing phospholipids and an aqueous solution of enzyme and acceptor compounds (e.g., ethanolamine, glycerol, serine). Transphosphatidylation with L- and D-serine gives phosphatidyl-L- and D-serine, respectively. Synthesis of phosphatidylinositol by bacterial enzyme is unsuccessful is likely the low affinity of the enzyme toward myo-inositol, a bulky molecule causing steric hindrances in the active site
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?
additional information
?
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-
PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, the latter with a primary alcohol, both pathway share a common intermediate, mechanism, overview
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-
?
additional information
?
-
-
the enzyme displays transphosphatidylation activity, and phosphatidylserine can be synthesized with L-serine and soybean lecithin as substrates
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?
additional information
?
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usage of a microaqueous water-immiscible organic solvent in the bioconversion of L-serine and Glycine max phosphatidylcholine solves the problem of water production and increased hydrolysis rates compared to transphosphatidylation. Using butyl acetate in a biphasic system, the transphosphatidylation rate is 86-88%, while the hydrolysis rate is 0-1%, method evaluation, overview
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?
additional information
?
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-
usage of a microaqueous water-immiscible organic solvent in the bioconversion of L-serine and Glycine max phosphatidylcholine solves the problem of water production and increased hydrolysis rates compared to transphosphatidylation. Using butyl acetate in a biphasic system, the transphosphatidylation rate is 86-88%, while the hydrolysis rate is 0-1%, method evaluation, overview
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?
additional information
?
-
-
G188 and D191 are the key amino acids involved in recognition of phospholipids. A426 and L438 enhance transphosphatidylation activities regardless of the substrate form
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?
additional information
?
-
-
PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, the latter with a primary alcohol, both pathway share a common intermediate, mechanism, overview
-
-
?
additional information
?
-
-
G188 and D191 are the key amino acids involved in recognition of phospholipids. A426 and L438 enhance transphosphatidylation activities regardless of the substrate form
-
-
?
additional information
?
-
-
structural requirements of substrates, general molecular aspects
-
?
additional information
?
-
-
in presence of glycerol, the rate of hydrolysis of phosphatiylcholine and the rate of phosphytidylglycerol formation are almost identical
-
-
?
additional information
?
-
PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, the latter with a primary alcohol, both pathway share a common intermediate, mechanism, overview
-
-
?
additional information
?
-
-
in presence of glycerol, the rate of hydrolysis of phosphatiylcholine and the rate of phosphytidylglycerol formation are almost identical
-
-
?
additional information
?
-
the enzyme prefers mixed micelle substrates to liposomal substrates. The rate-limiting steps of hydrolysis of mixed micelle 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine and emulsified lysophosphatidylcholine are the bulk step and the surface step, respectively
-
-
?
additional information
?
-
-
application of the dispersed phantom scatterer technique, which allows qualitatively and quantitatively evaluation of substrate recognition by inactivated PLD-PMF mutants, dissociation constants between different PLD mutants and LPC/C12E5-coated phantom nanoparticles, C12E5 is a commercial surfactant, n-pentaethylene glycol monododecyl ether, method evaluation, overview
-
-
?
additional information
?
-
-
PLDSt cannot catalyze transphosphatidylation of glycerol, L-serine, myo-inositol and ethanolamine, the Streptomyces tendae PLD possesses only hydrolytic activity
-
-
?
additional information
?
-
-
effects of biochemical properties of the substrates on phospholipase D activity
-
-
?
additional information
?
-
-
no substrate: phosphatidylethanolamine
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DNA + H2O
smaller DNA fragments
-
endonuclease
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
both phosphatidylcholine and phosphatidylethanolamine are substrates for phospholipase D in UMR-106 osteoblastic cells and can therefore be sources of phospholipid hydrolysis products for downstream signaling in osteoblast
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
phosphatidylcholine + H2O
choline + phosphatidic acid
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
parathyroid hormone stimulates phosphatidylethanolamine hydrolysis by phospholipase D in osteoblastic cells. Both phosphatidylcholine and phosphatidylethanolamine are substrates for phospholipase D in UMR-106 osteoblastic cells and can therefore be sources of phospholipid hydrolysis products for downstream signaling in osteoblast
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidic acid
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
phosphatidylserine + H2O
serine + phosphatidic acid
phospholipid + alcohol
phospholipid + alcohol
phospholipid + H2O
phosphatidic acid + alcohol
additional information
?
-
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
Regulation and effectors of phospholipase D and phosphatidic acid on the Golgi apparatus, overview
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
phosphatidic acid binds to ABI1, a PP2C, which functions as a negative regulator in abscisic acid signalling in stomata closure. Phosphatidic acid stimulated NADPH oxidase activity and reactive oxygen species production in wild-type and PLDalpha1-deficient cells, cellular and physiological effects of phosphatidic acid, overview
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
phosphatidic acid has unique bioactive properties and can modify both the physical and signalling properties of lipid bilayers. Perturbation of phosphatidic metabolism can alter membrane dynamics with consequences on cell viability, phosphatidic acid functions, overview
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
phosphatidic acid induces upregulation of MMP-2 mediated by protein kinase C, protein kinase A, nuclear factor-kappaB, and Sp1. Phosphatidic acid induces nuclear localization and the transactivation of NF-kappaB in glioma cells.
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
phosphatidic acid plays a regulatory role in important cellular processes such as secretion, cellular shape change, and movement
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
hydrolysis of phosphatidylcholine by phospholipase D leads to the generation of phosphatidic acid, which is itself a source of diacylglycerol. PLD2 emerges as an early player upstream of the Ras-MAPK-IL-2 pathway in T-cells via phosphatidic acid and diacylglycerol production
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
hydrolysis of phosphatidylcholine by phospholipase D leads to the generation of phosphatidic acid, PA, which is itself a source of diacylglycerol. PLD2 emerges as an early player upstream of the Ras-MAPK-IL-2 pathway in T-cells via PA and DAG production
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
phosphatidic acid activates the production of and promotes accumulation of silymarin, overview
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
phosphatidic acid acts as a second messenger in phosphorylation cascades
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidic acid
-
-
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidic acid
-
-
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
glycerol + phosphatidic acid
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
-
?
phosphatidylserine + H2O
serine + phosphatidic acid
-
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + alcohol
phospholipid + alcohol
-
transphosphaditylation
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
phosphoric ester hydrolysis
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
additional information
?
-
-
PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, the latter with a primary alcohol, both pathway share a common intermediate, mechanism, overview
-
-
?
additional information
?
-
-
involved in wound-induced metabolism of polyunsaturated fatty acids
-
?
additional information
?
-
-
hydrolysis of phosphatidylcholine by enzyme isoforms PLDzeta1 and PLDzeta2 during phosphorus starvation contributes to the supply of inorganic phosphorus for cell metabolism and diacylglycerol moieties for galactolipid synthesis
-
-
?
additional information
?
-
-
incubation of Arabidopsis thaliana cell suspensions with primary alcohols inhibit the induction of two salicylic acid-responsive genes, PR1 and WRKY38, in a dose dependent manner. This inhibitory effect is more pronounced when the primary alcohols are more hydrophobic. Secondary or tertiary alcohols have no inhibitory effect. These results show that PLD activity is upstream of the induction of these genes by salicylic acid. A detailed analysis of the regulation of salicylic acid-responsive genes show that PLD can act both positively and negatively, either on gene induction or gene repression
-
-
?
additional information
?
-
-
PLDalpha1 interacts with the Galpha1 subunit of the heterotrimeric G protein to inhibit stomatal opening
-
-
?
additional information
?
-
-
the different PLDs exhibit distinguishable reaction conditions, substrate preferences and subcellular localization, overview. PLDalpha1 interacts with Galpha protein, a heterotrimeric Galpha protein to prevent closed stomata from opening
-
-
?
additional information
?
-
Peanut PLD may be involved in drought sensitivity and tolerance responses. PLD gene expression is induced faster by drought stress in the drought-sensitive lines than in the drought tolerant lines. Cultivated peanut has multiple copies (3 to 5 copies) of the PLD gene
-
-
?
additional information
?
-
-
Peanut PLD may be involved in drought sensitivity and tolerance responses. PLD gene expression is induced faster by drought stress in the drought-sensitive lines than in the drought tolerant lines. Cultivated peanut has multiple copies (3 to 5 copies) of the PLD gene
-
-
?
additional information
?
-
-
regulation of phospholipase D activity by light and phytohormones. abscisic acid manifests a short-term stimulating effect on phospholipase D activity in the green seedlings and inhibits phospholipase D activity in the etiolated plants. Kinetin inhibits enzyme activity in the etiolated seedlings and does not affect its activity in light. gibberellic acid does not markedly affect phospholipase D activity in the etiolated plant and activates this enzyme in the green seedling
-
-
?
additional information
?
-
-
white and red light exposure inhibits enzyme activity in etiolated seedlings. Phospholipase D activity is regulated by light with involvement of phytochrome photoreceptor and associated with photosynthesis process
-
-
?
additional information
?
-
-
crosstalk between protein kinase A and C regulates phospholipase D and F-actin formation during sperm capacitation
-
-
?
additional information
?
-
-
vitamin C at pharmacological doses activates PLD in the lung microvascular endothelial cells through oxidative stress and activation of mitogen-activated protein kinase
-
-
?
additional information
?
-
-
PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor, the transphosphatidylation reaction is an index of PLD activity in intact cells
-
-
?
additional information
?
-
-
increase in local membrane monomeric tubulin concentration inhibits PLD2 activity. The PLD2 regulating mechanism via tubulin exists in endogeneous muscarinic receptor possessing cells
-
-
?
additional information
?
-
-
phorbol 12-myristate 13-acetate induces PLD2 activation via the involvement of protein kinase Calpha. PLD2 becomes phosphorylated on both Ser and Thr residues. Interaction rather than phosphorylation underscores the activation of PLD2 by protein kinase Calpha in vivo. Phosphorylation may contribute to the inactivation of the enzyme
-
-
?
additional information
?
-
-
phospholipase D activity is essential for actin localization and actin-based motility
-
-
?
additional information
?
-
-
phospholipase D facilitates phototransduction by maintaining adequate levels of phosphatidylinositol 4,5-bisphosphate and by protecting the visual system from metarhodopsin-induced, low light degeneration
-
-
?
additional information
?
-
-
enzyme is required for cellularization, i.e. A form of cytokinesis in which polarized membrane extension proceeds in part through incorporation of new membrane via fusion of apically-translocated Golgi-derived vesicles. Loss of enzyme activity frequently leads to early embryonic developmental arrest
-
-
?
additional information
?
-
-
phospholipase D alpha is a key enzyme involved in membrane deterioration that occurs during fruit ripening and senescence
-
-
?
additional information
?
-
-
phospholipase D alpha is a key enzyme involved in membrane deterioration that occurs during fruit ripening and senescence
-
-
?
additional information
?
-
-
purified PLDalpha is inactive in vitro on bilamellar substrates. It is fully active on mixed micelles made with phospholipids and a mixture of Triton-X100 and SDS at equal concentrations. Ca2+ interacts with the SDS contained in the mixed micelles thus leading to an aggregated form of the substrate which is more easily hydrolyzed by PLDalpha
-
-
?
additional information
?
-
-
activation of phospholipase D by 8-Br-cAMP occurs through a pathway involving Src, Ras, and ERK in human endometrial stromal cells
-
-
?
additional information
?
-
-
lysophosphatidic acid increases phospholipase D activity in neutrophils
-
-
?
additional information
?
-
-
Munc-18-1 is a potent negative regulator of basal PLD activity. EGF stimulation abolishes this interaction
-
-
?
additional information
?
-
-
PLD is actived by the chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine. PLD2, but not PLD1, contributes to PLD activity mediated by N-formyl-methionyl-leucyl-phenylalanine. Extracellular signal-regulated kinase/PLD2 pathway contributes to N-formyl-methionyl-leucyl-phenylalanine-mediated oxidant production
-
-
?
additional information
?
-
-
PLD1 is required for normal organization of the actin cytoskeleton and for cell motility. PLD1 is a critical factor in the organization of the actin-based cytoskeleton, with regard to cell adhesion and migration
-
-
?
additional information
?
-
-
PLD1 plays a role in the induction of gene expression of Cox-2 and IL-8
-
-
?
additional information
?
-
-
priming is a critical regulator of PLD activation
-
-
?
additional information
?
-
-
protein casein kinase II stimulates basal phospholipase D (PLD1 and PLD2) activity as well as PMA-induced phospholipase D activation in human U87 astroglioma cells
-
-
?
additional information
?
-
protein casein kinase II stimulates basal phospholipase D (PLD1 and PLD2) activity as well as PMA-induced phospholipase D activation in human U87 astroglioma cells
-
-
?
additional information
?
-
protein casein kinase II stimulates basal phospholipase D (PLD1 and PLD2) activity as well as PMA-induced phospholipase D activation in human U87 astroglioma cells
-
-
?
additional information
?
-
-
stimulation of PLD activity and its mRNA expression by lipopolysaccharides might be required for IL-2 R expression and a sustained PKC dependent intracellular pH elevation but not for secretion of IL-2 or IL-4 in T cells
-
-
?
additional information
?
-
-
the enzyme plays an essential role in the swelling-induced vesicle cycling and in the activation of volume-sensitive anion channels
-
-
?
additional information
?
-
the PLD gene undergoes qualitative changes in transcription regulation during granulocytic differentiation
-
-
?
additional information
?
-
-
the PLD gene undergoes qualitative changes in transcription regulation during granulocytic differentiation
-
-
?
additional information
?
-
-
endocytotic trafficking of my-opioid receptor MOR1, delta-opioid receptor DOR and cannabinoid receptor isoform CB1 are mediated by an isoform PLD2 dependent pathway
-
-
?
additional information
?
-
-
enzyme is activated downstream of ERK1/2 kinases upon chemokine receptor CCR5 activation and plays a major role in promoting HIV-1 LTR transactivation and virus replication
-
-
?
additional information
?
-
-
enzyme isoform PLD1 and PLD2 are closely related with Bcl-2 expression together with phospholipase A2, but not with phosphatidic acid phosphohydrolase, during taxotere-induced apoptosis in SNU 484 cells
-
-
?
additional information
?
-
-
isoform PLD1 isassociated with cell polarity and directionality concomitantly with adhesion and F-actin polymerization in response to IL-8
-
-
?
additional information
?
-
isoform PLD1 isassociated with cell polarity and directionality concomitantly with adhesion and F-actin polymerization in response to IL-8
-
-
?
additional information
?
-
-
isoform PLD1 plays a crucial role in collagen type I production through mTOR signaling in dermal fibroblast
-
-
?
additional information
?
-
-
isoform PLD2 is associated with cell polarity and directionality concomitantly with adhesion and F-actin polymerization in response to IL-8
-
-
?
additional information
?
-
isoform PLD2 is associated with cell polarity and directionality concomitantly with adhesion and F-actin polymerization in response to IL-8
-
-
?
additional information
?
-
-
phospholipase D functions as a GTPase activating protein through the phox homology domain, which directly activates the GTPase domain of dynamin. Enzyme increases epidermal growth factor receptor endocytosis at physiological concentrations of epidermal growth factor
-
-
?
additional information
?
-
-
up-regulation of beta-defensin-2 by cell wall extract of Fusobacterium nucleatum or phorbol 12-myristate 13-acetate is mediated by phospholipase D
-
-
?
additional information
?
-
PLD product phosphatidic acid acts as a membrane anchor of Rac1. The C-terminal polybasic motif of Rac1 is responsible for direct interaction with phosphatidic acid. It is shown that phosphatidic acid induces dissociation of Rho-guanine nucleotide dissociation inhibitor from Rac1 and that phosphatidic acid-mediated Rac1 localization is important for integrin-mediated lamellipodia formation, cell spreading, and migration
-
-
?
additional information
?
-
PLD product phosphatidic acid acts as a membrane anchor of Rac1. The C-terminal polybasic motif of Rac1 is responsible for direct interaction with phosphatidic acid. It is shown that phosphatidic acid induces dissociation of Rho-guanine nucleotide dissociation inhibitor from Rac1 and that phosphatidic acid-mediated Rac1 localization is important for integrin-mediated lamellipodia formation, cell spreading, and migration
-
-
?
additional information
?
-
PLD product phosphatidic acid acts as a membrane anchor of Rac1. The C-terminal polybasic motif of Rac1 is responsible for direct interaction with phosphatidic acid. Phosphatidic acid induces dissociation of Rho-guanine nucleotide dissociation inhibitor from Rac1 and that phosphatidic acid-mediated Rac1 localization is important for integrin-mediated lamellipodia formation, cell spreading, and migration
-
-
?
additional information
?
-
PLD product phosphatidic acid acts as a membrane anchor of Rac1. The C-terminal polybasic motif of Rac1 is responsible for direct interaction with phosphatidic acid. Phosphatidic acid induces dissociation of Rho-guanine nucleotide dissociation inhibitor from Rac1 and that phosphatidic acid-mediated Rac1 localization is important for integrin-mediated lamellipodia formation, cell spreading, and migration
-
-
?
additional information
?
-
-
effects of active and inactive phospholipase D2 on signal transduction, adhesion, migration, invasion, and metastasis in EL4 lymphoma cells, overview
-
-
?
additional information
?
-
isozymes PLD1 and PLD2 share aboout 50% homology, but are regulated and localized differently in the cell. In vitro, PLD2 has a higher basal activity than PLD1, but overall cellular activity of PLD is low
-
-
?
additional information
?
-
-
isozymes PLD1 and PLD2 share aboout 50% homology, but are regulated and localized differently in the cell. In vitro, PLD2 has a higher basal activity than PLD1, but overall cellular activity of PLD is low
-
-
?
additional information
?
-
-
NF-kappaB and transcription factor Sp1 are essential transcriptional factors linking PLD to MMP-2 upregulation
-
-
?
additional information
?
-
PLD isozymes are cleaved by caspase 3, cleavage site determination, isozyme PLD2alpha contains two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S between the PLD domains, mutational analysis, overview
-
-
?
additional information
?
-
PLD isozymes are cleaved by caspase 3, cleavage site determination, isozyme PLD2alpha contains two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S between the PLD domains, mutational analysis, overview
-
-
?
additional information
?
-
-
PLD isozymes are cleaved by caspase 3, cleavage site determination, isozyme PLD2alpha contains two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S between the PLD domains, mutational analysis, overview
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-
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additional information
?
-
PLD isozymes are cleaved by caspase 3, cleavage site determination, isozymes PLD1beta and PLD2alpha contain each two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S and DFID631R between the PLD domains, respectively, mutational analysis, overview
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?
additional information
?
-
PLD isozymes are cleaved by caspase 3, cleavage site determination, isozymes PLD1beta and PLD2alpha contain each two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S and DFID631R between the PLD domains, respectively, mutational analysis, overview
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-
?
additional information
?
-
-
PLD isozymes are cleaved by caspase 3, cleavage site determination, isozymes PLD1beta and PLD2alpha contain each two consensus motifs for caspase 3 cleavage, DXXD or D/E, D/E, X, D, located in the loop region at DDVD545S and DFID631R between the PLD domains, respectively, mutational analysis, overview
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-
?
additional information
?
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-
PLD1 mediates the reactive oxygen species-induced increase in diacylglycerol, which facilitates PKD1 localization to the mitochondria and its activation. Diacylglycerol, to which PKD1 is recruited, is formed downstream of phospholipase D1 and is required for PKD1 localization in the mitochondria and well as activation under oxidative stress, overview. Role for PLD1-induced DAG as a competent second messenger at the mitochondria that relays ROS to PKD1-mediated mitochondria-to-nucleus signaling
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additional information
?
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enzyme evokes inflammatory reactions following injections into rabbit skin. Enzyme has a small hemolytic effect
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?
additional information
?
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enzyme evokes inflammatory reactions following injections into rabbit skin. Enzyme has a small hemolytic effect
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?
additional information
?
-
-
enzyme evokes inflammatory reactions following injections into rabbit skin. Enzyme has a small hemolytic effect
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?
additional information
?
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enzyme evokes inflammatory reactions following injections into rabbit skin. Treatment of Madin-Darby canine kidney cells results in appearance of cytoplasmic vacuolization, altered cellular spreading and cell-cell adhesion. Enzyme causes a high degree of hemolysis
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additional information
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enzyme evokes inflammatory reactions following injections into rabbit skin. Treatment of Madin-Darby canine kidney cells results in appearance of cytoplasmic vacuolization, altered cellular spreading and cell-cell adhesion. Enzyme causes a high degree of hemolysis
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additional information
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enzyme evokes inflammatory reactions following injections into rabbit skin. Treatment of Madin-Darby canine kidney cells results in appearance of cytoplasmic vacuolization, altered cellular spreading and cell-cell adhesion. Enzyme causes a high degree of hemolysis
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additional information
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enzyme shows dermonbecrotic properties. Enzyme causes massive inflammatory response in rabbit skin dermis, evokes platelet aggregation, increases vascular permeability, causes edema and death in mice
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additional information
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down-regulation of melanogenesis is mediated by phospholipase D2 but not by phospholipase D1 through turbiquitin proteasome-mediated degradation of tyrosinase. PLD2 may play an important role in regulating pigmentation in vivo
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?
additional information
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essential role for phospholipase D in activation of protein kinase C and degranulation in mast cells. Production of phosphatidic acid by PLD facilitates activation of protein kinase C and, in turn, degranulation, although additional PLD-dependent processes appear to be critical for antigen-mediated degranulation
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additional information
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mechanical stimuli activate mTOR (mammalian target of rapamycin) signaling through a phospholipase D-dependent increase in phosphatidic acid
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additional information
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PLD might be implicated in core protein-induced transformation
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?
additional information
?
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sphingosine significantly stimulates phospholipase D activity in mouse C2c12 myoblasts via phosphorylation to sphingosine 1-phosphate
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?
additional information
?
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survival signals generated by PLD attenuate expression of Egr-1 by activation of phosphatidylinositol 3-kinase signaling pathway and induction of PTEN by early growth response-1, which confers resistance to apoptosis
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?
additional information
?
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the PLD2 PX domain enables PLD1 to mediate signal transduction via ERK1/2 by providing a direct binding site for phosphatidylinositol 3,4,5-triphosphate and by activating PLD1
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?
additional information
?
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mechanical stimuli activate signaling by mTOR, i.e. mammalian target of rapamycin, in skeletal muscle through an enzyme-dependent increase in phosphatidic acid
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?
additional information
?
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-
PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor
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?
additional information
?
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-
PLD2 is regulated by phosphorylation-dephosphorylation, detailed overview
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?
additional information
?
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enzyme augments gonococcus invasion of cervical epithelia by interacting with Akt kinase in a hosphatidylinositol-(3,4,5)-trisphosphate-independent manner, resulting in subversion of normal cervical cell signaling
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additional information
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PLD activity is constitutive during pollen tube growth. Hypoosmotic stress stimulates PLD activity, hyperosmotic stress attenuates PLD activity
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additional information
?
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ability of PLD-generated phosphatidic acid to control actin polymerization and the reciprocal ability of actin to specifically modulate PIP2-dependent PLD, PLDbeta, activity through direct interaction
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?
additional information
?
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ability of PLD-generated phosphatidic acid to control actin polymerization and the reciprocal ability of actin to specifically modulate PIP2-dependent PLD, PLDbeta, activity through direct interaction
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?
additional information
?
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ability of PLD-generated phosphatidic acid to control actin polymerization and the reciprocal ability of actin to specifically modulate PIP2-dependent PLD, PLDbeta, activity through direct interaction
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?
additional information
?
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-
ability of PLD-generated phosphatidic acid to control actin polymerization and the reciprocal ability of actin to specifically modulate PIP2-dependent PLD, PLDbeta, activity through direct interaction
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?
additional information
?
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-
constitutive cation channel activity in ear artery myocytes is mediated by diacylglycerol which is generated by phosphatidylcholine-phospholipase D via phosphatidic acid which represents a novel activation pathway of cation channels in vascular myocytes
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?
additional information
?
-
-
PLD is activated by H2O2. The activation by H2O2 enhances phytoalexin biosynthesis in rice cells
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?
additional information
?
-
isoform PLDbeta1 stimulates abscisic acid signaling by activating SAP kinase, thus repressing GAmyb expression and inhibiting seed germination
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?
additional information
?
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isoform PLDbeta1 stimulates abscisic acid signaling by activating SAP kinase, thus repressing GAmyb expression and inhibiting seed germination
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?
additional information
?
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-
PldA contributes to the ability of Pseudomonas aeruginosa PAO1 to persist in a chronic pulmonary infection model in rats
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?
additional information
?
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5-[4-acridin-[9-ylamino]phenyl]-5-methyl-3-methylenedihydrofuran-2-one inhibits the formyl-Met-Leu-Phe-stimulated phospholipase D activity, mainly through the blockade of RhoA activation and degranulation
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-
?
additional information
?
-
-
alpha-adrenoreceptor activation increases phospholipase D activity
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?
additional information
?
-
-
dependency of activation of protein kinase D on phospholipase D, phospholipase D could be a key molecule that links Rho/protein kinase C signaling to diacylglycerol for protein kinase D activation
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?
additional information
?
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interaction of the PLD1 PX domain with phosphatidylinositol 3,4,5-trisphosphate and/or phosphatidic acid (or phosphatidylserine) may be an important factor in the spatiotemporal regulation and activation of PLD1
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?
additional information
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lysophosphatidic acid activates protein translation through the action of PLD1-generated phosphatidic acid on mTOR and the phosphoinositide 3-kinase/Akt pathway
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?
additional information
?
-
-
Munc-18-1 is a potent negative regulator of basal PLD activity. EGF stimulation abolishes this interaction
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?
additional information
?
-
-
phospholipase D elevates the level of MDM2 and suppresses DNA damage-induced increase in p53
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?
additional information
?
-
-
phospholipase D plays an important role in the regulation of beta-hexosaminidase release in actively sensitized rat peritoneal mast cells
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?
additional information
?
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PLD1 is a signaling node, in which integration of convergent signals occurs within discrete locales of the cellular membrane
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?
additional information
?
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-
PLD2 may be involved in early developmental processes of some neuronal progenitors
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?
additional information
?
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-
prolonged elevation of PLD activity is required for myogenic differentiation
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?
additional information
?
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the enzyme participates in myogenesis through phosphatidic acid- and phosphatidylinositol bisphosphate-dependent actin fiber formation
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?
additional information
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-
thyrotrophin-releasing hormone increases phospholipase D activity through stimulation of protein kinase C in GH3 cells
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?
additional information
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phospholipase D activates native TRPC3 cation channels after stimulation of G-protein-coupled type I glutamate receptors in the cerebellum. Small GTPases might be involved in the activation mechanism of TRPC3 in rat cerebellar Purkinje cells, overview
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?
additional information
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PLD catalyzes the hydrolysis of phospholipids resulting in the generation of phosphatidic acid and the release of the polar head group. The enzyme also catalyzes a transphosphatidylation reaction, in which the aliphatic chain of the primary alcohol is transferred to the phosphatidyl moiety of the phosphatidic acid product
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additional information
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PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, 1-butanol serves as acceptor in the transphosphatidylation reaction, while 2-butanol does not. PLD-catalysed PtdOH formation may be necessary for EGF-induced macropinocytosis
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?
additional information
?
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-
the Arf-GTPase-activating protein Gsc1p is essential for sporulation and positively regulates the phospholipase D Spo14p
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?
additional information
?
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silymarin secretion and its elicitation by methyl jasmonate in cell cultures of Silybum marianum is mediated by phospholipase D-phosphatidic acid, overview
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?
additional information
?
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-
expression of LePLDbeta1 is increased upon treatment with xylanase. Possible involvement of LePLDbeta1 in plant defense response
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?
additional information
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interaction of PLDalpha C2 domain with synthetic unilamellar vesicles shows maximum affinity towards phosphatidic acid, and virtually no binding with phosphatidylcholine. Electrostatic, rather than a hydrophobic mode of interaction between C2 domain and the phospholipid vesicles. The binding towards phosphoinositides is reduced with increasing degree of phosphorylation
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(1S,2S)-N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-2-phenylcyclopropanecarboxamide
-
(1S,2S)-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
-
(1S,2S)-N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
-
(1S,2S)-N-[(1S)-2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
-
(1S,2S)-N-[(1S)-2-[4-(6-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
-
(1S,2S)-N-[(2S)-1-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]propan-2-yl]-2-phenylcyclopropanecarboxamide
-
-
(1S,2S)-N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-2-phenylcyclopropanecarboxamide
-
(1S,2S)-N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-2-phenylcyclopropanecarboxamide
-
(1S,2S)-N-[2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-2-phenylcyclopropanecarboxamide
-
1,2-bis(2-aminophenoxy)-ethane-N,N,N',N'-tetraacetic acid tetrakis(acetoxymethyl) ester
-
i.e. BAPTA-AM, chelator of intracellular free calcium, application results in reduction of extracellular pH-induced enzyme activity
1-(3,4-difluorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
1-(3-bromophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
1-(3-chlorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
1-(3-fluorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
1-(4-chlorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
1-(4-fluorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
1-benzyl-4-carbonoimidoyl-N-(3,4-difluorophenyl)piperidin-4-amine
-
-
1-benzyl-4-carbonoimidoyl-N-(3-chlorophenyl)piperidin-4-amine
-
-
1-benzyl-4-carbonoimidoyl-N-(3-fluorophenyl)piperidin-4-amine
-
-
1-benzyl-4-carbonoimidoyl-N-(4-chlorophenyl)piperidin-4-amine
-
-
1-benzyl-4-carbonoimidoyl-N-(4-fluorophenyl)piperidin-4-amine
-
-
1-benzyl-4-[(3,4-difluorophenyl)amino]piperidine-4-carboxamide
-
-
1-benzyl-4-[(3-bromophenyl)amino]piperidine-4-carboxamide
-
-
1-benzyl-4-[(3-chlorophenyl)amino]piperidine-4-carboxamide
-
-
1-benzyl-4-[(3-fluorophenyl)amino]piperidine-4-carboxamide
-
-
1-benzyl-4-[(4-chlorophenyl)amino]piperidine-4-carboxamide
-
-
1-benzyl-4-[(4-fluorophenyl)amino]piperidine-4-carboxamide
-
-
1-benzyl-N-(4-bromophenyl)-4-carbonoimidoylpiperidin-4-amine
-
-
1-benzylpiperidin-4-one
-
-
2'-isopropyl-4'-(trimethylammoniumchloride)-5'-methylphenyl piperidine-1-carboxylate:
-
75% noncompetitive inhibition at 25 mM; choline analog
3,4-difluoro-N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]benzamide
-
3,4-difluoro-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
-
3,4-difluoro-N-[2-[4-(6-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
-
3-methyl-N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]benzamide
-
30kDA protein factor from bovine brain cytosol
-
inhibition due to interaction with phosphatidylinositol 4,5-biphosphate
-
4-(4-(2-(3-methoxyphenyl)benzo[b]thiophen-3-yl)phenoxy)-N,N-dimethylethan-1-amine
4-amino-3-methoxy-N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]benzamide
-
4-chloro-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
-
4-chloro-N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
-
4-chloro-N-[(1S)-2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
-
4-chloro-N-[2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
-
4-chloro-N-[2-[4-(6-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
-
4-fluoro-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
-
4-fluoro-N-[(1S)-2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
-
4-fluoro-N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]benzamide
-
-
4-fluoro-N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]benzamide
-
-
4-fluoro-N-[2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
-
5,5'-dimethyl-1,2-bis-(2-aminophenoxy)-ethane-N,N,N',N'-tetraacetic acid
-
partial
5-fluoro-N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-1H-indole-2-carboxamide
-
-
5-fluoro-N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-1H-indole-2-carboxamide
-
-
5-[4-acridin-[9-ylamino]phenyl]-5-methyl-3-methylenedihydrofuran-2-one
-
inhibits the formyl-Met-Leu-Phe-stimulated phospholipase D activity, mainly through the blockade of RhoA activation and degranulation
6-fluoro-N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]naphthalene-2-carboxamide
-
8-(2-aminoethyl)-1-(3,4-difluorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
8-(2-aminoethyl)-1-(3-chlorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
8-(2-aminoethyl)-1-(3-fluorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
8-(2-aminoethyl)-1-(4-bromophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
8-(2-aminoethyl)-1-(4-chlorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
8-(2-aminoethyl)-1-(4-fluorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
8-benzyl-1-(3,4-difluorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
8-benzyl-1-(3-bromophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
8-benzyl-1-(3-chlorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
8-benzyl-1-(3-fluorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
8-benzyl-1-(4-chlorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
8-benzyl-1-(4-fluorophenyl)-1,3,8-triazaspiro[4.5]decan-4-one
-
-
Ag+
-
5 mM, 77% inhibition
Ag2+
-
in the presence of Triton X-100
calphostin C
-
the lower affinity first generation inhibitor does not distinguish between isozymes PLD1 and 2
Cd2+
-
slight stimulation
ceramide
-
inhibits PLD at the catalytic subunit by competing with phosphatidylinositol-4,5-bisphosphate. Ceramide levels are increased coincidentally with reduced PLD activity in senescent cells. Treatment of cells with ceramide results in a dose-dependent decrease in PLD activity and diacylglycerol accumulation
cetyltrimethylammonium bromide
-
-
CTAB
-
inhibitory at concentrations at or above that of 1 lysophosphatidylcholine
curcumin
-
the lower affinity first generation inhibitor does not distinguish between isozymes PLD1 and 2
deoxycholic acid
-
0.45%, 26% residual activity
dithiobis-(2-nitrobenzoic acid)
-
-
FeSO4
-
2 mM, 78% of initial activity
forskolin
inhibits the activating effect of thrombin. Translocation to the plasma membrane of PLD1, but not PLD2, is inhibited
glucose
-
suppression of enzyme activity in etiolated seedling
H2O2
-
exposure of cells to H2O2 leads to transient increase in activity followed by 90% decrease
Inositol
-
at 0.075 mM in culture medium,reduction of enzyme activity by 30-40%
lysophosphatidylcholine
-
-
N-(2-(1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)-2-naphthamide
-
an isoform-selective small molecule phospholipase D2 inhibitor
N-lauroylethanolamine
-
mediates differential effects on cellular organization and seedling growth, in part through the differential modulation of specific isoforms of phospholipase D. 1-Butanol induces more pronounced modifications in cytoskeletal organization, seedling growth, and cell division at concentrations severalfold higher than N-lauroylethanolamine
N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]naphthalene-2-carboxamide
-
N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
-
N-[(1S)-2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-3,4-difluorobenzamide
-
N-[(1S)-2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-4-chlorobenzamide
-
N-[(1S)-2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
-
N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-3,4-difluorobenzamide
-
N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-4-fluorobenzamide
-
N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
-
N-[(1S)-2-[4-(6-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
-
N-[(2S)-1-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]propan-2-yl]naphthalene-2-carboxamide
-
-
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-1,2,3,4-tetrahydronaphthalene-2-carboxamide
-
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-1-benzothiophene-2-carboxamide
-
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-3-phenylprop-2-ynamide
-
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]naphthalene-2-carboxamide
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]quinoline-3-carboxamide
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]quinoxaline-2-carboxamide
-
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
-
-
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
-
-
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
-
-
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
-
-
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
-
-
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
-
-
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
-
-
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
-
-
N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
-
-
N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-2-carboxamide
-
-
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
-
-
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
-
-
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
-
-
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
-
-
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
-
-
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
-
-
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
-
-
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
-
-
N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
-
-
N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
-
-
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-3,4-dihydronaphthalene-2-carboxamide
-
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-3-phenylprop-2-ynamide
-
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]naphthalene-2-carboxamide
-
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]quinoline-3-carboxamide
-
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]quinoline-6-carboxamide
-
N-[2-[4-(4-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-fluorobenzamide
-
N-[2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-chlorobenzamide
-
N-[2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-fluorobenzamide
-
N-[2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-methylbenzamide
-
N-[2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]naphthalene-2-carboxamide
-
Ni2+
-
2.5 mM, complete loss of both hydrolytic activity and transphosphatidylation
phosphatidylethanolamine
-
-
PMSF
-
5 mM, 60% inhibition
polyoxyethylene-4-lauryl ether
-
0.45%, 21% residual activity
polyoxylethylene-4-laurylether
-
relative activity: 3%
-
prostaglandin E1
inhibits the activating effect of thrombin; inhibits the activating effect of thrombin. Translocation to the plasma membrane of PLD1 is inhibited but only at high concentration
protein kinase A
inhibits the activating effect of thrombin. Translocation to the plasma membrane of PLD1, but not PLD2, is inhibited
-
Proteinkinase C
-
phosphorylated and inhibited the enzyme in vitro
-
sodium dodecylsulfate
-
0.45%, 3% residual activity
sphinganine
-
does not alter basal PLD2 activity, but inhibits PLD2 activation induced by [D-Ala2,Me Phe4,Glyol5]enkephalin and beta-endorphin, overview
Triton CF-54/Tween 80
-
-
-
tubulin
-
increase in local membrane monomeric tubulin concentration inhibits PLD2 activity by direct interaction, carbachol increases the association between PLD2 with tubulin
-
1-butanol
-
-
1-butanol
-
mediates differential effects on cellular organization and seedling growth, in part through the differential modulation of specific isoforms of phospholipase D. 1-Butanol induces more pronounced modifications in cytoskeletal organization, seedling growth, and cell division at concentrations severalfold higher than N-lauroylethanolamine
1-butanol
inhibitor of enzyme. Pretreatment with 1-butanol suppresses Co2+-induced COX-2 expression and prostaglandin E2 formation
1-butanol
-
inhibitor of enzyme. Suppression of enzyme activity results in increased phosphorylation of Smad2 and Smad3 on sites that get phosphorylated by the TGFbeta receptor and positively regulate TGFbeta signaling and in suppression of phosphorylation on sites that are phosphorylated by MAP kinase and negatively regulate TGFbeta signaling. Suppression of enzyme activy also leads to increased expression of the cyclin-dependent kinase inhibitors p21Cip1 and p27Kip1
1-butanol
-
inhibition of enzyme, leading to block of beta-defensin-2 up-regulation by cell wall extract of Fusobacterium nucleatum or phorbol 12-myristate 13-acetate
1-butanol
-
1-butanol inhibits PLD2 and is potent in cancelling ERK1/2 activation
1-butanol
-
treatment of human neutrophils to butan-1-ol significantly dampenes functional responses such as degranualtion, chemotaxis, and oxidative burst
1-butanol
-
inhibits the mechanically induced increase in phosphatidic acid in skeletal muscle and mechanical activation of signaling by mTOR, i.e. mammalian target of rapamycin
1-butanol
-
1-butanol inhibits PLD2 and is potent in cancelling ERK1/2 activation
1-butanol
-
inhibits PLD hydrolytic activity
1-butanol
-
selectively inhibits production of phosphatidic acid
1-butanol
-
does not causes direct inhibition of TRPC3 channels, but causes blocking of phospholipase D which interferes with retrograde signaling, overview. Neither voltage-gated Ca2+-channels nor Ca2+-activated Cl channels are affected by 1-butanol
2-mercaptoethanol
-
-
2-mercaptoethanol
-
5 mM, 25% inhibition
4-(4-(2-(3-methoxyphenyl)benzo[b]thiophen-3-yl)phenoxy)-N,N-dimethylethan-1-amine
-
-
4-(4-(2-(3-methoxyphenyl)benzo[b]thiophen-3-yl)phenoxy)-N,N-dimethylethan-1-amine
-
-
Al3+
-
stimulates in the absence of Triton X-100
Al3+
-
inhibits the phosphatidylinositol-4,5-bisphosphate-dependent isozyme
Al3+
-
2.5 mM, complete loss of both hydrolytic activity and transphosphatidylation
Al3+
-
activation of transphosphatidylation
alpha-synuclein
-
binds to PLD and inhibits its activity, it also markedly depressed the dopamine-induced Na+ current response in vivo
-
Ba2+
-
complete inhibition
Ba2+
-
1 mM, 15-25% inhibition
Ba2+
-
complete inhibition
Ca2+
inhibitory above 1 mM
Ca2+
substantial reduction of stability due to salt-induced aggregation
Ca2+
-
inhibitory at 5 mM and 10 mM, substrate dioleoylphosphatidylethanolamine, stimulation at 2.5 mM, substrate dioleoylphosphatidylcholine
Cetylpyridinium chloride
-
-
Cetylpyridinium chloride
-
-
Co2+
-
1 mM, 50-60% inhibition
Co2+
-
2.5 mM, complete loss of both hydrolytic activity and transphosphatidylation
Co2+
-
complete inhibition
Co2+
-
slight stimulation
Cu2+
-
complete inhibition
Cu2+
-
10 mM, complete inhibition
Cu2+
-
2.5 mM, complete loss of both hydrolytic activity and transphosphatidylation
desketoraloxifene
-
-
dithiothreitol
-
-
dithiothreitol
-
5 mM, 20% inhibition
EDTA
-
1.5 mM, 30% loss of activity
EDTA
-
complete inhibition
EDTA
-
5 mM, 94% inhibition
EDTA
-
complete inhibition at 2 mM
EGTA
-
96% inhibition at 5 mM
ethanol
-
suppression of PLD-mediated phosphatidic acid formation by alcohol alleviated the growth-promoting effect of PLDepsilon
ethanol
-
inhibition of enzyme, leading to block of beta-defensin-2 up-regulation by cell wall extract of Fusobacterium nucleatum or phorbol 12-myristate 13-acetate
ethanol
inhibits PLD and reduces surface effects, e.g. the increase of PLD mRNA and activity, osteocalcin and osteoprotegerin, and protein kinase C and alkaline phosphatase specific activities, as well as the decrease of cell number
Fe2+
-
10 mM, 91% of initial activity
Fe2+
-
stimulates in the absence of Triton X-100
Fe2+
-
10 mM, complete inhibition
Fe3+
-
10 mM, complete loss of activity
Fe3+
-
stimulates in the absence of Triton X-100
Fe3+
-
complete inhibition at 5 mM
Fe3+
-
2.5 mM, complete loss of both hydrolytic activity and transphosphatidylation
Fe3+
-
5 mM, 44% inhibition
halopemide
-
-
halopemide
-
the higher affinity second generation inhibitor does not distinguish between isozymes PLD1 and 2
Hg2+
-
in the presence of Triton X-100
Hg2+
-
10 mM, complete inhibition
Mg2+
-
10 mM, 78% of initial activity
Mg2+
-
2.5 mM, inhibitory to both hydrolytic activity and transphosphatidylation
Mg2+
-
stimulates in the absence of Triton X-100
Mg2+
-
slight stimulation
Mn2+
-
stimulates in the absence of Triton X-100
Mn2+
-
1 mM, 45-55% inhibition
Mn2+
-
2.5 mM, complete loss of both hydrolytic activity and transphosphatidylation
Mn2+
-
substrate specific
Mn2+
-
slight stimulation
Munc-18-1
-
2 nM is required for 50% inhibition, inhibits phospholipase D activity by direct interaction in an epidermal growth factor-reversible manner
-
Munc-18-1
-
inhibits phospholipase D activity by direct interaction in an epidermal growth factor-reversible manner
-
n-butanol
-
-
n-butanol
PLD inhibition disrupts the actin cytoskeleton in tobacco pollen tubes; PLD inhibition disrupts the actin cytoskeleton in tobacco pollen tubes; PLD inhibition disrupts the actin cytoskeleton in tobacco pollen tubes
n-butanol
n-butanol completely blocks the migration of NBT-II cells on collagen-coated substrates and disturbes the characteristic localization of actin along edge of lamellipodia
n-butanol
-
inhibits phosphatidic acid production by PLD, prevents silymarin elicitation by methyljasmonate or mastoparan, and also impedes its release in non-elicited cultures. Exogenous addition of phosphatidic acid reverses the inhibitory action of nBuOH, both in control and methyljasmonate-treated cultures
n-butanol
-
inhibition of PLD leads to the partial inhibition of the photosynthetic phosphoenolpyruvate carboxylase, C4-PEPC, phosphorylation, overview
N-ethylmaleimide
-
-
N-laurylsarcosine
-
0.45%, 0% residual activity
N-laurylsarcosine
-
75% inhibition at 1.5%
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]naphthalene-2-carboxamide
-
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]naphthalene-2-carboxamide
-
-
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]quinoline-3-carboxamide
-
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]quinoline-3-carboxamide
-
-
neomycin
inhibitory in native myocardium, where phosphatidylinositol-4,5-bisphosphate restores, not inhibitory with partially purified enzyme; inhibits activity in human atrial myocardium, but has no effect on the activity of partially solubilized enzyme
neomycin
-
abolishes activation by GTP or ATP
neomycin
-
inhibits the mechanically induced increase in phosphatidic acid in skeletal muscle
oleic acid
-
-
p-chloromercuribenzoate
-
complete inhibition
p-chloromercuribenzoate
-
complete inhibition
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
complete inhibition
resveratrol
-
a phytoalexin with antiinflammatory activity in C5 anaphylatoxin-stimulated primary neutrophils, blocks PLD activity and membrane recruitment
resveratrol
-
a phytoalexin with antiinflammatory activity in C5 anaphylatoxin-stimulated primary neutrophils and in a mouse model of acute peritonitis, blocks PLD activity and membrane recruitment
SDS
-
-
SDS
-
inhibitory at concentrations at or above that of 1 lysophosphatidylcholine
SDS
-
5 mM, 50% inhibition
SDS
-
relative activity: 41%
SDS
-
complete inhibition at 1.5%
Sn2+
-
stimulates in the absence of Triton X-100
Sn2+
-
complete inhibition
Triton X-100
-
substrate-dependent inhibition
Triton X-100
complete loss of activity and prohibition of any stimulation by phosphatidylinositol 4,5-bisphosphate
Triton X-100
-
inhibitory at concentrations at or above that of 1 lysophosphatidylcholine
Triton X-100
-
activating up to 0.4%, inhibitory above
Tween 20
-
-
Tween 20
-
0.45%, 3% residual activity
Tween 80
-
-
Tween 80
-
0.45%, 5% residual activity
Zn2+
-
10 mM, 47% of initial activity
Zn2+
-
10 mM, complete inhibition
Zn2+
-
1 mM, 45% inhibition
Zn2+
-
2.5 mM, complete loss of both hydrolytic activity and transphosphatidylation
additional information
-
either intracellular injection of alpha-synuclein or extracellular application of 1-butanol, inhibitors of PLD, significantly depress the dopamine-induced Na+ current response in neurons
-
additional information
-
white and red light exposure inhibit enzyme activity in etiolated seedling, far-red light eliminates red-light-induced decrease in activity
-
additional information
-
enzyme completely loses activity upon dialysis
-
additional information
-
phospholipase D2 immobilized covalently on CNBr-activated Sepharose expresses 10% of the activity of the soluble enzyme, the enzyme immobilized by binding on to anti-PLD2 IgG-Sepharose show 38% of the activity of the soluble enzyme
-
additional information
-
no inhibiton by EDTA
-
additional information
-
inhibition of PLD significantly reduces the cell motility of CCL39 cells
-
additional information
-
PLD activity is decreased in the presence of components required for the monooxygenase (MMO) activity (reducing system), including 100% phosphatidylcholine membranes, NADPH-cytochrome P450 reductase and NADPH. Lysophosphatidylserine recoveres the PLD activity in a concentration-dependent manner
-
additional information
-
the inhibition of PLD-mediated phosphatidic acid production by n-butanol selectively blocks the secretion of von Willebrand factor, but not that of tPA
-
additional information
inhibition of the PLD product formation phosphatidic acid by adding 1-butanol significantly decreases cell spreading; inhibition of the PLD product formation phosphatidic acid by adding 1-butanol significantly decreases cell spreading
-
additional information
inhibition of the PLD product formation phosphatidic acid by adding 1-butanol significantly decreases cell spreading; inhibition of the PLD product formation phosphatidic acid by adding 1-butanol significantly decreases cell spreading
-
additional information
isozyme PLD2alpha contains functional caspase 3 cleavage sites; isozymes PLD1beta and PLD2alpha contain functional caspase 3 cleavage sites and identify the critical aspartate residues within PLD1beta that affect its activation by phorbol esters and attenuate phosphatidylcholine hydrolysis during apoptosis
-
additional information
isozyme PLD2alpha contains functional caspase 3 cleavage sites; isozymes PLD1beta and PLD2alpha contain functional caspase 3 cleavage sites and identify the critical aspartate residues within PLD1beta that affect its activation by phorbol esters and attenuate phosphatidylcholine hydrolysis during apoptosis
-
additional information
-
isozyme PLD2alpha contains functional caspase 3 cleavage sites; isozymes PLD1beta and PLD2alpha contain functional caspase 3 cleavage sites and identify the critical aspartate residues within PLD1beta that affect its activation by phorbol esters and attenuate phosphatidylcholine hydrolysis during apoptosis
-
additional information
-
alpha-synuclein, a small cytosolic protein, does not inhibit phospholipase D
-
additional information
-
no inhibition by 2-butanol
-
additional information
inhibition of PLD reduces the effects of surface microstructure/energy on protein kinase C, suggesting that PLD mediates the stimulatory effect of microstructured/high-energy surfaces via PKC-dependent signaling
-
additional information
-
inhibition of PLD reduces the effects of surface microstructure/energy on protein kinase C, suggesting that PLD mediates the stimulatory effect of microstructured/high-energy surfaces via PKC-dependent signaling
-
additional information
-
inhibition of PLD1 by pharmacological inhibitors blocks PKD1 activation under oxidative stress
-
additional information
-
downregulation of Arf1 and cytohesin-1 by siRNA leads to reduced PLD transphosphatidylation activity, overview
-
additional information
-
design, synthesis, and biological evaluation of halogenated N-(2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)benzamides as inhibitors of PLD2 or dual PLD1/PLD2 inhibitors, overview
-
additional information
-
overview on inhibitory compounds and mechanism
-
additional information
-
no inhibition by 2-butanol
-
additional information
-
PLD activity is modified by microtubule dynamics
-
additional information
no inhibition by tert-butanol; no inhibition by tert-butanol; no inhibition by tert-butanol
-
additional information
no inhibition by tert-butanol; no inhibition by tert-butanol; no inhibition by tert-butanol
-
additional information
no inhibition by tert-butanol; no inhibition by tert-butanol; no inhibition by tert-butanol
-
additional information
-
no inhibition by tert-butanol; no inhibition by tert-butanol; no inhibition by tert-butanol
-
additional information
-
the silica-induced phospholipase D activity is partially attenuated by the pretreatment with U73122, genistein, PD 98056 and mepacrine
-
additional information
-
PLD activity is decreased in the presence of components required for the monooxygenase (MMO) activity (reducing system), including 100% phosphatidylcholine membranes, NADPH-cytochrome P450 reductase and NADPH. Lysophosphatidylserine recoveres the PLD activity in a concentration-dependent manner
-
additional information
n-butanol completely blocks the migration of NBT-II cells on collagen-coated substrates and disturbes the characteristic localization of actin along edge of lamellipodia
-
additional information
n-butanol completely blocks the migration of NBT-II cells on collagen-coated substrates and disturbes the characteristic localization of actin along edge of lamellipodia
-
additional information
-
dominant negative Rac1, N17Rac1, completely inhibits PLD activation by EGF, but not by PDGF. Dominant-negative RalA and Ras also abolish PLD activation by EGF
-
additional information
-
treatment with iso-, sec- or tert-butanol has no effect on silymarin production
-
additional information
-
phosphatidic acid by itself has no effect on PEPC phosphorylation, but when combined with n-butanol, phosphatidic acid reverses the inhibitory effect of this compound
-
additional information
-
no inhibitory effect of metal ions
-
additional information
-
in subsidiary cell mother cells treated with butanol-1, which blocks phosphatidic acid production via PLDs, Actin filament-patch formation laterally to the inducing guard mother cell and the subsequent asymmetric division are inhibited. In these subsidiary cell mother cells, cell division plane determination, as expressed by MT preprophase band formation, is not disturbed. Exogenously applied phosphatidic acid partially relieves the butanol-1 effects on subsidiary cell mother cells. In contrast to subsidiary cell mother cells, butanol-1 does not affect the symmetric guard cell mother cell division
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(D-Ala2, methyl-Phe4, Glyol5)enkephalin
-
treatment of cells co-expressing isoform PLD2 and my-opioid receptor MOR1 leads to increase in PLD2 activity and an induction of receptor endocytosis
1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
-
500fold stimulation is observed upon incorporation of 10 mol 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate (POPA) into 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) vesicles in the presence of Ca2+ ions. Differential scanning calorimetry shows that the POPA-specific activation correlates with the phase behavior of the POPC/POPA vesicles in the presence of Ca2+ ions
24R,25(OH)2D3
PLD is activated by 24R,25(OH)2D3 in a surface-dependent manner
3-(3,4-dichlorophenyl)-1,1-dimethylurea
-
inhibitor of electron transport in chloroplast, stimulation of enzyme activity in green seedling
4beta-phorbol-12,13-didecanoate
-
i.e. 4betaPDD, a phorbol ester
abscisic acid
rapid induction of isoform PLDbeta1, enzyme stimulates abscisic acid signaling by activating SAP kinase, thus repressing GAmyb expression and inhibiting seed germination
ADP
-
at 1 mM, 200% of control activity
ADP-ribosylation factor
-
ADP-ribosylation factor 1
-
i.e. Arf1, a small G protein, stimulates PLD hydrolytic activity
-
ADP-ribosylation factor 6
-
i.e. Arf6, a small G protein, stimulates PLD hydrolytic activity
-
amyloid beta peptide
-
residues 1-42, i.e. Abeta1-42, a formyl-peptid-receptor-like 1 agonist, activates 3-4fold in microglia and astrocytes, respectively, at 0.001 mM. Endocytosis of Abeta1-42 in glial cells is PLD-dependent
-
arachidonic acid
-
only in presence of Mg2+
Arf proteins
-
activate isozyme PLD1 and a truncated form of PLD2
-
Arf-1
-
the catalytic activator stimulates PLD1 by enhancing the catalytic constant kcat. Full-length enzyme and N-terminally truncated enzyme are strongly activated by Arf-1-GTPgammaS
-
Arf4 protein
-
in 293T cells overexpressing EGFR, Arf4 associates with the cytoplasmic region of EGFR and directly regulates PLD2 activation, but not PLD1 activation
-
benzothiadiazole
-
rapid activation of isoforms PLDalpha, PLDbeta/gamma, PLDdelta. Strongest response for PLDbeta/gamma
beta-endorphin
-
opioid receptor-mediated activation
butanol
-
transphosphatidylation increases activity
cAMP
-
at 1 mM, 273% of control activity
Carbachol
-
PLD1 is activated by cholinergic agonists. Atropine inhibits this PLD1 activation
cholera toxin
-
stimulation of enzyme
-
Collagen
-
adhesion of myeloid-macrophage cell lines to fibronectin is accompanied by marked stimulation of enzyme activity
CpG oligodeoxynucleotides
-
induce PLD activation, increase PLD activity, PLD-dependent reactive oxygen intermediate production, PLD-dependent phagolysosome maturation, and PLD-dependent intracellular mycobacterial killing in type II alveolar epithelial cells
-
CtBP1/BARS
-
a short splice variant of the CtBP1 gene and a physiological activator of PLD1 required in agonist-induced macropinocytosis. Stimulation of cells by serum or EGF results in the association of CtBP1/BARS with PLD1, which is specifically blocked by 1-butanol. CtBP1/BARS acts synergistically with ARF1 protein in activation of PLD, dependent on GTPgammaS or GTP but not on GDP, overview
-
Cu2+
-
very rapid induction of enzyme accompanied by accumulation of both phosphatidic acid and phosphatidylbutanol. Highest activity 2 h after copper addition, decrease thereafter. Enhanced enzyme gene expression contributes to the increase in activity
diacylglycerol
-
interaction of phospholipase D with the lipidic activator at the air-water interface
formylmethionyl-leucyl-proline
-
i.e. fMLF, activates 4fold in microglia and astrocytes, respectively, at 0.001 mM, the activation is inhibited by WRW4, a formyl-peptid-receptor-like 1 antagonist
Fusobacterium nucleatum cell wall extract
-
stimulation
-
GDP
-
at 1 mM, 312% of control activity
Grb2 protein
-
directly interacts with and activates PLD2 through its SH2 domain, which in turn activates ERK1/2, upon EGF stimulation
-
GTP-binding proteins
-
the PLD1 isoform can be activated by GTP-binding proteins, PKC, and tyrosine kinases. Synergistic activation of PLD1 with combinations of ARF and Rho, Rho and PKC, and ARF and PKC. Isozyme PLD2 remains unaffected by these activators
-
GTPases
PLD1 is activated by PKCalpha and GTPases such as RhoA, RacI, Cdc42, and ADP-ribosylation factor, ARF, whereas PLD2 is not
-
guanosine 5'-3-O-(thio)triphosphate
Hg2+
-
mercury chloride, and methylmercury, activates PLD, the stimulation is regulated by Ca2+ and calmodulin, mechanism, overview. Calcium chelating agents and calcium depletion, e.g. by EGTA, calmodulin inhibitors, e.g. calmidazolium chloride and trifluoperazine, and L-type calcium channel blockers nifedipine, nimodipine, and diltiazem attenuate the stimulation of PLD by mercury, overview
histamine
-
evokes a transient increase in intraendothelial Ca2+-concentration and enhancey PLD activity significantly. A significant fraction of PLD1 translocates to the plasma membrane after 5 min of histamine stimulation of HUVECs
iodoacetic acid
rapid induction of isoform PLDbeta1
L-ascorbic acid
-
activates the lipid signaling enzyme PLD at pharmacological doses, 5 mM, in the bovine lung microvascular endothelial cells, with modulation of PLD activation by phospholipase A2, PLA2. Antioxidants attenuate vitamin C-induced PLA2 , e.g. N-acetylcysteine, propyl gallate, or enzyme catalase activation
light
-
light-dependent increase in PLD activity
-
lysophosphatidic acid
-
-
methyl jasmonate
-
rapid activation of isoforms PLDalpha, PLDbeta/gamma, PLDdelta
methyl {(1S,2S)-3-oxo-2-[(2Z)-pent-2-en-1-yl]cyclopentyl}acetate
-
increases PLD activity
my-opioid receptor variant MOR1D
-
activation of isoform PLD2
-
phenylephrine
-
increases phosphatidylbutanol formation in CCL39 cells
phorbol 12-myristate 13-acetate
Phorbol esters
activate isozyme PLD1beta
phorbol-12-myristate-13-acetate
-
induces PLD2 activation
phosphatidylinositol 3,4,5-triphosphate
phosphatidylinositol 3,4,5-trisphosphate
phosphatidylinositol 4,5-bisphosphate
phosphatidylinositol phosphate
phosphatidylinositol-3,4,5-trisphosphate
phosphatidylinositol-3,4-diphosphate
-
very effective activator
phosphatidylinositol-3,5-diphosphate
-
effective activator
phosphatidylinositol-3-phosphate
-
effective activator
phosphatidylinositol-4,5-bisphosphate
phosphatidylinositol-4,5-diphosphate
-
very effective activator
phosphoinositide-4,5-bisphosphate
-
i.e. PIP2, phosphoinositides, particularly PIP2, another key regulator of PLD activation are required by PLDbeta, PLDgamma, PLDdelta, and PLDzeta for activity
polyethylene-4-laurylether
-
propanolol
-
only hydrolase activity
prostaglandin E1
causes a modest elevation of PLD activity in resting platelets. prostaglandin E1-induced PLD activity is increased by 25% in the presence of Ca2+. Maximal activity at 5 micromol prostaglandin E1
protein kinase Calpha
-
activation of PLD1 involves N- and C-terminal PLD domains
-
R(+)-hydroxy(dipropylamino)tetralin hydrobromide
-
i.e. (+)7-OH DPAT, stimulates D3 receptor-mediated PLD activity
Rheb
-
Rheb binds and activates PLD1 in vitro in a GTP-dependent manner. Overexpression of the small GTPase Rheb activates PLD1 in cells by about 2.5fold in the absence of mitogenic stimulation, and the knockdown of Rheb impairs serum stimulation of PLD activation, overview
-
Rho family G-proteins
-
RhoB or C, but not RhoA, activate PLD. The activation is irreversibly blocked by Clostridium difficile toxin B, an inhibitor for all Rho family G-proteins, or Clostridium botulinum C3 exoenzyme, a specific blocker for RhoA-C, and also by the GAP domain of p50RhoGAP, kinetics, overview
-
Rho protein
-
small G proteins of the Rho and Arf families activate phospholipase D1. Small GTPases might be involved in the activation mechanism of TRPC3 in rat cerebellar Purkinje cells. Rho GTPases can activate phospholipase D1 through two mechanisms: direct binding to phospholipase D1 or activation of phosphatidylinositol-4,5-kinase, which triggers phosphatidylinositol-4,5-bisphosphate production, an essential cofactor for phospholipase D1 activity
-
RhoA protein
-
recombinant D3 dopamine receptor, D2S receptor, signals to activation of phospholipase D through a complex with RhoA in HEK-293 cells
-
sodium dodecylsulfate
-
in molar ratio phosphatidylcholine to SDS 4.32:1
sphingosine
-
only hydrolase activity
taxotere
-
increase in enzyme activity. Overexpression of enzyme isozymes results in inhibition of taxotere-induced apoptotic cell death, accompanied by up-regulated expression of Bcl-2 and inhibited taxotere-induced activation of procaspase 3
thyrotropin
-
PLD-1, stimulation up to 2.3fold, accompanied by translocation of ADP-ribosylation factor and RhoA to the membrane fraction
-
TNF-alpha
stimulation in a dose-dependent manner
-
Tween 80
-
activates 2fold at 1.5%
UDP
-
extracellular application of nucleotides stimulates enzyme activity and shows a sustained activation of extracellular signal-regulated kinase. Effects on enzyme and extracellular signal-regulated kinase are not additive and not coupled to DNA synthesis. Best effects are with ATP and UTP at 0.01 mM and above
UTP
-
extracellular application of nucleotides stimulates enzyme activity and shows a sustained activation of extracellular signal-regulated kinase. Effects on enzyme and extracellular signal-regulated kinase are not additive and not coupled to DNA synthesis. Best effects are with ATP and UTP at 0.01 mM and above
Vasopressin
-
a PLD agonist
vitamin C
-
at pharmacological doses activates PLD in the lung microvascular endothelial cells through oxidative stress and activation of mitogen-activated protein kinase
[D-Ala2,Me Phe4,Glyol5]enkephalin
-
opioid receptor-mediated activation
ADP-ribosylation factor
-
GTP dependent activation
-
ADP-ribosylation factor
-
required for activity
-
ADP-ribosylation factor
-
GTP dependent activation
-
ADP-ribosylation factor
-
GTP dependent activation
-
ARF GTPases
-
all ARF proteins 1-6 stimulate PLD1 and PLD2 to a similar extent
-
ARF GTPases
-
all ARF proteins 1-6 stimulate PLD to a similar extent
-
ARF GTPases
-
all ARF proteins 1-6 stimulate PLD to a similar extent
-
ARF protein
-
ARF family small GTPases, which are composed of six isoforms, ARF1-6 act as PLD activators, they activates PLD1 and PLD2. ARFs are myristoylated at their N-terminal glycine residue and this lipid modification is required to fully activate PLD1 [11,12]. In the ARF-dependent activation of PLD1, phosphatidylinositol 4,5-disphosphate is an essential cofactor. Phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 4,5-disphosphate act as cofactors and bind to the PX domain, which is also responsible for protein-protein interactions. PLD2 directly interacts with the phosphatidylinositol 4-phosphate 5-kinase
-
ARF protein
-
ARF family small GTPases, which are composed of six isoforms, ARF1-6 act as PLD activators, they activates PLD1 and PLD2. ARFs are myristoylated at their N-terminal glycine residue and this lipid modification is required to fully activate PLD1 [11,12]. In the ARF-dependent activation of PLD1, phosphatidylinositol 4,5-disphosphate is an essential cofactor. Phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 4,5-disphosphate act as cofactors and bind to the PX domain, which is also responsible for protein-protein interactions. PLD2 directly interacts with the phosphatidylinositol 4-phosphate 5-kinase
-
ARF protein
-
ARF family small GTPases, which are composed of six isoforms, ARF1-6 act as PLD activators, they activates PLD1 and PLD2. ARFs are myristoylated at their N-terminal glycine residue and this lipid modification is required to fully activate PLD1 [11,12]. In the ARF-dependent activation of PLD1, phosphatidylinositol 4,5-disphosphate is an essential cofactor. Phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 4,5-disphosphate act as cofactors and bind to the PX domain, which is also responsible for protein-protein interactions. PLD2 directly interacts with the phosphatidylinositol 4-phosphate 5-kinase
-
ARF protein
-
small G proteins of the Rho and Arf families activate phospholipase D1
-
Arf1 protein
-
activates PLD2 and PLD1 in vitro
-
Arf1 protein
-
activates PLD2 and PLD1 in vitro
-
Arf1 protein
-
activates PLD2 and PLD1 in vitro
-
Arf1 protein
-
activates PLD2 and PLD1 in vitro
-
Arf1 protein
-
activates PLD2 and PLD1 in vitro
-
Arf1 protein
-
activates PLD, acts synergistically with CtBP1/BARS in activation of PLD, dependent on GTPgammaS or GTP but not on GDP, overview
-
Arf1 protein
-
activates PLD2 and PLD1 in vitro
-
ATP
-
at 1 mM, 320% of control activity, 1 mM ATP + 0.1 mM GTP, 720% of control activity, effect is abolished by neomycin
ATP
-
extracellular application of nucleotides stimulates enzyme activity and shows a sustained activation of extracellular signal-regulated kinase. Effects on enzyme and extracellular signal-regulated kinase are not additive and not coupled to DNA synthesis. Best effects are with ATP and UTP at 0.01 mM and above
Ca2+
-
required, 1 mM
Ca2+
-
inhibits the PLD37/18-catalyzed hydrolysis of dibutyroylphosphatidylcholine at basic pH values, but activates the enzyme more than twofold at pH 5.5. Addition of Ca2+ at pH 8.0 increases the transphosphatidylation activity 2.5- and 3.5fold with 5 and 20 mM Ca2+, respectively. At pH 9.0, Ca2+ inhibits both phosphohydrolase and transferase activities with much less inhibition to the latter
Cdc42
-
in addition to interactions with Rac and Rho, PLD1 is regulated by Cdc42
-
Cdc42
-
in addition to interactions with Rac and Rho, PLD1 is regulated by Cdc42
-
Cdc42
-
stimulation of full-length enzyme and N-terminally truncated enzyme by GTPgammaS-loaded Cdc42
-
Cdc42
-
in addition to interactions with Rac and Rho, PLD1 is regulated by Cdc42
-
CHAPS
-
-
CHAPS
-
relative activity: 201
CHAPS
-
relative activity: 195%
CHAPS
-
activates 1.8fold at 1.5%
deoxycholic acid
-
relative activity: 246%
deoxycholic acid
-
relative activity: 273%
deoxycholic acid
-
activates 2.2fold at 1.5%
dynamin
-
a large GTPase, can interact with PLD in a GTP dependent manner in vitro
-
dynamin
-
a large GTPase, can interact with PLD in a GTP dependent manner in vitro
-
dynamin
-
a large GTPase, can interact with PLD in a GTP dependent manner in vitro
-
dynamin
-
a large GTPase, can interact with PLD in a GTP dependent manner in vitro
-
dynamin
-
a large GTPase, can interact with PLD in a GTP dependent manner in vitro
-
dynamin
-
a large GTPase, can interact with PLD in a GTP dependent manner in vitro
-
ethanol
-
-
ethanol
-
transphosphatidylation increases activity
ethyl ether
-
stimulates
ethyl ether
-
stimulates in the presence of Ca2+
fibronectin
-
adhesion of primary neutrophils and monocyte-derived macrohages as well as myeloid-macrophage cell lines to fibronectin is accompanied by marked stimulation of enzyme activity
-
fibronectin
in OVAR-3 cells fibronectin-mediated integrin activation specifically induces cell spreading which activates PLD
-
GTP
-
-
GTP
-
at 0.1 mM, 273% of control activity, 1 mM ATP + 0.1 mM GTP, 720% of control activity, effect is abolished by neomycin
GTPgammaS
-
at 0.005 mM, 446% of control activity
GTPgammaS
-
membrane fraction, 5fold increase in activity, membrane plus cytosolic fraction, 8fold increase in activity
guanosine 5'-3-O-(thio)triphosphate
-
GTP analog
guanosine 5'-3-O-(thio)triphosphate
-
GTP analog
H2O2
-
isozyme PLDdelta is activated by H2O2
H2O2
-
exposure of cells to H2O2 leads to transient increase in activity followed by 90% decrease
ionomycin
-
-
ionomycin
-
a Ca2+ ionophore
linoleic acid
less than oleic acid
linoleic acid
-
only in presence of Mg2+
linolenic acid
less than oleic acid
lysophosphatidylserine
-
stimulates PLD activity in a concentration-dependent manner and approximately 5fold and 8fold increases in CYP1A2 and CYP2E1 activities, respectively, are shown in the presence of 2 mol% of the lysophosphatidylserine when compared to a 100% phosphatidylcholine matrix. LysoPS also accompanies conformational changes in both CYP1A2 and CYP2E1 when assayed by circular dichroism
lysophosphatidylserine
-
stimulates PLD activity in a concentration-dependent manner and approximately 5fold and 8fold increases in CYP1A2 and CYP2E1 activities, respectively, are shown in the presence of 2 mol% of the lysophosphatidylserine when compared to a 100% phosphatidylcholine matrix. LysoPS also accompanies conformational changes in both CYP1A2 and CYP2E1 when assayed by circular dichroism
mastoparan
-
mastoparan
-
a PLD activity stimulator
mastoparan
-
G-protein inhibitor, treatment of roots results in accumulation of both phosphatidic acid and phosphatidylbutanol
oleic acid
best stimulation, optimal at 0.5 mM, stimulates binding to substrate, in presence of Ca2+
oleic acid
-
only in presence of Mg2+
phorbol 12-myristate 13-acetate
-
stimulation
phorbol 12-myristate 13-acetate
-
phorbol ester stimulation involves proteinkinase C but not ADP-ribosylation factor proteins
phorbol 12-myristate 13-acetate
-
a protein kinase C activator also activates PLD, activation is inhibited by 1-butanol
phorbol 12-myristate 13-acetate
-
activates 13fold at 0.001 mM in microglia and astrocytes
phosphatidic acid
-
only with addition of lecithin and SDS
phosphatidic acid
up to 2fold
phosphatidic acid
-
interaction of phospholipase D with the lipidic activator at the air-water interface
phosphatidic acid
-
the Streptomyces chromofuscus PLD seems to be dependent on presence of phosphatidic acid for activity on phospholipids
phosphatidylethanolamine
-
required for maximal activity of the beta and gamma-enzymes
phosphatidylethanolamine
-
activates PLD activity, leading to increased matrix metalloproteinase 9, MMP-9, activity
phosphatidylinositol 3,4,5-triphosphate
-
specifically interacts with the phox homology domain of phospholipase D1 and stimulates activity
phosphatidylinositol 3,4,5-triphosphate
-
-
phosphatidylinositol 3,4,5-triphosphate
-
-
phosphatidylinositol 3,4,5-trisphosphate
-
increases activity
phosphatidylinositol 3,4,5-trisphosphate
increases PLD activity
phosphatidylinositol 3,4,5-trisphosphate
-
binds to N-terminal phox consensus sequence of PLD1 and PLD2
phosphatidylinositol 3,4,5-trisphosphate
-
activity of PLD1 and PLD2 is highly dependent on the presence of phosphatidylinositol 4,5-bisphosphate or phosphatidylinositol 3,4,5-trisphosphate
phosphatidylinositol 4,5-bisphosphate
-
-
phosphatidylinositol 4,5-bisphosphate
-
binding is modulated by Ca2+
phosphatidylinositol 4,5-bisphosphate
required
phosphatidylinositol 4,5-bisphosphate
-
the interaction of Ca2+ with PLDbetacat (PLD with a deleted regulatory C2 domain) increases the affinity of the protein for the activator phosphatidylinositol 4,5-bisphosphate. Ca2+ binding to the C2 domain stimulates phosphatidylcholine binding but inhibits phosphatidylinositol 4,5-bisphosphate
phosphatidylinositol 4,5-bisphosphate
-
PLDbeta, PLDgamma, PLDdelta, and PLDzeta require PIP2 for activity
phosphatidylinositol 4,5-bisphosphate
-
essential cofactor
phosphatidylinositol 4,5-bisphosphate
strong activating effect at 2-10 mM CaCl2
phosphatidylinositol 4,5-bisphosphate
-
-
phosphatidylinositol 4,5-bisphosphate
activates
phosphatidylinositol 4,5-bisphosphate
-
increases activity
phosphatidylinositol 4,5-bisphosphate
-
only in vitro
phosphatidylinositol 4,5-bisphosphate
-
binds to N-terminal pleckstrin homology of PLD1 and PLD2
phosphatidylinositol 4,5-bisphosphate
-
activity of PLD1 and PLD2 is highly dependent on the presence of phosphatidylinositol 4,5-bisphosphate or phosphatidylinositol 3,4,5-trisphosphate
phosphatidylinositol 4,5-bisphosphate
-
-
phosphatidylinositol 4,5-bisphosphate
-
stimulation of full-length enzyme and N-terminally truncated enzyme
phosphatidylinositol 4,5-bisphosphate
-
-
phosphatidylinositol phosphate
-
-
phosphatidylinositol phosphate
-
only in vitro
phosphatidylinositol-3,4,5-trisphosphate
-
effective activator
phosphatidylinositol-3,4,5-trisphosphate
with partially purified enzyme, stimulation up to 5fold
phosphatidylinositol-4,5-bisphosphate
required
phosphatidylinositol-4,5-bisphosphate
less than oleic acid, best at 0.03 mM
phosphatidylinositol-4,5-bisphosphate
in native myocardium, stimulation up to 2fold at 0.1 mM, accompanied by increase in diacylglycerol, with partially purified enzyme, stimulation up to 10fold at 0.1 mM
phosphatidylinositol-4,5-bisphosphate
-
required for PLD2 activity
phosphatidylinositol-4,5-bisphosphate
-
an essential cofactor for phospholipase D1 activity
phosphatidylinositol-4,5-bisphosphate
-
-
polyethylene-4-laurylether
-
relative activity: 125%
-
polyethylene-4-laurylether
-
activates 2.1fold at 1.5%
-
Protein kinase C
-
-
-
Protein kinase C
-
activates isozyme PLD1
-
Protein kinase C
-
only phorbolester activated proteinkinase C
-
Rac1
-
stimulation of full-length enzyme and N-terminally truncated enzyme by GTPgammaS-loaded Rac1
-
Rac1
-
PLD activation by EGF is dependent on Rac1, and not on PKC, in Rat1 fibroblasts
-
Rho GTPases
-
activate isozyme PLD1
-
Rho GTPases
-
PLD1 and PLD2 activity is regulated by the Rho family of small GTPases
-
Rho GTPases
-
PLD1 and PLD2 activity is regulated by the Rho family of small GTPases
-
Rho GTPases
-
PLD1 and PLD2 activity is regulated by the Rho family of small GTPases
-
RhoA
-
-
RhoA
-
only in synergy with ARF1
RhoA
-
small G proteins ARF3 and RhoA in the presence of guanosine 5'-3-O-(thio)triphosphate
RhoA
-
stimulation of full-length enzyme and N-terminally truncated enzyme by GTPgammaS-loaded RhoA
RhoA
-
mediates PDGF-induced PLD activation in Rat1 fibroblasts
salicylic acid
-
activates transphosphatidylation reaction of PLD in a dose-dependent manner
salicylic acid
-
rapid activation of isoforms PLDalpha, PLDbeta/gamma, PLDdelta
SDS
-
-
SDS
-
maximal activation at 1 mM
SDS
-
relative activity: 189
serotonin
-
i.e. 5-hydroxytryptamine, 5-HT, activates PLD via the 5-HT 2A receptor, leading to the generation of phosphatidic acid that promotes smooth muscle cell proliferation through activations of mammalian target of rapamycin, mTOR, S6K1 and MAPK but not the Rho or PI3-kinase/Akt signaling pathways, overview. Activation is completely blocked by ketanserin
serotonin
-
i.e. 5-hydroxytryptamine, 5-HT, activates PLD via the 5-HT 2A receptor, leading to the generation of phosphatidic acid that promotes smooth muscle cell proliferation through activations of mammalian target of rapamycin, mTOR, S6K1 and MAPK but not the Rho or PI3-kinase/Akt signaling pathways, overview. Activation is completely blocked by ketanserin
sodium deoxycholate
-
-
thrombin
-
-
thrombin
activation in a dose-dependent manner. Thrombin-induced PLD activity is dependent on autocrine stimulation
-
Triton X-100
-
substrate-dependent activation
Triton X-100
greatly stimulating
Triton X-100
-
in molar ratio phosphatidylcholine to Triton X-100 2.5:1
Triton X-100
-
up to 0.4%, inhibitory above
Triton X-100
-
relative activity: 429%
Triton X-100
-
optimal at 1.5%
Triton X-100
-
0.375%, 75% increase in activity
Triton X-100
-
relative activity: 292%
Triton X-100
in the presence of 0.05-0.5% and 0.1-0.2% (wt/vol) Triton X-100, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine and choline plasmalogen are efficiently hydrolyzed, respectively. Hydrolysis of lysophosphatidylcholine and choline lysoplasmalogen does not require Triton X-100, the hydrolytic activity is inhibited by more than 0.05% (wt/vol) Triton X-100
Triton X-100
-
activates 2.65fold at 1.5%
Tween-20
-
relative activity: 257%
Tween-20
-
relative activity: 345%
Tween-20
-
activates 2.3fold at 1.5%
Tween-80
-
relative activity: 249%
Tween-80
-
relative activity: 292%
additional information
no activation by stearic or palmitic acid
-
additional information
no requirement for phosphatidylethanolamine in substrate vesicles, comparison of isozymes
-
additional information
-
activity of phospholipase D in plants increases under different hyperosmotic stresses, such as dehydration, drought, and salinity, overview
-
additional information
-
PLDepsilon activity and phosphatidic acid content enhance growth under hyperosmotic stres
-
additional information
-
cold stress treatment strongly stimulates the phospholipase D activity and affects the phosphatidic acid levels of the plasma membranes. Concommitantly, the H+-ATPase activity is strongly inhibited, which correlates with a reduced association with the regulatory 14-3-3 proteins
-
additional information
-
epidermal growth factor triggers the activation of PLD in various cell types, such as a bovine luteal cell line
-
additional information
-
enzyme is independent of phosphatidylinositol-4,5-bisphosphate
-
additional information
-
phorbol 12-myristate 13-acetate induces PLD2 activation via the involvement of protein kinase Calpha. PLD2 becomes phosphorylated on both Ser and Thr residues. Interaction rather than phosphorylation underscores the activation of PLD2 by protein kinase Calpha in vivo. Phosphorylation may contribute to the inactivation of the enzyme
-
additional information
-
epidermal growth factor triggers the activation of PLD in various cell types, such as a Chinese hamster lung fibroblast cell line, CCL39, and a Chinese hamster embryo fibroblast cell line, IIC9
-
additional information
-
not activating: AMP
-
additional information
-
adhesion of myeloid-macrophage cell lines to fibronectin is accompanied by marked stimulation of enzyme activity
-
additional information
-
overexpression of tumor suppressor PTEN results in 30% increase in basal enzyme activity
-
additional information
-
epidermal growth factor triggers the activation of PLD in various cell types, such as osteoblastic cells, a human embryonic kidney cell line HEK-293, a human epidermoid carcinoma cell line A-431, a human cervical cancer cell line HeLa, and human dermal fibroblasts
-
additional information
-
in some physiological settings, the PLD2 activity appears to be regulated by the classical MAP kinase, extracellular signal-regulated kinase pathway. In neutrophilic HL-60 cells and HEK 293T cells stably expressing fMLP receptors, PLD2 is activated through ERK1/2 MAP kinase upon fMLP stimulation
-
additional information
-
PLD1 is activated by oxidative stress in various cell lines. Reactive oxygen species-induced PLD1 activation involves PKC and tyrosine kinases in various mammalian cell systems
-
additional information
-
PLD2 activity is enhanced by PMA/ionomycin stimulation
-
additional information
-
the overexpression of tuberous sclerosis complex 2, TSC2, suppresses PLD1 activation, whereas the knockdown or deletion of TSC2 leads to elevated basal activity of PLD
-
additional information
-
[D-Ala2,Me Phe4,Glyol5]enkephalin and beta-endorphin strongly induce PLD2 activation, whereas the non-endocytotic drugs morphine and buprenorphine do not activate PLD2
-
additional information
-
overview on activating compounds and mechanism
-
additional information
-
acidic extracellular pH induces enzyme activity both via Ca2+ influx and acidic shingomyelinase
-
additional information
-
mechanical stimulation of skeletal muscle with intermittent passive stretch ex vivo induces phospholipase D activation, phosphatidic acid accumulation, and signaling by mTOR, i.e. mammalian target of rapamycin
-
additional information
-
epidermal growth factor triggers the activation of PLD in various cell types, such as mouse embryo fibroblasts, MEFs, a mouse myoblast cell line, C2C12, and a mouse embryo fibroblast cell line Swiss 3T3
-
additional information
-
in some physiological settings, the PLD2 activity appears to be regulated by the classical MAP kinase, extracellular signal-regulated kinase pathway
-
additional information
-
PLD activity is modified by microtubule dynamics
-
additional information
-
epidermal growth factor triggers the activation of PLD in various cell types, such as immortalized rabbit corneal epithelial cells
-
additional information
-
interaction of the PLD1 PX domain with phosphatidylinositol 3,4,5-trisphosphate and/or phosphatidic acid (or phosphatidylserine) may be an important factor in the spatiotemporal regulation and activation of PLD1
-
additional information
-
no activation of thymocyte enzyme by eicosapentaenoic acid. Negative correlation of enzyme activation and proliferative response of thymocytes to fatty acids
-
additional information
-
activation mechanism of PLD in macropinocytosis, overview
-
additional information
-
epidermal growth factor triggers the activation of PLD in various cell types, such as calvarial osteoblastic cells and 3Y1 rat fibroblasts
-
additional information
-
in some physiological settings, the PLD2 activity appears to be regulated by the classical MAP kinase, extracellular signal-regulated kinase pathway
-
additional information
-
no inhibition of PLD by WRW4
-
additional information
-
no activation by phorbol-12-myristate-13-acetate or GTPgammaS
-
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0.0026 - 0.03
(1S,2S)-N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-2-phenylcyclopropanecarboxamide
0.0001 - 0.02
(1S,2S)-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
0.000008 - 0.00115
(1S,2S)-N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
0.0000037 - 0.0064
(1S,2S)-N-[(1S)-2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
0.000012 - 0.0038
(1S,2S)-N-[(1S)-2-[4-(6-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
0.02
(1S,2S)-N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-2-phenylcyclopropanecarboxamide
0.000035 - 0.0039
(1S,2S)-N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-2-phenylcyclopropanecarboxamide
0.000002 - 0.00052
(1S,2S)-N-[2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-2-phenylcyclopropanecarboxamide
0.00015 - 0.0002
3,4-difluoro-N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]benzamide
0.000038 - 0.014
3,4-difluoro-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
0.000004 - 0.000014
3,4-difluoro-N-[2-[4-(6-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
0.0034 - 0.027
3-methyl-N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]benzamide
0.0026 - 0.02
4-(4-(2-(3-methoxyphenyl)benzo[b]thiophen-3-yl)phenoxy)-N,N-dimethylethan-1-amine
0.00055 - 0.0059
4-amino-3-methoxy-N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]benzamide
0.000043 - 0.012
4-chloro-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
0.0000064 - 0.0012
4-chloro-N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
0.0000074 - 0.00104
4-chloro-N-[(1S)-2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
0.000018 - 0.000061
4-chloro-N-[2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
0.000007 - 0.000042
4-chloro-N-[2-[4-(6-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
0.00013 - 0.01
4-fluoro-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
0.000011 - 0.0031
4-fluoro-N-[(1S)-2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
0.0067 - 0.012
4-fluoro-N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]benzamide
0.00061 - 0.014
4-fluoro-N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]benzamide
0.000012 - 0.000375
4-fluoro-N-[2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
0.000025 - 0.00021
5-fluoro-N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-1H-indole-2-carboxamide
0.00003 - 0.00029
5-fluoro-N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-1H-indole-2-carboxamide
0.00012 - 0.00085
6-fluoro-N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]naphthalene-2-carboxamide
0.0026 - 0.0099
desketoraloxifene
0.000025 - 0.00014
N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]naphthalene-2-carboxamide
0.000066 - 0.013
N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
0.0000035 - 0.000187
N-[(1S)-2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-3,4-difluorobenzamide
0.000004 - 0.00089
N-[(1S)-2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-4-chlorobenzamide
0.0000055 - 0.0039
N-[(1S)-2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
0.000003 - 0.00073
N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-3,4-difluorobenzamide
0.00001 - 0.0014
N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-4-fluorobenzamide
0.000046 - 0.000933
N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
0.000002 - 0.00036
N-[(1S)-2-[4-(6-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
0.00099 - 0.00425
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-1,2,3,4-tetrahydronaphthalene-2-carboxamide
0.00003 - 0.00015
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-1-benzothiophene-2-carboxamide
0.0016 - 0.0021
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-3-phenylprop-2-ynamide
0.00011 - 0.001
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]naphthalene-2-carboxamide
0.00009 - 0.0019
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]quinoline-3-carboxamide
0.02
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]quinoxaline-2-carboxamide
0.000009 - 0.00578
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
0.000004 - 0.00039
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
0.000023 - 0.0028
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
0.00003 - 0.00206
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
0.00005 - 0.00347
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
0.0000034 - 0.00025
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
0.000004 - 0.0012
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
0.000005 - 0.00087
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
0.00002 - 0.0015
N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
0.000063 - 0.0025
N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-2-carboxamide
0.008 - 0.01
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
0.0001 - 0.00266
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
0.00035 - 0.0059
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
0.00036 - 0.0027
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
0.00559 - 0.00567
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
0.00005 - 0.000335
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
0.000655 - 0.00227
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
0.0002 - 0.0035
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
0.00008 - 0.0017
N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
0.00004 - 0.002
N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
0.00011 - 0.00086
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-3,4-dihydronaphthalene-2-carboxamide
0.00004 - 0.00073
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-3-phenylprop-2-ynamide
0.000021 - 0.00038
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]naphthalene-2-carboxamide
0.000008 - 0.000042
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]quinoline-3-carboxamide
0.00007 - 0.00074
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]quinoline-6-carboxamide
0.000021 - 0.0003
N-[2-[4-(4-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-fluorobenzamide
0.000003 - 0.000097
N-[2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-chlorobenzamide
0.000004 - 0.000076
N-[2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-fluorobenzamide
0.00001 - 0.00024
N-[2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-methylbenzamide
0.000004 - 0.00014
N-[2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]naphthalene-2-carboxamide
0.033
Na3VO4
Brassica juncea var. juncea
pH 5.5, 37°C
0.0078
NaAlF4
Brassica juncea var. juncea
pH 5.5, 37°C
0.0026
(1S,2S)-N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD1
0.03
(1S,2S)-N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD2
0.0001
(1S,2S)-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD1
0.02
(1S,2S)-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD2
0.000008
(1S,2S)-N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD1
0.00115
(1S,2S)-N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD2
0.0000037
(1S,2S)-N-[(1S)-2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD1
0.0064
(1S,2S)-N-[(1S)-2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD2
0.000012
(1S,2S)-N-[(1S)-2-[4-(6-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD1
0.0038
(1S,2S)-N-[(1S)-2-[4-(6-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD2
0.02
(1S,2S)-N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD1
0.02
(1S,2S)-N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD2
0.000035
(1S,2S)-N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD1
0.0039
(1S,2S)-N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD2
0.000002
(1S,2S)-N-[2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD1
0.00052
(1S,2S)-N-[2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-2-phenylcyclopropanecarboxamide
Homo sapiens
isoform PLD2
0.00015
3,4-difluoro-N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]benzamide
Homo sapiens
isoform PLD1
0.0002
3,4-difluoro-N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]benzamide
Homo sapiens
isoform PLD2
0.000038
3,4-difluoro-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
Homo sapiens
isoform PLD1
0.014
3,4-difluoro-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
Homo sapiens
isoform PLD2
0.000004
3,4-difluoro-N-[2-[4-(6-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
Homo sapiens
isoform PLD1
0.000014
3,4-difluoro-N-[2-[4-(6-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
Homo sapiens
isoform PLD2
0.0034
3-methyl-N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]benzamide
Homo sapiens
isoform PLD1
0.027
3-methyl-N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]benzamide
Homo sapiens
isoform PLD2
0.0026
4-(4-(2-(3-methoxyphenyl)benzo[b]thiophen-3-yl)phenoxy)-N,N-dimethylethan-1-amine
Homo sapiens
-
isofom PLD1, cellular assay, pH 7.5, 37°C
0.0047
4-(4-(2-(3-methoxyphenyl)benzo[b]thiophen-3-yl)phenoxy)-N,N-dimethylethan-1-amine
Homo sapiens
-
isofom PLD1, recombinant protein, pH 7.5, 37°C
0.0071
4-(4-(2-(3-methoxyphenyl)benzo[b]thiophen-3-yl)phenoxy)-N,N-dimethylethan-1-amine
Homo sapiens
-
isofom PLD2, recombinant protein, pH 7.5, 37°C
0.0075
4-(4-(2-(3-methoxyphenyl)benzo[b]thiophen-3-yl)phenoxy)-N,N-dimethylethan-1-amine
Pseudomonas aeruginosa
-
monomeric substrate, pH 7.5, 37°C
0.0161
4-(4-(2-(3-methoxyphenyl)benzo[b]thiophen-3-yl)phenoxy)-N,N-dimethylethan-1-amine
Pseudomonas aeruginosa
-
substrate presented in liposome, pH 7.5, 37°C
0.02
4-(4-(2-(3-methoxyphenyl)benzo[b]thiophen-3-yl)phenoxy)-N,N-dimethylethan-1-amine
Homo sapiens
-
isofom PLD2, cellular assay, pH 7.5, 37°C
0.00055
4-amino-3-methoxy-N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]benzamide
Homo sapiens
isoform PLD2
0.0059
4-amino-3-methoxy-N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]benzamide
Homo sapiens
isoform PLD1
0.000043
4-chloro-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
Homo sapiens
isoform PLD1
0.012
4-chloro-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
Homo sapiens
isoform PLD2
0.0000064
4-chloro-N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
Homo sapiens
isoform PLD1
0.0012
4-chloro-N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
Homo sapiens
isoform PLD2
0.0000074
4-chloro-N-[(1S)-2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
Homo sapiens
isoform PLD1
0.00104
4-chloro-N-[(1S)-2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
Homo sapiens
isoform PLD2
0.000018
4-chloro-N-[2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
Homo sapiens
isoform PLD1
0.000061
4-chloro-N-[2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
Homo sapiens
isoform PLD2
0.000007
4-chloro-N-[2-[4-(6-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
Homo sapiens
isoform PLD1
0.000042
4-chloro-N-[2-[4-(6-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
Homo sapiens
isoform PLD2
0.00013
4-fluoro-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
Homo sapiens
isoform PLD1
0.01
4-fluoro-N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
Homo sapiens
isoform PLD2
0.000011
4-fluoro-N-[(1S)-2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
Homo sapiens
isoform PLD1
0.0031
4-fluoro-N-[(1S)-2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]benzamide
Homo sapiens
isoform PLD2
0.0067
4-fluoro-N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]benzamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.012
4-fluoro-N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]benzamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00061
4-fluoro-N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]benzamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.014
4-fluoro-N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]benzamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.000012
4-fluoro-N-[2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
Homo sapiens
isoform PLD1
0.000375
4-fluoro-N-[2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]benzamide
Homo sapiens
isoform PLD2
0.000025
5-fluoro-N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-1H-indole-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.00021
5-fluoro-N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-1H-indole-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00003
5-fluoro-N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-1H-indole-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.00029
5-fluoro-N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-1H-indole-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00012
6-fluoro-N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD1
0.00085
6-fluoro-N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD2
0.0026
desketoraloxifene
Homo sapiens
-
isoform PLD2, cellular assay, pH 7.5, 37°C
0.0061
desketoraloxifene
Homo sapiens
-
isoform PLD1, cellular assay, pH 7.5, 37°C
0.0099
desketoraloxifene
Pseudomonas aeruginosa
-
substrate presented in liposome, pH 7.5, 37°C
0.000025
N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD1
0.00014
N-[(1S)-1-methyl-2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD2
0.000066
N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD1
0.013
N-[(1S)-2-[4-(4-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD2
0.0000035
N-[(1S)-2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-3,4-difluorobenzamide
Homo sapiens
isoform PLD1
0.000187
N-[(1S)-2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-3,4-difluorobenzamide
Homo sapiens
isoform PLD2
0.000004
N-[(1S)-2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-4-chlorobenzamide
Homo sapiens
isoform PLD1
0.00089
N-[(1S)-2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-4-chlorobenzamide
Homo sapiens
isoform PLD2
0.0000055
N-[(1S)-2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD1
0.0039
N-[(1S)-2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD2
0.000003
N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-3,4-difluorobenzamide
Homo sapiens
isoform PLD1
0.00073
N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-3,4-difluorobenzamide
Homo sapiens
isoform PLD2
0.00001
N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-4-fluorobenzamide
Homo sapiens
isoform PLD1
0.0014
N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]-4-fluorobenzamide
Homo sapiens
isoform PLD2
0.000046
N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD1
0.000933
N-[(1S)-2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD2
0.000002
N-[(1S)-2-[4-(6-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD1
0.00036
N-[(1S)-2-[4-(6-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]-1-methylethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD2
0.00099
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-1,2,3,4-tetrahydronaphthalene-2-carboxamide
Homo sapiens
isoform PLD2
0.00425
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-1,2,3,4-tetrahydronaphthalene-2-carboxamide
Homo sapiens
isoform PLD1
0.00003
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-1-benzothiophene-2-carboxamide
Homo sapiens
isoform PLD2
0.00015
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-1-benzothiophene-2-carboxamide
Homo sapiens
isoform PLD1
0.0016
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-3-phenylprop-2-ynamide
Homo sapiens
isoform PLD2
0.0021
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]-3-phenylprop-2-ynamide
Homo sapiens
isoform PLD1
0.00011
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD2
0.001
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD1
0.00009
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]quinoline-3-carboxamide
Homo sapiens
isoform PLD2
0.0019
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]quinoline-3-carboxamide
Homo sapiens
isoform PLD1
0.02
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]quinoxaline-2-carboxamide
Homo sapiens
isoform PLD1
0.02
N-[2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-8-yl)ethyl]quinoxaline-2-carboxamide
Homo sapiens
isoform PLD2
0.000009
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.00578
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.000004
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.00039
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.000023
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.0028
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00003
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.00206
N-[2-[1-(3,4-difluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00005
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.00347
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.0000034
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.00025
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.000004
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.0012
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.000005
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.00087
N-[2-[1-(3-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00002
N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.0015
N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.000063
N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.0025
N-[2-[1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.008
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.01
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.0001
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.00266
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00035
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.0059
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00036
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.0027
N-[2-[1-(4-bromophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00559
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00567
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-4-fluorobenzamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.00005
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.000335
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]-5-fluoro-1H-indole-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.000655
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.00227
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.0002
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.0035
N-[2-[1-(4-chlorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00008
N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.0017
N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00004
N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
Homo sapiens
-
isozyme PLD2, pH and temperature not specified in the publication
0.002
N-[2-[1-(4-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]dec-8-yl]ethyl]quinoline-3-carboxamide
Homo sapiens
-
isozyme PLD1, pH and temperature not specified in the publication
0.00011
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-3,4-dihydronaphthalene-2-carboxamide
Homo sapiens
isoform PLD1
0.00086
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-3,4-dihydronaphthalene-2-carboxamide
Homo sapiens
isoform PLD2
0.00004
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-3-phenylprop-2-ynamide
Homo sapiens
isoform PLD1
0.00073
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-3-phenylprop-2-ynamide
Homo sapiens
isoform PLD2
0.000021
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD1
0.00038
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD2
0.000008
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]quinoline-3-carboxamide
Homo sapiens
isoform PLD1
0.000042
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]quinoline-3-carboxamide
Homo sapiens
isoform PLD2
0.00007
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]quinoline-6-carboxamide
Homo sapiens
isoform PLD1
0.00074
N-[2-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]quinoline-6-carboxamide
Homo sapiens
isoform PLD2
0.000021
N-[2-[4-(4-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-fluorobenzamide
Homo sapiens
isoform PLD1
0.0003
N-[2-[4-(4-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-fluorobenzamide
Homo sapiens
isoform PLD2
0.000003
N-[2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-chlorobenzamide
Homo sapiens
isoform PLD1
0.000097
N-[2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-chlorobenzamide
Homo sapiens
isoform PLD2
0.000004
N-[2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-fluorobenzamide
Homo sapiens
isoform PLD1
0.000076
N-[2-[4-(5-bromo-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-fluorobenzamide
Homo sapiens
isoform PLD2
0.00001
N-[2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-methylbenzamide
Homo sapiens
isoform PLD1
0.00024
N-[2-[4-(5-chloro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]-4-methylbenzamide
Homo sapiens
isoform PLD2
0.000004
N-[2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD1
0.00014
N-[2-[4-(5-fluoro-2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]ethyl]naphthalene-2-carboxamide
Homo sapiens
isoform PLD2
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evolution
the enzyme belongs to the PLD superfamily, PLD superfamily members share a common core structure, and a common catalytic mechanism
evolution
-
the enzyme belongs to the PLD superfamily, PLD superfamily members share a common core structure, and thereby, a common catalytic mechanism
evolution
-
the enzyme belongs to the PLD superfamily, PLD superfamily members share a common core structure, and thereby, a common catalytic mechanism
evolution
-
the enzyme belongs to the PLD superfamily, PLD superfamily members share a common core structure, and thereby, a common catalytic mechanism
evolution
the enzyme belongs to the PLD superfamily, PLD superfamily members share a common core structure, and thereby, a common catalytic mechanism
evolution
the enzyme belongs to the PLD superfamily, PLD superfamily members share a common core structure, and thereby, a common catalytic mechanism
evolution
the enzyme belongs to the PLD superfamily, PLD superfamily members share a common core structure, and thereby, a common catalytic mechanism
evolution
-
the enzyme belongs to the PLD superfamily, PLD superfamily members share a common core structure, and thereby, a common catalytic mechanism
-
evolution
-
the enzyme belongs to the PLD superfamily, PLD superfamily members share a common core structure, and thereby, a common catalytic mechanism
-
malfunction
-
disruption of phospholipase D causes a reduction in the organism's ability to thrive in serum, a deficiency in epithelial cell invasion, and diminished pathogenesis in a murine model of pneumonia
malfunction
-
inhibition of Pld1 function, by siRNA-mediated downregulation or 1-butanol, does not strongly impair the dorsal-ventral guidance of primary/secondary motor axons
malfunction
-
inhibition of RalA or PKC, activators of PLD, also inhibits endocytosis of EGFR
malfunction
-
lipase-inactive PLD1 or inhibition of PLD1 by pharmacological inhibitors blocks PKD1 activation under oxidative stress
malfunction
-
phospholipase D isozymes are overexpressed in various human tumor tissues and involved in tumorigenesis. The increased expression of PLD and its enzymatic activity in the glioma stimulate the secretion and expression of matrix metalloproteinase 2, MMP-2 and induce the invasiveness of glioma cells, mechanism, overview
malfunction
-
phospholipase D, a phosphatidic acid-synthesizing enzyme, is linked to multiple aspects of normal brain function and to Alzheimer's disease, the most common neurodegenerative disorder, an imbalance in phospholipids is involved in development of Alzheimer's disease, overview
malfunction
PLD inhibition disrupts the actin cytoskeleton in tobacco pollen tubes, with severe disorganization of actin, both in the apex and in the shank
malfunction
-
PLD2 is active in lymphoma cell metastasis, cells expressing active PLD2 form metastases in syngeneic mice
malfunction
-
pretreatment of human neutrophils with PLD inhibitor resveratrol significantly blocks oxidative burst, leukocyte migration, degranulation, and inflammatory cytokine production involving inhibition of sphingosine kinase activity and ERK1/2 phosphorylation
malfunction
-
pretreatment of mouse neutrophils with PLD inhibitor resveratrol significantly blocks oxidative burst, leukocyte migration, degranulation, and inflammatory cytokine production involving inhibition of sphingosine kinase activity and ERK1/2 phosphorylation
malfunction
-
suppression of PLDbeta1 enhances disease resistance against rice bacterial blight as well as rice blast
malfunction
-
cells lacking PldB preferentially sort to the stalk in chimeric fruiting bodies with wild-type cells
malfunction
-
knockdown of OsPLD-1 affects H+-ATPase- and Na+/H+ antiporter-related gene expression and inhibits salt-induced increase of H+-ATPase activity
malfunction
-
cells lacking PldB preferentially sort to the stalk in chimeric fruiting bodies with wild-type cells
-
metabolism
-
phosphatidic acid is a source of diacylglycerol, the two versatile lipid second messengers are at the centre of a phospholipid signalling network and as such are involved in several cellular functions
metabolism
-
phosphatidic acid is a source of diacylglycerol, the two versatile lipid second messengers are at the centre of a phospholipid signalling network and as such are involved in several cellular functions
metabolism
-
phospholipase D1 is regulated by ADP-ribosylation factors which are themselves regulators of vesicle trafficking
metabolism
-
phospholipase D1 is regulated by ADP-ribosylation factors which are themselves regulators of vesicle trafficking
metabolism
-
the regulation of PLD activity by phosphoinositides, particularly by PtdIns(4,5)P2 provides a link with a number of proteins known to regulate cytoskeletal changes associated with adhesion and migration of cells, while this is also apparent when the additional PLD regulators, in particular the small GTPases, are considered
metabolism
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the regulation of PLD activity by phosphoinositides, particularly by PtdIns(4,5)P2 provides a link with a number of proteins known to regulate cytoskeletal changes associated with adhesion and migration of cells, while this is also apparent when the additional PLD regulators, in particular the small GTPases, are considered
metabolism
-
the regulation of PLD activity by phosphoinositides, particularly by PtdIns(4,5)P2 provides a link with a number of proteins known to regulate cytoskeletal changes associated with adhesion and migration of cells, while this is also apparent when the additional PLD regulators, in particular the small GTPases, are considered
metabolism
-
the sites of phospholipid hydrolysis by phospholiphosphatidic acids D, C, A, and the targets of phosphatidic acid identified in plants that are potentially involved in hyperosmotic stress responses, and regulation of PLD isozymes in hyperosmotic stresses, overview
metabolism
-
high glucose increases insulin secretion through a PLD1-related pathway, high glucose induces the PLD1 binding of Arf6, which is involved in the glucose-induced insulin secretion pathway
metabolism
-
identification of a signaling pathway for PLD in the lacrimal gland with Rho and ROCK1 activating PLD1, but not PLD2, in response to cholinergic agonists causing their association with one another. Formation of this signaling complex results in the downstream activation of MEK and ERK, but the activation is independent of the signaling molecules Ras, Raf, Pyk2, and cSrc, which usually activate ERK. Activation of ERK then attenuates cholinergic agonist-stimulated protein secretion. The muscarinic activation of PLD1 attenuates protein secretion by activating ERK
metabolism
-
PldB mediates quorum sensing in the CMF pathway and regulates the dissociation of G protein Galpha2betagamma
metabolism
-
when rice suspension-cultured cells are treated with 100 mM NaCl, PLDalpha activity in cell extracts show a transient activation with a threefold increase at 1 h. The amount of OsPLDalpha protein decreases slightly in the cytosolic fractions, whereas it increases significantly in the tonoplast after NaCl treatment. Knockdown of OsPLD-1 prevents the NaCl-induced increase in the transcript level of OsVHA-A, encodes TP H+-ATPase, and OSA2, encodes PM H+-ATPase, as well as OsNHX1, encodes TP Na+/H+ antiporter
metabolism
-
PldB mediates quorum sensing in the CMF pathway and regulates the dissociation of G protein Galpha2betagamma
-
physiological function
-
activity of Pld1 in the developing notochord is essential for vascular development in vertebrates. Pld1 may regulate the ISV development through a parallel pathway controlling angiogenesis or play a role downstream of these angiogenic pathways, overview
physiological function
-
different PLD isozymes are likely to serve diverse functions in membrane trafficking, endocytosis, exocytosis, cell growth, differentiation and actin cytoskeletal organization. Regulatory function of PLD, detailed overview. Phospholipase D signalling is involved in neurite outgrowth
physiological function
-
different PLD isozymes are likely to serve diverse functions in membrane trafficking, endocytosis, exocytosis, cell growth, differentiation and actin cytoskeletal organization. Regulatory function of PLD, detailed overview. Phospholipase D signalling is involved in neurite outgrowth
physiological function
-
different PLD isozymes are likely to serve diverse functions in membrane trafficking, endocytosis, exocytosis, cell growth, differentiation and actin cytoskeletal organization. Regulatory function of PLD, detailed overview. Phospholipase D signalling is involved in neurite outgrowth
physiological function
-
essential role of PLD2 activity in the opioid-mediated induction of reactive oxygen species synthesis
physiological function
-
importance and activating role of PLD2 for LPS-induced NO synthesis in Raw 264.7 cells with involvement of the S6K1-p42/44 MAPK-STAT3 pathway. Binding of transcription factor STAT3 to the iNOS promoter is mediated by PLD2
physiological function
-
involvement of isozyme phospholipase Dzeta2 in root hydrotropism through the suppression of root gravitropism by abscisic acid, overview
physiological function
-
involvement of PLD in response to water deficits and salinity. Isozyme PLDdelta plays an important role in protecting cells from damage by reactive oxygen species. Isozyme PLDalpha1 promotes stomatal closure and reduces water loss. PLDalpha1 and PLDdelta are involved in seedling tolerance to salt stress. PLDalpha3 and PLDepsilon enhance plant growth and hyperosmotic tolerance. The different PLDs regulate the production of phosphatidic acid, a key class of lipid mediators in plant response to environmental stresses. Signalling and regulatory functions of PLD isozymes and phosphatidic acid in Arabidopsis thaliana response to drought and salinity, overview. PLDalpha1 and phosphatidic acid play a positive role in abscisic acid effects on preventing water loss. Involvement of PLDalpha3 in salt stress response, and of isozyme PLDepsilon in N signalling and plant growth under salt stress and water deficiency with genetic alterations of PLDepsilon affecting plant root architecture and biomass production, overview
physiological function
-
isozyme PLDalpha3 plays a positive role in hyperosmotic stress through a mechanism different from that for PLDalpha1, which mediates the effect of abscisic acid on stomatal movements. PLDalpha3 enhances root growth and accelerates flowering time under hyperosmotic stress. Alterations of PLDalpha3 activity affect the level of phosphatidic acid, and of transcripts of TOR and AGC2.1, of ABA-responsive genes, and of phosphorylated S6K protein under hyperosmotic stress, overview. PLDalpha3 may be involved in the crosstalk among glucose sensing, abscisic acid response, and S6K activation to regulate growth and development
physiological function
-
key role for phospholipase D in the generation of the slow excitatory postsynaptic current in cerebellar Purkinje cells
physiological function
main function of PLD is to hydrolyze membrane phosphatidylcholine to generate the precursor signaling molecule phosphatidic acid and choline. PLD activity is required for osteoblast differentiation, and isozyme PLD2 is the main isoform involved in this pathway
physiological function
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participation of PLD/phosphatidic acid in the light-mediated transduction signalling cascade of phosphoenolpyruvate carboxylase, C4-PEPC, phosphorylation through a phosphoenolpyruvate carboxylase kinase, PEPC-k, overview
physiological function
phosphatidic acid plays a regulatory role in important cellular processes such as secretion, cellular shape change, and movement. PLD-based signaling also plays a pro-mitogenic and pro-survival role in cells and therefore anti-apoptotic
physiological function
-
phosphatidic acid, a lipid generated by PLD, favors membranes with negative curvature and thus can facilitate both membrane fission and fusion. Role for PLD in endocytosis and membrane recycling from endocytic pathways, overview. PLD is involved n internalization of signaling receptors in endocytosis
physiological function
-
phospholipase D and its product phosphatidic acid are upstream regulators of the mitogenic mTOR signaling in both mitogenesis and the mechanical stimulation of skeletal muscle growth. Isozyme PLD1, but not PLD2, is required for Rheb activation of the mTOR pathway and for Rheb activation of S6K1, PLD1 is a bona fide effector for Rheb
physiological function
-
phospholipase D cleaves phospholipids into phosphatidic acid and free-head groups such as choline
physiological function
phospholipase D is a key enzyme involved in phospholipid catabolism, initiating a lipolytic cascade in membrane deterioration during senescence and stress
physiological function
-
phospholipase D signaling is involved in serotonin-induced mitogenesis of pulmonary artery smooth muscle cells. PLD activation participates in the cellular proliferation response to serotonin
physiological function
-
phospholipase D signaling is involved in serotonin-induced mitogenesis of pulmonary artery smooth muscle cells. PLD activation participates in the cellular proliferation response to serotonin
physiological function
-
PLD acting upstream of the MAP kinases ERK1/2 may play a key role in the regulation of IL-2 production by stimulated Jurkat cells. PLD2 promotes an early and sustained increase in ERK1/2 phosphorylation in recombinant T-cell lines, which is inhibited by 1-butanol
physiological function
PLD activity controls the structure of the actin cytoskeleton in tobacco pollen tubes, actin forms affect differently the activity of distinct tobacco C2 PLDs, overview
physiological function
-
PLD activity is a key enzyme involved in CpG oligodeoxynucleotides-induced intracellular mycobacterial killing in human monocytes/macrophages. Phagolysosome biogenesis from endosomes appears to be mediated by PLD activation, which is inhibited by ethanol in vivo in A-549 cells, overview
physiological function
-
PLD generates bioactive lipid second messengers in vascular endothelial cells
physiological function
PLD is a key enzyme involved in secretion, endocytosis and receptor signalling with importance of PLD1 in formyl peptide receptor, FPRL1 and FPRL2, function. Function in endocytosis, receptor recycling, and reactivation for receptor activity, overview
physiological function
PLD is a key enzyme involved in secretion, endocytosis and receptor signalling with importance of PLD2 in formyl peptide receptor, FPRL1 and FPRL2, function. Function in endocytosis, receptor recycling, and reactivation for receptor activity, overview
physiological function
-
PLD is activated by Rho family G-protein RhoB or C, which facilitates dopamine-induced Na+ current response in neurons, overview
physiological function
-
PLD is especially involved in regulating biosynthesis and metabolism of phospholipids. Role of phospholipase D in amyloid-beta protein precursor, APP, trafficking, amyloid-beta protein generation, and in signaling mechanisms downstream of beta-amyloid as well as in the trafficking and processing of amyloid precursor protein. PLD1 positively regulates the delivery of PS1 to the cell surface in an APP-independent fashion. Role of the PLD pathway in brain regulation, PLD function, overview
physiological function
-
PLD is involved in stress fiber formation
physiological function
-
PLD may play a role in mitosis through the production of diacylglycerol, phosphatidic acid, and lysophosphatidic acid
physiological function
-
PLD mediates amyloid beta peptides endocytosis into glial cells, and ERK1/2 phosphorylation by a formyl-peptid-receptor-like 1, FPRL1, agonists in glial cells
physiological function
-
PLD serves as a sigalling intermediate for activation of matrix metalloproteinase 9, MMP-9, that is critical in digesting the extracellular matrix and has a vital function in tumor metastasis and invasion, overview. PKC-dependent activation of MMP-9 in fibrosarcoma cells requires PLD activity
physiological function
-
PLD1 controls Rap1 trafficking and regulates Rap1 activity, a small GTPase that modulates adhesion of T cells by regulating inside-out signaling through LFA-1, by controlling exocytosis of a stored, vesicular pool of Rap1 that can be activated by C3G upon delivery to the plasma membrane, overview. Inside-out signaling through Rap1 requires PLD1. PLD1 resides on the same vesicles as Rap1, is delivered along with Rap1 to the plasma membranes of stimulated T cells, and is required for Rap1 activation and T-cell adhesion
physiological function
-
PLD2 is involved in activation of phosphorylation of focal adhesion kinase, and it plays a role in spreading and elongation of cells. Active PLD2 enhances FAK phosphorylation, Akt activation, and cell invasion in EL4 lymphoma cells, overview
physiological function
-
PLD2 plays the role of master regulator and in an ill-defined manner regulates Rho function, PLD1 activity is downstream of this activation, however the generated phosphatidic acid controls changes in cytoskeletal organisation through its regulation of phosphatidylinositol-4-phosphate-5-kinase activity, overview. Regulatory mechanisms of PLD1 and PLD2 cellular activities, overview
physiological function
-
PLD2 plays the role of master regulator and in an ill-defined manner regulates Rho function, PLD1 activity is downstream of this activation, however the generated phosphatidic acid controls changes in cytoskeletal organisation through its regulation of phosphatidylinositol-4-phosphate-5-kinase activity, overview. Regulatory mechanisms of PLD1 and PLD2 cellular activities, overview
physiological function
-
PLD2 plays the role of master regulator and in an ill-defined manner regulates Rho function, PLD1 activity is downstream of this activation, however the generated phosphatidic acid controls changes in cytoskeletal organisation through its regulation of phosphatidylinositol-4-phosphate-5-kinase activity, PLD2 master regulator model, overview. Relation between PLD activation and cytoskeletal remodelling, PLD signalling during cell adhesion, PLD regulation of integrin adhesiveness, cell spreading, and of actin polymerisation during cell spreading, regulation of of stress fibre formation, regulatory mechanisms of PLD1 and PLD2 cellular activities, overview. PLD signalling regulates actin-myosin contractility necessary for cell spreading
physiological function
-
PLD2 promotes an early and sustained increase in ERK1/2 phosphorylation in recombinant T-cell lines, which is inhibited by 1-butanol.
physiological function
-
PLDepsilon and phosphatidic acid promote organism growth and play a role in nitrogen signaling. The lipid-signaling process may play a role in connecting membrane sensing of nutrient status to increased plant growth and biomass production
physiological function
-
polymorphonuclear neutrophil stimulation with fMLP stimulates small G proteins such as ADP-ribosylation factors Arf1 and Arf6, leading to phospholipase D activation and functions such as degranulation and the oxidative burst, regulation, overview
physiological function
-
role for PLD1-induced diacylglycerol as a competent second messenger at the mitochondria that relays ROS to PKD1-mediated mitochondria-to-nucleus signaling, overview
physiological function
-
Role of PLD in the production of diacylglycerol, overview. Possible role for PLD in facilitating the fission of vesicles from the trans-Golgi network which are targeted to the embryonic cortex, and it is required for fusion of vesicles into the plasma membrane, overview
physiological function
-
role of PLD in the production of diacylglycerol, overview. Role of phospholipase D at the Golgi apparatus, overview
physiological function
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role of PLDalpha1 in promoting abscisic acid sensitivity and stomatal closure. PLDalpha1 and phosphatidic acid regulate stomatal closure via a bifurcating pathway and interacts with the Galpha1 subunit of the heterotrimeric G protein to inhibit stomatal opening. PLDalpha1-derived phosphatidic acid binds to ABI1, a protein phosphatase 2C, that functions as a negative regulator in the abscisic acid signaling pathway, overview
physiological function
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roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner
physiological function
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roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner
physiological function
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roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner
physiological function
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roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner
physiological function
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roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner
physiological function
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roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner
physiological function
-
the phospholipid degrading PLD plays an important role in regulation of cytoskeleton remodelling
physiological function
-
the PLD1 protein in the heart is strongly associated with the early postnatal development of the heart in rats. Isozyme PLD1, but not PLD2, is the major PLD isozyme involved in the natal and postnatal development of the rat heart
physiological function
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vesicular trafficking such as macropinocytosis is a dynamic process that requires coordinated interactions between specialized proteins and lipids that involves PLD and its physiological activator, the fission protein CtBP1/BARS in agonist-induced macropinocytosis, overview. Molecular mechanisms of lipid remodelling regulation during macropinocytosis. PLD-catalysed PtdOH formation may be necessary for EGF-induced macropinocytosis
physiological function
-
D type phospholipases are enzymes that hydrolyze the head group of phospholipids to produce phosphatidic acid
physiological function
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OsPLDalpha is involved in salt tolerance in rice through the mediation of H+-ATPase activity and transcription
physiological function
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phospholipase D is involved in myogenesis, process modelling with PLD requirement for cell differentiation. PLD is required for S6K1 phosphorylation both the long (p85) and short (p70) S6K1 isoforms are phosphorylated in a PLD1-dependent way, vasopressin stimulation also induces phosphorylation of Akt on Ser-473 through PLD1-dependent activation of mTORC2 complex. Under differentiating conditions, mTORC2 and Akt are activated in a PLD-dependent way. Regulation of mTOR by PLD and myogenic differentiation, overview
physiological function
-
phospholipase Dalpha is involved in fruit development
physiological function
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PLDalpha1 promotes stomatal closure and reduces water loss. PLDalpha1 and PLDdelta are involved in seedling tolerance to salt stress. PLDalpha3 and PLDepsilon enhance plant growth and hyperosmotic tolerance. The different PLDs regulate the production of phosphatidic acid that is a key class of lipid mediators in plant response to environmental stresses. PLD-produced phosphatidic acids and its molecular targets in hyperosmotic stress responses, overview. PLDdelta plays a role in plant response to reactive oxygen species, dehydration, and salt stresses, while PLDepsilon plays a role in N signalling and plant growth under salt stress and water deficiency, and PLDalpha3 in salt and mild drought responses
physiological function
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PldB regulates cAMP chemotaxis, overview. Phospholipase D controls Dictyostelium development by regulating G protein signaling, its activity is required for CMF to alter the kinetics of cAMP-induced G protein signaling, overview
physiological function
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role of a phospholipase D-related signaling pathway in insulin secretion caused by high glucose in the pancreatic beta-cell line MIN6N8
physiological function
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involvement of the enzyme in the receptor endocytosis and recycling of many G-protein coupled receptors e.g., opioid, formyl or dopamine receptors. The enzyme plays an important function in cell regulation and receptor trafficking. Protein kinases and GTP binding proteins of the ADP-ribosylation and Rho families regulate the two mammalian PLD isoforms 1 and 2. The enzyme and its product phosphatidic acid are implicated in a wide range of physiological processes and diseases including inflammation, diabetes, oncogenesis or neurodegeneration. Analysis of mechanism and regulation of the enzyme in the context of membrane located G-protein coupled receptor function, overview
physiological function
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isoform PLD2 downregulation decreases the transcription of FoxO3a target genes Cu/Zn superoxide dismutase, Mn superoxide dismutase, catalase, thioredoxin-2, and peroxiredoxin-5, whereas ectopic PLD2 expression elevates the mRNA levels of these antioxidant genes
physiological function
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isoforms PLD1 and PLD2 regulate different steps in mast cell degranulation. PLD1 deficiency impairs FcepsilonRI-mediated mast cell degranulation while PLD2 deficiency enhances it. PLD deficiency affects activation of the phosphoinositide 3-kinase pathway and RhoA. Although PLD1 deficiency impairs F-actin disassembly, PLD2 deficiency enhances microtubule formation
physiological function
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photoreceptors contain a light-dependent phospholipase D activity. During illumination, loss of PLD results in an enhanced reduction in rhabdomere size, accumulation of Rab7 positive, rhodopsin1-containing vesicles in the cell body and reduced rhodopsin protein, associated with reduced levels of phosphatidic acid. In wild-type photoreceptors, during illumination, enhanced PLD activity is sufficient to clear rhodopsin1-containing vesicles from the cell body by a process dependent on Arf1-GTP levels and retromer complex function
physiological function
reconstitution of human PLD1 is able to completely rescue retinal degeneration in a loss of function Drosophila PLD mutant. PLD1 is unable to restore the levels of a subset of unique species of phosphatidic acid in Drosophila. Both Drosophila PLD and human PLD1 are uniquely distributed to the subplasma membrane region in photoreceptors
physiological function
reconstitution of human PLD2 is only partly able to rescue retinal degeneration in a loss of function Drosophila PLD mutant. PLD2 is unable to restore the levels of a subset of unique species of phosphatidic acid in Drosophila. Contrary to the Drosophila enzyme, isoform PLD2 does not localize with subplasma membrane actin
physiological function
red clover necrotic mosaic virus RCNMV RNA replication complexes formed in Nicotiana benthamiana contain isoforms PLDalpha and PLDbeta. PLDs and PLDs-derived phosphatidic acid are required for viral RNA replication. Exogenous application of phosphatidic acid enhances viral RNA replication in plant cells and plant-derived cellfree extracts. A viral auxiliary replication protein binds to phosphatidic acid in vitro, and the amount of phosphatidic acid increases in RCNMV-infected plant leaves
physiological function
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The effects of phospholipase D activity and its product phosphatidic acid on the Ca2+ sensitivity and rate of fusion in late exocytosis correlate with modulatory upstream roles in docking and priming rather than to direct effects on fusion per se
physiological function
EXJ48329
the loop structure (amino acids 1-25) in the N-terminal segment of PLD has a positive effect on the binding to phospholipid monolayers, especially to 1,2-dimyristoyl-sn-glycero-3-phosphoserine and 1,2-dimyristoyl-sn-glycero-3-phosphocholine. The deletion of the helix structure (amino acids 26-34) basically has no influence on the binding to phospholipid monolayers. The deletion of the C-terminal amino acids 434-487 does not significantly change the binding selectivity of PLD for the various phospholipid monolayer tested here. The three-strand segment (amino acids 434-469) has a great negative effect on the interfacial binding to the phospholipid monolayers
physiological function
the mRNA level of Pld-1 is inversely correlated with aging. RNAi-mediated knockdown of Pld-1 expression in nematodes enhances reactive oxygen species and lipofuscin accumulation and decreases lifespan, motility, and resistance to stress. Pld-1 knockdown represses the long lifespan of age-1 and akt-1 mutants but does not further reduce the lifespan of daf-16 mutants. The reactive oxygen species scavenger N-acetyl-L-cysteine attenuates the lifespan shortening and age-related biomarkers triggered by pld-1 knockdown. Pld-1 RNAi downregulates the expression of daf-16 target genes such as sod-3, dod-11, and mtl-1 in nematodes
physiological function
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PldB regulates cAMP chemotaxis, overview. Phospholipase D controls Dictyostelium development by regulating G protein signaling, its activity is required for CMF to alter the kinetics of cAMP-induced G protein signaling, overview
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additional information
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stimulation of the serotonin 5-HT2A receptor and the angiotensin II receptor, AT1AR, two G-protein-coupled receptors, leads to their sequestration from endosomes to into a Rab11-positive juxtanuclear compartment in a PKC- and PLD-dependent manner, detailed overview. The PKC- and PLD-dependent sequestration of receptors results in co-sequestration of other plasma membrane proteins and receptors, e.g. of epidermal growth factor receptor and protease activated receptor-1
additional information
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both PLD isozymes associate with membrane receptors including G-protein coupled receptors, receptor tyrosine kinases or integrins, which all mediate signalling of PLD activation
additional information
change of the PLD structure upon phospholipid binding, conformational change of the gate-like structure formed by the two loops around Y126 and G381, residues, W187, Y191 and Y385 are responsible for head group specificity, structure overview
additional information
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the conserved glycine-glycine (GG) and glycine-serine (GS) motifs, especially the Ser residue, in the Streptoverticillium cinnamoneum enzyme are essential in affecting transphosphatidylation activity. The motifs are located seven residues downstream of the HKD motifs, in a close proximity to the catalytic histidines. The GG/GS motifs are suggested to maintain local conformation of the active site by positioning the catalytic His through the hydrogen bond network
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DELTA1-158
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PLD with a deleted regulatory C2 domain exhibits Ca2+-dependent activity, is much less active and requires a higher level of Ca2+ than the full-length enzyme PLDbeta
R399P
complete loss of activity
R611D
loss of more than 80% of phosphatidylinositol-stimulated activity, 50% of oleate-stimulated activity
A426F
less than 1% of wild-type activity with substrate phosphatidyl-p-nitrophenol
C310S
-
significant increase in total and transphosphatidylation activity
C625S
-
significant increase in total and transphosphatidylation activity
H443A
less than 1% of wild-type activity with substrate phosphatidyl-p-nitrophenol
L483H
less than 1% of wild-type activity with substrate phosphatidyl-p-nitrophenol
D389N
-
single nucleotide polymorphism, activity comparable to wild-type
F250S
-
dramatic reduction of enzyme activity
G901D
naturally occuring polymorphism, mutation results in catalytically inactive protein
H380R
-
single nucleotide polymorphism, complete loss of activity
K228R
-
dramatic reduction of enzyme activity
L207F
-
single nucleotide polymorphism, complete loss of activity
R128K
-
isoform PLD1, mutation in phox homology domain, reduction in activation of GTPase, unable to increase endocytosis of epidermal growth factor receptor
R145K
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isoform PLD1, mutation in phox homology domain, reduction in activation of GTPase, unable to increase endocytosis of epidermal growth factor receptor
R165K
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isoform PLD1, mutation in phox homology domain, reduction in activation of GTPase, unable to increase endocytosis of epidermal growth factor receptor
R197K
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isoform PLD1, mutation in phox homology domain, reduction in activation of GTPase, unable to increase endocytosis of epidermal growth factor receptor
S152A
-
single nucleotide polymorphism, activity comparable to wild-type
S230F
-
dramatic reduction of enzyme activity
W253C
-
almost complete loss of enzyme activity
K898R
-
catalytically inactive mutant of PLD1
R179A
-
mutation disrupts binding of the activator phosphatidylinositol 3,4,5-triphosphate
R179K
-
mutation disrupts binding of the activator phosphatidylinositol 3,4,5-triphosphate
N232A
site-directed mutagenesis of isozyme PLDbeta1, leads to reduced actin and G-protein binding
N323A/T382A
site-directed mutagenesis of isozyme PLDbeta1, leads to reduced actin and G-protein binding
T382A
site-directed mutagenesis of isozyme PLDbeta1, leads to reduced actin and G-protein binding
A349E/E352Q
strong suppression of hydrolysis and an increase in the transphosphatidylation activity
367stop
-
complete loss of activity
377stop
-
complete loss of activity
387stop
-
activity comparable to wild-type
C170S
-
activity comparable to wild-type
C222S
-
activity comparable to wild-type
C224S
-
considerable reduction in activity
C237S
-
activity comparable to wild-type
C255S
-
activity comparable to wild-type
C288S
-
activity comparable to wild-type
D147N
-
complete loss of activity
D189N
-
less than 0.1% of wild-type activity
D284N
-
complete loss of activity
DELTAN138
-
complete loss of activity
DELTAN55
-
activity comparable to wild-type
DELTAN85
-
complete loss of activity
H185N
-
less than 0.1% of wild-type activity
H187N
-
less than 0.1% of wild-type activity
H190N
-
less than 0.1% of wild-type activity
H253N
-
complete loss of activity
H321N
-
complete loss of activity
H331N
-
4% of wild-type activity
H343N
-
activity comparable to wild-type
H353N
-
activity comparable to wild-type
H380R
-
single nucleotide polymorphism, low catalytic activity
L207F
-
single nucleotide polymorphism, low catalytic activity
E134P/G195S
mutant displays increased actiity with N-hexanoyl-D-erythrosphingosylphosphorylcholine but still prefers ethanolamine substrates over choline substrates
D40H/T291Y
site-directed mutagenesis of residues D40 and T291 located within dynamic surface loops, the mutant is able to synthesize phosphatidylinositol by transphosphatidylation
D40H/W187D/Y191Y/R329G/Y385R
random mutagenesis of mutant W187D/Y191Y/Y385R, the resulting mutant shows increased thermostability compared to the wild-type enzyme and transphosphatidylation with myo-inositol and phosphocholine
D40H/W187D/Y191Y/T291Y/R329G/Y385R
random mutagenesis of mutant W187D/Y191Y/Y385R, the resulting mutant shows increased thermostability compared to the wild-type enzyme and transphosphatidylation with myo-inositol and phosphocholine
D40H/W187D/Y191Y/T291Y/Y385R
random mutagenesis of mutant W187D/Y191Y/Y385R, the resulting mutant shows increased thermostability compared to the wild-type enzyme and transphosphatidylation with myo-inositol and phosphocholine
W187D/Y191Y/T291Y/R329G/Y385R
random mutagenesis of mutant W187D/Y191Y/Y385R, the resulting mutant shows increased thermostability compared to the wild-type enzyme and transphosphatidylation with myo-inositol and phosphocholine
W187F/Y191R
mutant enzyme is able to synthesize phosphatidylinositol using dioleoyl-phosphatidylcholine and myo-inositol as a substrate, the mutant enzyme generates a mixture of structural isomers of phosphatidylinositol with the phosphatidyl groups connected at different positions of the inositol ring. In the cases of 1,2-diols, triols, and myo-inositol mutant W187F/Y191R generates the corresponding transphosphatidylated products more efficiently than wild-type. The phosphatidylcholine-hydrolyzing activity of the mutant PLD is much lower than that of the wild-type enzyme (Km higher, Vmax much lower than wild-type). Mutant enzyme is able to transphosphatidylate various cyclohexanols with a preference for bulkier compounds
W187N/Y191Y/Y385R
mutant generates phosphatidylinositol as a mixture of 1-phosphatidylinositol and 3-phosphatidylinositol in the ratio of 76/24
W187X/Y191X/Y385X
mutations are introduced in the pld gene at the positions corresponding to three amino acid residues that might be involved in substrate recognition, and the mutated genes are expressed in Escherichia coli. High-throughput screening of approximately 10000 colonies for phosphatidylinositol-synthesizing activity identifies 25 phosphatidylinositol-synthesizing mutant PLDs
Y385R
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the mutation contributes to the selectivity for the 1(3)-PI synthesis
C123A
enzymatically inactive, secondary structure and thermostability similar to wild type
C123S
enzymatically inactive, secondary structure and thermostability similar to wild type
H171A
17% of wild type activity
H187A
dramatic decrease in activity
H200A
dramatic decrease in activity
H266A
17% of wild type activity, activation by phosphatidic acid up to 12fold
G215S
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site-directed mutagenesis of the GG/GS motifs resulting in a several fold enhancement in transphosphatidylation activity
G216S
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site-directed mutagenesis of the GG/GS motifs resulting in a several fold enhancement in transphosphatidylation activity
G216S/S489G
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site-directed mutagenesis of the GG/GS motifs resulting in a several fold enhancement in transphosphatidylation activity
H167N
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site-directed mutagenesis of a catalytic residue, the activity of the variant is completely lost even if the protein does not present any significant structural modification
H440N
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site-directed mutagenesis of a catalytic residue, the activity of the variant is completely lost even if the protein does not present any significant structural modification
K169S
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site-directed mutagenesis of a catalytic residue, the activity of the variant is completely lost even if the protein does not present any significant structural modification
K442S
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site-directed mutagenesis of a catalytic residue, the activity of the variant is completely lost even if the protein does not present any significant structural modification
D16A
caspase 3 cleavage motif mutant of isozyme PLD2
D16A
site-directed mutagenesis of isozyme PLD2D16A, the mutant shows altered cleavage by caspase 3 compared to the wild-type enzyme
D28A
caspase 3 cleavage motif mutant of isozyme PLD2
D28A
site-directed mutagenesis of isozyme PLD2D28A, the mutant does not show altered cleavage by caspase 3 compared to the wild-type enzyme
K758R
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catalytically inactive. Inhibition of enzyme activity by overexpression of the mutant blocks the constitutive isoform PLD2 activation and impairs the endocytosis of my-opioid receptors MOR1D
K758R
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catalytically inactive mutant of isozyme PLD2
K898R
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catalytically inactive mutant of isozyme PLD1
K898R
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catalytically inactive PLD1 mutant
K758R
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catalytically inactive mutant of PLD2
K758R
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catalytically inactive PLD2 mutant
W187D/Y191Y/Y385R
site-directed mutagenesis, the mutant is able to synthesize phosphatidylinositol by transphosphatidylation, thermostabilization of enzyme mutant W187D/Y191Y/Y385R, termed DYR, is attempted by rational design based on deletion of the D40 loop, generating two variants, DELTA37-45 DYR and DELTA38-46 DYR PLD. DELTA38-46 DYR shows highest thermostability as its activity half-life at 70°C proves 11.7 and 8.0 times longer than that of the DYR mutant and mutant DELTA37-45 DYR, respectively, molecular dynamics, overview
W187D/Y191Y/Y385R
site-directed mutagenesis, the mutant synthesizes phosphatidylinositol from myo-inositol and phosphocholine by transphosphatidylation
W187N/Y191Y/Y385R/G186T
mutant generates phosphatidylinositol as a mixture of 1-phosphatidylinositol and 3-phosphatidylinositol in the ratio of 87/13 and of 97/3 at 20°C, respectively
W187N/Y191Y/Y385R/G186T
mutant generates phosphatidylinositol as a mixture of 1-phosphatidylinositol and 3-phosphatidylinositol in the ratio of 93/7 at 37°C and of 97/3 at 20°C, respectively
A426F/L438H
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mutation in residues located in the c-terminal flexible loop. Increase in activities and increase in thermotolerance and tolerance against organic solvents
A426F/L438H
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mutation in residues located in the c-terminal flexible loop. Increase in activities and increase in thermotolerance and tolerance against organic solvents
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additional information
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generation of an Acinetobacter baumannii strain 98-37-09 transposon mutant library using the EZ-Tn5 R6Kori/KAN-2 Tnp transposome system, construction of the ACJ2, A1S_2989 mutant. Disruption of phospholipase D causes a reduction in the organism's ability to thrive in serum, a deficiency in epithelial cell invasion, and diminished pathogenesis in a murine model of pneumonia
additional information
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construction of GST fusion proteins containing parts of the enzyme, identification of a phosphatidylinositol-binding region, deletion of this region abolishes enzyme activity
additional information
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enzyme suppressed ecotype, mechanical wounding of leaves results in significantly less hydrolysis of phosphatidylcholine than in wild type, phospholipid acyl composition in wild type and enzyme-suppressed mutants
additional information
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expression and characterization of putative C2 domains and structural features
additional information
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disruption of isoforms PLDzeta2 and PLDzeta1 function results in a smaller decrease in phosphatidylcholine and a smaller increase in digalactosyldiacylglycerol in phosphorus-starved roots
additional information
enzyme-deficient mutant shows proliferation of membranes inside the vacuole
additional information
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enzyme-deficient mutant shows proliferation of membranes inside the vacuole
additional information
Atpldalpha 1 and AtPLDdelta single and double knock-out mutants exhibit enhanced sensitivity to high salinity stress in a plate assay. Both PLDs are activated upon dehydration and the knock-out mutants are hypersensitive to hyperosmotic stress, displaying strongly reduced growth
additional information
Atpldalpha 1 and AtPLDdelta single and double knock-out mutants exhibit enhanced sensitivity to high salinity stress in a plate assay. Both PLDs are activated upon dehydration and the knock-out mutants are hypersensitive to hyperosmotic stress, displaying strongly reduced growth
additional information
knockout and overexpression of PLDalpha3 alter plant response to salinity and water deficit. Alterations of PLDalpha3 result in changes in phosphatidic acid level and membrane lipid composition. PLDalpha3-knockout plants display increased sensitivities to salinity and water deficiency and also tend to induce abscisic acid-responsive genes more readily than wild-type plants, whereas PLDalpha3-overexpressed plants have decreased sensitivities. PLDalpha3-knockout plants flower later than wild-type plants in slightly dry conditions, whereas PLDalpha3-overexpressed plants flower earlier
additional information
knockout and overexpression of PLDalpha3 alter plant response to salinity and water deficit. Alterations of PLDalpha3 result in changes in phosphatidic acid level and membrane lipid composition. PLDalpha3-knockout plants display increased sensitivities to salinity and water deficiency and also tend to induce abscisic acid-responsive genes more readily than wild-type plants, whereas PLDalpha3-overexpressed plants have decreased sensitivities. PLDalpha3-knockout plants flower later than wild-type plants in slightly dry conditions, whereas PLDalpha3-overexpressed plants flower earlier
additional information
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knockout and overexpression of PLDalpha3 alter plant response to salinity and water deficit. Alterations of PLDalpha3 result in changes in phosphatidic acid level and membrane lipid composition. PLDalpha3-knockout plants display increased sensitivities to salinity and water deficiency and also tend to induce abscisic acid-responsive genes more readily than wild-type plants, whereas PLDalpha3-overexpressed plants have decreased sensitivities. PLDalpha3-knockout plants flower later than wild-type plants in slightly dry conditions, whereas PLDalpha3-overexpressed plants flower earlier
additional information
PLD activity during the wounding response is restricted to the ruptured cells using 32P-labelled phospholipid analyses of Arabidopsis pld knock-out mutants and PLD-silenced tomato cell-suspension cultures. plda1 knock-out lines have reduced wounding-induced phosphatidic acid production, and the remainder is completely eliminated in a plda1/d double knock-out line
additional information
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gene pldzeta2 mutations significantly retard or disturb root hydrotropic responses, but cause no morphological abnormality, inhibitory effect of abscisic acid on gravitropism is affected in pldf2 mutant roots. Construction of transgenic Arabidopsis thaliana plants expressing the isozyme via transfection by Agrobacterium tumefaciens LBA4404
additional information
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isozyme PLDdelta-KO cells exhibit a higher rate of H2O2-induced cell death than the wild-type. Unlike PLDalpha1-KO plants, PLDdelta-KO plants are still able to produce the normal levels of reactive oxygen species in response to stresses, such as abscisic acid and freezing. The stomata in epidermal peels from PLDalpha1-deficient Arabidopsis thaliana plants fail to close in response to abscisic acid, whereas external supply of phosphatidic acid, the lipid product of PLD, promotes the stomatal closure in wild-type and PLDalpha1-deficient Arabidopsis thaliana plants. PLDalpha3-KO plants accumulate a similar level of abscisic acid as the wild-type, but display higher levels of abscisic acid response gene expression. The root growth of PLDalpha3-KO seedlings is also more inhibited by abscisic acid treatment than wild-type
additional information
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knockout of PLDepsilon decreases root growth and biomass accumulation, whereas overexpression of PLDepsilon enhances root growth and biomass accumulation. Increased expression of PLDepsilon also promotes root hair elongation and primary root growth under severe nitrogen deprivation. Growth phenotypes of PLDepsilon mutant seedlings under different conditions, detailed overview
additional information
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Nicotiana tabacum transgenic plants, overexpressing Arabidopsis thaliana isozyme PLDalpha1, display more susceptibility to drought than control plants, drought also induces an increase in PLDa1 activity. High level of PLDalpha1 activity is correlated to membrane degradation in late stages of drought, as demonstrated by ionic leakage and lipid peroxidation. Recombinant PLD2 promotes stomatal closure at earlier stages, but disrupts membranes in prolonged drought stress, phenotype, overview
additional information
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PLDalpha3-knockout plants are less tolerant to salt stress than wild-type plants. In addition, under water deficit conditions, PLDalpha3-KO plants flower later, whereas PLDalpha3-overexpressing plants flower earlier than wild-type plants. PLDalpha3-KO seeds and seedlings are less sensitive to glucose, whereas overexpression of PLDalpha3 enhances glucose sensitivity compared to the wild-type
additional information
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creation of 35 enzyme variants bearing mutations in the two HKD motifs, the C-terminus, or the eight cysteine resiudes. Analysis of transphosphatidylation activity and hydrolytic activity of mutants. All positions tested prove to be very sensitive towards amino acid exchanges with respect to hydrolytic activity in the absence of glycerol as well as to the ratio of hydrolytic and transphosphatidylation activities in the presence of glycerol
additional information
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generation of mosaic pld1 deficient embryos, that show partial suppression of intersegmental vessel defects in the segments containing transplanted wild-type somitic and notochord cells, or notochord cells alone. 1-Butanol treatment phenocopies the ISV defects of pld1 morphants, overview. The early chordamesoderm marker shh is normally downregulated in pld1 morphants or 1-butanol treated embryos, ths notochord differentiation is not affected when Pld1 function is disrupted. No changes in VEGF and semaphorins 3a1 expressions
additional information
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construction of a pldB disruption mutant by nucleotide replacement
additional information
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construction of a pldB disruption mutant by nucleotide replacement
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additional information
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enzyme is required for cellularization, i.e. A form of cytokinesis in which polarized membrane extension proceeds in part through incorporation of new membrane via fusion of apically-translocated Golgi-derived vesicles. Loss of enzyme activity frequently leads to early embryonic developmental arrest. Chronic enzyme deficiency causes abnormal Golgi structure and secretory vesicle trafficking
additional information
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in Drosophila, the absence of PLD is lethal by preventing embryonic cellularization and causes abnormal Golgi apparatus structure and vesicle trafficking
additional information
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deletion of pleckstrin homology domain, disruption of normal cellular localization, loss of enzyme activity
additional information
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deletion of the phox homology domain in isoforms PLD1 or PLD2 results in reduction in activation of GTPase, mutants are unable to increase endocytosis of epidermal growth factor receptor. Silencing of enzymes expression retard endocytosis of epidermal growth factor
additional information
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depletion of enzyme by siRNA in macrophages results in significant inhibition of phagocyte adhesion and is accompanied by reductions in total cellular F-actin
additional information
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expression of wild-type and catalytically inactive enzyme isoforms in HeLa-MAGI cells enhances and inhibits the LTR activation, respectively, without altering Tat expression. Wild-type and inactive enzyme isoforms also respectively potentiate and inhibit HIV-1BAL replication in MAGI cells
additional information
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induction of apoptosis by co-treatment using tumor necrosis factor alpha and cycloheximide induces enzyme activity after 1 h whereas both enzyme activity and isoform PLD1 protein are strongly decreased after 24 h. Tumor necrosis factor alpha/cycloheximide-induced cell death is significantly lowered in cells overexpressing isoform PLD1 or by exogenous bacterial enzyme. Cells depleted in enzyme proteins by siRNA treatment exhibit higher susceptibility to apoptosis
additional information
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overexpression of enzyme isozymes in SNU 4784 cancer cell results in inhibition of taxotere-induced apoptotic cell death, accompanied by up-regulated expression of Bcl-2 and inhibited taxotere-induced activation of procaspase 3. Selective inhibition of phospholipase by specific siRNa leads to exacerbation of taxotere-induced apoptosis
additional information
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overexpression of isoform PLD1, but not PLD2, results in increased procollagen I production in dermal fibroblast. Reduction of isoform PLD1 expression by siRNA is accompanied by diminution of procollagen biosynthesis and also ribosomal S6 kinase 1 phosphorylation
additional information
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overexpression of isoforms PLD1 and PLD2, but not their inactive mutants, stimulates Co2+-induced COX-2 expression and prostaglandin E2 production. PLD1 enhances COX-2 expression by Co2+ via reactive oxygen species, p38 MAK kinase, PKC-delta, and PKA, but not ERK, whereas PLD2 enhances Co2+-induced COX-2 expression via reactive oxygen species and p38 MAP kinase, but not PKC-delta, PKA and ERK
additional information
overexpression of isoforms PLD1 and PLD2, but not their inactive mutants, stimulates Co2+-induced COX-2 expression and prostaglandin E2 production. PLD1 enhances COX-2 expression by Co2+ via reactive oxygen species, p38 MAK kinase, PKC-delta, and PKA, but not ERK, whereas PLD2 enhances Co2+-induced COX-2 expression via reactive oxygen species and p38 MAP kinase, but not PKC-delta, PKA and ERK
additional information
overexpression of isoforms PLD1 and PLD2, but not their inactive mutants, stimulates Co2+-induced COX-2 expression and prostaglandin E2 production. PLD1 enhances COX-2 expression by Co2+ via reactive oxygen species, p38 MAK kinase, PKC-delta, and PKA, but not ERK, whereas PLD2 enhances Co2+-induced COX-2 expression via reactive oxygen species and p38 MAP kinase, but not PKC-delta, PKA and ERK
additional information
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silencing of isoform PLD1 by siRNA leads to an abolishment of basal chemokinesis of HL-60 cells that cannot be rescued with chemoattractants ENA-78, FMLP, and IL-8. Transient overexpression of PLD1 increases both chemokinesis and chemotaxis toward IL-8 and FMLP but not toward ENA-78. Chemokinesis is not mediated by the enzymatic activity of PLD1, but the chemotactic response is
additional information
silencing of isoform PLD1 by siRNA leads to an abolishment of basal chemokinesis of HL-60 cells that cannot be rescued with chemoattractants ENA-78, FMLP, and IL-8. Transient overexpression of PLD1 increases both chemokinesis and chemotaxis toward IL-8 and FMLP but not toward ENA-78. Chemokinesis is not mediated by the enzymatic activity of PLD1, but the chemotactic response is
additional information
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silencing of isoform PLD2 by siRNA leads to cell migration arrest, whereas ENA-78 selectively increases endogenous PLD2 activity and chemotaxis of HL-60 cells overexpressing enzyme
additional information
silencing of isoform PLD2 by siRNA leads to cell migration arrest, whereas ENA-78 selectively increases endogenous PLD2 activity and chemotaxis of HL-60 cells overexpressing enzyme
additional information
by PLD RNAi experiments it is shown that PLD activity is required for integrin-mediated cell spreading. RNAi targeting PLD1 or PLD2, or both isoforms reduces integrin-mediated phosphatidic acid. In correlation with phosphatidic acid generation, PLD knockdown reduces cell spreading which is restored by direct phosphatidic acid treatment
additional information
by PLD RNAi experiments it is shown that PLD activity is required for integrin-mediated cell spreading. RNAi targeting PLD1 or PLD2, or both isoforms reduces integrin-mediated phosphatidic acid. In correlation with phosphatidic acid generation, PLD knockdown reduces cell spreading which is restored by direct phosphatidic acid treatment
additional information
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reduction of endogenous PLD1 expression using RNAi markedly inhibits the secretion of von Willebrand factor from histamine-stimulated HUVECs. PLD2 knockdown on the other hand shows no effect
additional information
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reduction of endogenous PLD2 shows no effect towards the secretion of von Willebrand factor from histamine-stimulated HUVECs
additional information
using antisense oligonucleotides to PLD1 and PLD2, respectively, it is shown that TNFalpha stimulates PLD1 and not PLD2. Furthermore, it is shown that PLD1 is required for the activation of sphingosine kinase and cytosolic calcium signals and for NFkappaB and ERK1/2 activation. PLD1 is required for TNF-alpha-induced production of several important cytokines, such as IL-1beta, IL-5, IL-6, and IL-13, in human monocytes
additional information
using antisense oligonucleotides to PLD1 and PLD2, respectively, it is shown that TNFalpha stimulates PLD1 and not PLD2. Furthermore, it is shown that PLD1 is required for the activation of sphingosine kinase and cytosolic calcium signals and for NFkappaB and ERK1/2 activation. PLD1 is required for TNF-alpha-induced production of several important cytokines, such as IL-1beta, IL-5, IL-6, and IL-13, in human monocytes
additional information
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using antisense oligonucleotides to PLD1 and PLD2, respectively, it is shown that TNFalpha stimulates PLD1 and not PLD2. Furthermore, it is shown that PLD1 is required for the activation of sphingosine kinase and cytosolic calcium signals and for NFkappaB and ERK1/2 activation. PLD1 is required for TNF-alpha-induced production of several important cytokines, such as IL-1beta, IL-5, IL-6, and IL-13, in human monocytes
additional information
using antisense oligonucleotides to PLD1 and PLD2, respectively, it is shown that TNFalpha stimulates PLD1 and not PLD2. Furthermore, it is shown that PLD1, and not PLD2, is required for the activation of sphingosine kinase and cytosolic calcium signals and for NFkappaB and ERK1/2 activation
additional information
using antisense oligonucleotides to PLD1 and PLD2, respectively, it is shown that TNFalpha stimulates PLD1 and not PLD2. Furthermore, it is shown that PLD1, and not PLD2, is required for the activation of sphingosine kinase and cytosolic calcium signals and for NFkappaB and ERK1/2 activation
additional information
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using antisense oligonucleotides to PLD1 and PLD2, respectively, it is shown that TNFalpha stimulates PLD1 and not PLD2. Furthermore, it is shown that PLD1, and not PLD2, is required for the activation of sphingosine kinase and cytosolic calcium signals and for NFkappaB and ERK1/2 activation
additional information
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interleukin-2 production evoked by PMA/ionomycin stimulation or CD3/CD28 engagement is enhanced in the two T-cell lines overexpressing PLD2. hPLD2 overexpression results in an increase of ERK1/2 phosphorylation by about 50% within 60 min
additional information
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knockdown of isozyme PLD2 by two independent shRNAs has no effect on Rheb activation of S6K1
additional information
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overexpression of phospholipase D enhances matrix metalloproteinase-2 expression and glioma cell invasion via protein kinase C and protein kinase A/NF-kappaB/Sp1-mediated signaling pathways
additional information
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PLD1 knockdown in Jurkat cells, silencing PLD1 but not PLD2 expression with shRNA inhibits plasma membrane localization of GFP-Rap1
additional information
PLD1 silencing by siRNA in HT-29 cells affects formyl peptide receptor, FPRL1 and FPRL2, activity, overview
additional information
PLD1 silencing by siRNA in HT-29 cells affects formyl peptide receptor, FPRL1 and FPRL2, activity, overview
additional information
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PLD1 silencing by siRNA in HT-29 cells affects formyl peptide receptor, FPRL1 and FPRL2, activity, overview
additional information
PLD1/2 double knockdown reduces surface-induced effects, i.e. the increase of PLD mRNA and activity, osteocalcin and osteoprotegerin, and protein kinase C and alkaline phosphatase specific activities, as well as the decrease of cell number, overview. shRNAs for human PLD1 and PLD2 are used to silence MG63 cells. Wild-type and PLD1 or PLD1/2 silenced cells are cultured on smooth-pretreatment surfaces. PLD is required for the differentiation of osteoblast-like MG63 cells on machined and grit-blasted titanium surfaces, role of PLD in osteoblast response to titanium surface microstructure. PLD silencing affects osteoblast differentiation, inhibition of PLD reduces the effects of surface microstructure/energy on protein kinase C, suggesting that PLD mediates the stimulatory effect of microstructured/high-energy surfaces via PKC-dependent signaling, phenotypes, detailed overview
additional information
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PLD1/2 double knockdown reduces surface-induced effects, i.e. the increase of PLD mRNA and activity, osteocalcin and osteoprotegerin, and protein kinase C and alkaline phosphatase specific activities, as well as the decrease of cell number, overview. shRNAs for human PLD1 and PLD2 are used to silence MG63 cells. Wild-type and PLD1 or PLD1/2 silenced cells are cultured on smooth-pretreatment surfaces. PLD is required for the differentiation of osteoblast-like MG63 cells on machined and grit-blasted titanium surfaces, role of PLD in osteoblast response to titanium surface microstructure. PLD silencing affects osteoblast differentiation, inhibition of PLD reduces the effects of surface microstructure/energy on protein kinase C, suggesting that PLD mediates the stimulatory effect of microstructured/high-energy surfaces via PKC-dependent signaling, phenotypes, detailed overview
additional information
PLD2 silencing by siRNA in HT-29 cells affects formyl peptide receptor, FPRL1 and FPRL2, activity, overview
additional information
PLD2 silencing by siRNA in HT-29 cells affects formyl peptide receptor, FPRL1 and FPRL2, activity, overview
additional information
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PLD2 silencing by siRNA in HT-29 cells affects formyl peptide receptor, FPRL1 and FPRL2, activity, overview
additional information
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siRNA-mediated reduction of endogenous PLD2 expression results in a nearly complete inhibition of the opioid-induced H2O2 production in Rattus norvegicus mu-opioid receptor MOPr-expressing HEK293 cells, while in control cells it has no effect on [D-Ala2,Me Phe4,Glyol5]enkephalin and beta-endorphin effects on the DCFDA fluorescence
additional information
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dominant negative PLD1 inhibits glucose-induced Beta2 expression, and glucose-induced insulin secretion is blocked by treatment with 1-butanol or PLD1-siRNA
additional information
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interleukin-2 production evoked by PMA/ionomycin stimulation or CD3/CD28 engagement is enhanced in the two T-cell lines overexpressing PLD2
additional information
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overexpression of phospholipase D isozymes, leads to downregulation of protein kinase CKII activity via proteasome-dependent CKIIbeta degradation in NIH3T3 cells. Co-localization of CKIIbeta and PLD isozymes in NIH3T3 cells
additional information
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transfection of PLD1, PLD2, and their dominant negative forms into Raw 264.7 cells, only PLD2 overexpression, but not that of PLD1, increases NO synthesis and iNOS expression. LPS-induced NO synthesis and iNOS expression are blocked by PLD2 siRNA, suggesting that LPS upregulates NO synthesis through PLD2. Knockdown of PLD2 with siRNA also decreases phosphorylation of S6K1, p42/44 MAPK and STAT3 induced by LPS
additional information
antisense-mediated knockdown of tobacco pollen PLDs results in inhibition of pollen tube growth
additional information
antisense-mediated knockdown of tobacco pollen PLDs results in inhibition of pollen tube growth
additional information
antisense-mediated knockdown of tobacco pollen PLDs results in inhibition of pollen tube growth
additional information
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antisense-mediated knockdown of tobacco pollen PLDs results in inhibition of pollen tube growth
additional information
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construction of OsPLDbeta1-knockdown plants, that show the accumulation of reactive oxygen species in the absence of pathogen infection, knockdown of OsPLDbeta1 results in the up-/down-regulation of more than 1400 genes, including the induction of defense-related genes such as pathogenesis-related protein genes and WRKY/ERF family transcription factor genes, leading to e.g. hypersensitive response-like cell death and phytoalexin production, or upregulation of defense-related genes and transcriptions factors, quantitative RT-PCR analysis, phenotype, overview
additional information
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construction of OsPLDalpha1 knockdown cell by RNA interference methods
additional information
depletion of both PLD1 and PLD2 isoenzymes using shRNA reduces the velocity of the migration, but depletion of PLD2 inhibits motility more severly than that of PLD1
additional information
depletion of both PLD1 and PLD2 isoenzymes using shRNA reduces the velocity of the migration, but depletion of PLD2 inhibits motility more severly than that of PLD1
additional information
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the inhibition of EGF-induced macropinocytosis caused either by PLD1 or PLD2 knockdown is rescued by the co-expression of the respective wild-type PLD isoforms, whereas the expression of a lipase inactive mutant, lipase-negative (LN)-PLD1 or LN-PLD2, does not restore macropinocytotic activity
additional information
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construction of a partially deleted pld mutant DELTApldt strain, shows reduced virulence in guinea pigs compared to the wild-type strain, phenotype of infection at high and low doses of wild-type and mutant rickettsiae, overview. Inoculation with the DELTApld mutant at low doses confers effective immune protection against the virulent strain in the guinea pig model
additional information
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sec14 mutant, enzyme activity is elevated by 40% at restrictive temperature
additional information
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gene silencing reveals that this PLD is indeed involved in the salt-induced phosphatidic acid production, but not exclusively. Genetically modified tomato plants with reduced LePLDalpha 1 protein levels do not reveal altered salt tolerance
additional information
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the 187H/191Y/385R mutant generates 1-phosphatidylinositol more than 3-phosphatidylinositol, whereas 187T/191Y/385R generates 1-phosphatidylinositol less than 3-phosphatidylinositol
additional information
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the phosphatidylcholine-hydrolyzing activity of the mutant PLD 187F/191R/385Y is much lower than that of the wild-type enzyme, the mutant enzyme is able to transphosphatidylate various cyclohexanols with a preference for bulkier compounds
additional information
the phosphatidylcholine-hydrolyzing activity of the mutant PLD 187F/191R/385Y is much lower than that of the wild-type enzyme, the mutant enzyme is able to transphosphatidylate various cyclohexanols with a preference for bulkier compounds
additional information
increased thermostability of mutant enzymes, especially those with D40H/T291Y mutation, compared to the wild-type enzyme, molecular dynamics analysis and molecular dynamics simulation, overview
additional information
protein engineering to create enzyme variants that can synthesize phosphatidylinositol from phosphatidylcholine and myo-inositol by transphosphatidylation by site-directed saturation mutagenesis at positions suspected to be involved in substrate recognition, namely Trp187, Tyr191 and Tyr385, high-throughput screening. Three variants (187D/191Y/385R, 187A/191Y/385R and 187M/191Y/385R) selectively produced 1(3)-phosphatidylinositol over the other phosphatidylinositol isomers
additional information
truncation of C-terminal 530 bp, no enzymic activtiy probably due o misfolding
additional information
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truncation of C-terminal 530 bp, no enzymic activtiy probably due o misfolding
additional information
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expression of PLD37/18 in Escherichia coli. PLD37 is the N-terminal fragment which contains the active site. PLD18 is the C-terminal fragment which is likely to play a regulatory role. The proteolytically clipped PLD37/18 is more active than the intact enzyme, but is no longer subject to product activation
additional information
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addition of PLD from Streptomyces chromofocus of exogenous PtdOH causes the normally semiround Hamster IIC9 fibroblasts to become more elongated in shape. Moreover, the PLD and PtdOH-induced change in cell morphology is driven by the formation of actin stress fibres
additional information
high-yield phosphatidylserine production via yeast surface display of the enzyme in Pichia pastoris strain GS115/pKFS-pldh. Thermostability, acid stability and organic solvent tolerance of the dPLD are significantly enhanced compared with the secreted wild-type enzyme from Streptomyces chromofuscus
additional information
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high-yield phosphatidylserine production via yeast surface display of the enzyme in Pichia pastoris strain GS115/pKFS-pldh. Thermostability, acid stability and organic solvent tolerance of the dPLD are significantly enhanced compared with the secreted wild-type enzyme from Streptomyces chromofuscus
additional information
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targeted mutations in the GG/GS motifs reveal its influence on both enzymatic activity and stability, a remarkable, 9-27 fold enhancement in transphosphatidylation activity is observed in the mutants
additional information
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construction of chimeras between TH-2PLD and PLD from a distict Streptomyces sp.
additional information
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isolation of mutants with higher activities, higher thermostability and tolerance against organic solvents, and with improved selectivity of the transphosphatidylation activity
additional information
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isolation of mutants with higher activities, higher thermostability and tolerance against organic solvents, and with improved selectivity of the transphosphatidylation activity
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additional information
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construction of chimeras between TH-2PLD and PLD from a distict Streptomyces sp.
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additional information
grape berries are pretreated at 8°C for 3 h and then transferred to 45°C for heat stress. Compared with the control without low temperature pretreatment, membrane permeability and malondialdehyde contents are reduced and the expression of HSP73 increases in the low temperature-pretreated berries under heat stress. During low temperature acclimation, PLD, salicylic acid and HSP73 are activated. The expression of HSP73 and the accumulation of free salicylic acid induced by low temperature can be inhibited by PLD activity inhibitor
additional information
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grape berries are pretreated at 8°C for 3 h and then transferred to 45°C for heat stress. Compared with the control without low temperature pretreatment, membrane permeability and malondialdehyde contents are reduced and the expression of HSP73 increases in the low temperature-pretreated berries under heat stress. During low temperature acclimation, PLD, salicylic acid and HSP73 are activated. The expression of HSP73 and the accumulation of free salicylic acid induced by low temperature can be inhibited by PLD activity inhibitor
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.