Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-alkyl-sn-glycero-3-phospho-L-serine + H2O
1-alkyl-sn-glycerol 3-phosphate + L-serine
-
-
-
-
?
1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycero-3-phosphate + choline
-
-
-
?
1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycerol 3-phosphate + choline
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O
1-alkyl-sn-glycero-3-phosphate + ethanolamine
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O
1-alkyl-sn-glycerol 3-phosphate + ethanolamine
1-heptadecanoyl-sn-glycero-3-phosphocholine + H2O
1-heptadecanoyl-sn-glycerol 3-phosphate + choline
1-linoleoyl-2-lyso-glycerophoshorylcholine + H2O
1-linoleoyl-sn-glycerol-3-phosphate + choline
-
-
-
-
?
1-linoleoyl-sn-glycero-3-phosphocholine + H2O
1-linoleoyl-sn-glycerol 3-phosphate + choline
1-myristoyl-lysophosphatidylcholine + H2O
1-myristoyl-sn-gycerol-3-phosphate + choline
-
-
-
-
?
1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-2-lyso-sn-glycero-3-phosphate + choline
1-O-alkyl-2-lyso-sn-glycero-3-phosphoethanolamine + H2O
1-O-alkyl-2-lyso-sn-glycero-3-phosphate + ethanolamine
-
the microsomal enzyme
the microsomal enzyme
?
1-O-alkyl-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-sn-glycerol 3-phosphate + choline
i.e. lyso-platelet-activating factor
-
-
?
1-O-hexadecyl-2-lyso-glycerophosphorylcholine + H2O
1-O-hexadecyl-sn-glycerol-3-phosphate + choline
-
lysoPAF (alkyl-lysophosphatidylcholine), lysoPLD shows higher activity towards lysoPAF
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + choline
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphoethanolamine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + ethanolamine
1-O-octadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-octadecyl-2-lyso-sn-glycero-3-phosphate + choline
-
-
-
?
1-palmitoyl-2-lyso-glycerophoshorylcholine + H2O
1-palmitoyl-sn-glycerol-3-phosphate + choline
-
-
-
-
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-sn-glycerol 3-phosphate + choline
1-stearoyl-2-lyso-glycerophoshorylcholine + H2O
1-stearoyl-sn-glycerol-3-phosphate + choline
-
-
-
-
?
4-nitrophenyl thymidine 5'-phosphate + H2O
4-nitrophenol + thymidine 5'-phosphate
-
-
-
-
?
4-nitrophenyl-TMP + H2O
4-nitrophenol + TMP
-
-
-
-
?
4-nitrophenyl-TMP + H2O
?
-
-
-
-
?
5-[[(23R)-33-(4-[[4-(dimethylamino)phenyl]diazenyl]phenyl)-20,23-dihydroxy-20-oxido-15,33-dioxo-3,6,9,12,19,21,25-heptaoxa-16,32-diaza-20-phosphatritriacont-1-yl]carbamoyl]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid + H2O
?
-
fluorogenic substrate analogue for lysophosphatidylcholine
-
-
?
arachidoyl-lysophosphatidylcholine + H2O
1-arachidoyl-sn-gycerol-3-phosphate + choline
behenoyl-lysophosphatidylcholine + H2O
1-behenoyl-sn-gycerol-3-phosphate + choline
bis(4-nitrophenyl)phosphate + H2O
?
-
-
-
-
?
bis(para-nitrophenyl)phosphate + H2O
?
-
-
-
-
?
caproyl-lysophosphatidylcholine + H2O
1-hexanoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
capryl-lysophosphatidylcholine + H2O
1-decanoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
caprylyl-lysophosphatidylcholine + H2O
1-octanoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
coumarin-phosphate-fluorescein + H2O
?
-
-
-
-
?
decanoyl-lysophosphatidylcholine + H2O
1-decanoyl-sn-gycerol-3-phosphate + choline
FS-2 + H2O
?
-
fluorogenic substrate analogue for lysophosphatidylcholine
-
-
?
FS-3 + H2O
2-(6-hydroxy-3-oxo-9a,10a-dihydro-3H-xanthen-9-yl)-5-[(18-hydroxy-15-oxo-3,6,9,12-tetraoxa-16-azaoctadec-1-yl)carbamoyl]benzoic acid + (2R)-2-hydroxy-3-(phosphonooxy)propyl 6-[(4-[(E)-[4-(dimethylamino)phenyl]diazenyl]benzoyl)amino]hexanoate
-
fluorogenic lysoPLD substrate
-
-
?
hexanoyl-lysophosphatidylcholine + H2O
1-hexanoyl-sn-gycerol-3-phosphate + choline
lauroyl-lysophosphatidylcholine + H2O
1-lauroyl-sn-gycerol-3-phosphate + choline
lyso-phosphatidylcholine + H2O
lyso-phosphatidic acid + choline
-
-
central in some key metabolic deregulations
-
?
lysoDDPB + H2O
?
-
synthesized by an enzyme-assisted strategy. Lysophosphatidylcholine analogue that contains a fluorescence quencher at each acyl chain terminus and a fluorophore appended to the phospholipid headgroup through a choline-mimetic linker
-
-
?
lysophosphatidyl choline + H2O
lysophosphatidic acid + choline
lysophosphatidyl ethanolamine + H2O
lysophosphatidic acid + ethanolamine
-
-
-
?
lysophosphatidylcholine + H2O
lysophosphatic acid + choline
-
LPC, purified enzyme hydrolyzes saturated forms of lysophosphatidylcholine more robustly than unsaturated forms
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
lysophosphatidylcholine 16:0 + H2O
?
-
-
-
-
?
lysophosphatidylcholine 18:0 + H2O
?
-
-
-
-
?
lysophosphatidylcholine 18:1 + H2O
?
-
-
-
-
?
myristoyl-lysophosphatidylcholine + H2O
1-myristoyl-sn-gycerol-3-phosphate + choline
N-arachidonoyl-lysophosphatidylethanolamine + H2O
lysophosphatidic acid + N-arachidonoyl-ethanolamine
-
-
-
?
N-arachidonoyllysophosphatidylethanolamine + H2O
lysophosphatidic acid + N-arachidonoylethanolamine
-
-
-
?
N-oleoyl-lysophosphatidylethanolamine + H2O
lysophosphatidic acid + N-oleoyl-ethanolamine
-
-
-
?
N-oleoyllysophosphatidylethanolamine + H2O
lysophosphatidic acid + N-oleoylethanolamine
-
-
-
?
N-palmitoyl-lysophosphatidylethanolamine + H2O
lysophosphatidic acid + N-palmitoyl-ethanolamine
-
-
-
?
N-palmitoyl-lysoplasmenylethanolamine + H2O
lysoplasmenic acid + N-palmitoyl-ethanolamine
-
-
-
?
N-palmitoyllysophosphatidylethanolamine + H2O
lysophosphatidic acid + N-palmitoylethanolamine
N-palmitoyllysoplasmenylethanolamine + H2O
lysoplasmenic acid + N-palmitoylethanolamine
-
-
-
?
octanoyl-lysophosphatidylcholine + H2O
1-octanoyl-sn-gycerol-3-phosphate + choline
oleoyl-lysophosphatidylcholine + H2O
1-oleoyl-sn-gycerol 3-phosphate + choline
p-nitrophenyl phenylphosphate + H2O
p-nitrophenol + phenylphosphate
-
-
-
?
p-nitrophenyl thymidine 5'-monophosphate + H2O
?
-
-
-
-
?
palmitoyl-lysophosphatidylcholine + H2O
1-palmitoyl-sn-gycerol-3-phosphate + choline
platelet-activating factor + H2O
? + choline
-
PAF, same extent as palmityl-lysophosphatidylcholine
-
-
?
sphingosylphosphorylcholine + H2O
sphingosine 1-phosphate + choline
sphingosylphosphorylcholine + H2O
sphingosine-1-phosphate + choline
-
-
-
-
?
stearoyl-lysophosphatidylcholine + H2O
1-stearoyl-sn-gycerol-3-phosphate + choline
[(11R)-1-(4-[(Z)-[4-(dimethylamino)phenyl]diazenyl]phenyl)-N-[3-[(5-[5-[(3,5-dimethyl-2H-pyrrol-2-ylidene-kappaN)methyl]-1H-pyrrol-2-yl-kappaN]pentanoyl)amino]propyl]-11,14-dihydroxy-N,N-dimethyl-1,8-dioxo-9,13,15-trioxa-2-aza-14-phosphaheptadecan-17-aminiumato 14-oxide](difluoro)boron(1+) + H2O
?
-
synthesized by an enzyme-assisted strategy. lysophosphatidylcholine analogue that contains a fluorescence quencher at each acyl chain terminus and a fluorophore append to the phospholipid headgroup through a choline-mimetic linker
-
-
?
[(2R)-26-(4-[(Z)-[4-(dimethylamino)phenyl]diazenyl]phenyl)-2,5-dihydroxy-5-oxido-10,26-dioxo-4,6,13,16,19,22-hexaoxa-9,25-diaza-5-phosphahexacos-1-yl 6-[(5-[5-[(3,5-dimethyl-2H-pyrrol-2-ylidene-kN)methyl]-1H-pyrrol-2-yl-kappaN]pentanoyl)amino]hexanoatato](difluoro)boron + H2O
?
-
fluorogenic substrate analogue for lysophosphatidylcholine
-
-
?
[5-[[(23S)-33-(4-[(E)-[4-(dimethylamino)phenyl]diazenyl]phenyl)-20,23-dihydroxy-20-oxido-15,26,33-trioxo-3,6,9,12,19,21,25-heptaoxa-16,32-diaza-20-phosphatritriacont-1-yl]carbamoyl]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)phenyl]acetic acid + H2O
?
-
second-generation fluorogenic autotaxin/lysoPLD substrate. The molecule consists of an ethanoamido head group linked to a dabcyl quencher via the amino group. The hydroxyl group of the head group is conjugated to fluorescein via a phosphodiester bond and a polyethylene glycol linker. [5-[[(23S)-33-(4-[(E)-[4-(dimethylamino)phenyl]diazenyl]phenyl)-20,23-dihydroxy-20-oxido-15,26,33-trioxo-3,6,9,12,19,21,25-heptaoxa-16,32-diaza-20-phosphatritriacont-1-yl]carbamoyl]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)phenyl]acetic acid is therefore a more lipid-like substrate than coumarin-phosphate-fluorescein
-
-
?
additional information
?
-
1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycerol 3-phosphate + choline
-
-
-
-
?
1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycerol 3-phosphate + choline
-
-
-
-
?
1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycerol 3-phosphate + choline
-
-
-
-
?
1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycerol 3-phosphate + choline
-
-
-
-
?
1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycerol 3-phosphate + choline
-
-
-
-
?
1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycerol 3-phosphate + choline
-
16:0, 18:1 and 18:2-lysophosphatidylcholine are the predominant physiological substrates of the enzyme in rabbit aqueous humor
-
-
?
1-alkyl-sn-glycero-3-phosphocholine + H2O
1-alkyl-sn-glycerol 3-phosphate + choline
-
-
-
-
?
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O
1-alkyl-sn-glycero-3-phosphate + ethanolamine
-
-
-
?
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O
1-alkyl-sn-glycero-3-phosphate + ethanolamine
-
-
-
?
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O
1-alkyl-sn-glycerol 3-phosphate + ethanolamine
-
-
-
-
?
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O
1-alkyl-sn-glycerol 3-phosphate + ethanolamine
-
-
-
-
?
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O
1-alkyl-sn-glycerol 3-phosphate + ethanolamine
-
-
-
-
r
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O
1-alkyl-sn-glycerol 3-phosphate + ethanolamine
-
-
-
-
?
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O
1-alkyl-sn-glycerol 3-phosphate + ethanolamine
-
-
-
-
?
1-heptadecanoyl-sn-glycero-3-phosphocholine + H2O
1-heptadecanoyl-sn-glycerol 3-phosphate + choline
-
-
-
-
?
1-heptadecanoyl-sn-glycero-3-phosphocholine + H2O
1-heptadecanoyl-sn-glycerol 3-phosphate + choline
-
-
-
-
?
1-linoleoyl-sn-glycero-3-phosphocholine + H2O
1-linoleoyl-sn-glycerol 3-phosphate + choline
-
-
-
-
?
1-linoleoyl-sn-glycero-3-phosphocholine + H2O
1-linoleoyl-sn-glycerol 3-phosphate + choline
-
-
-
-
?
1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-2-lyso-sn-glycero-3-phosphate + choline
-
-
-
?
1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-alkyl-2-lyso-sn-glycero-3-phosphate + choline
-
may play a role in the metabolism of platelet-activating factor
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + choline
-
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + choline
-
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + choline
-
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + choline
-
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + choline
-
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + choline
-
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + choline
-
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + choline
-
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphocholine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + choline
-
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphoethanolamine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + ethanolamine
-
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphoethanolamine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + ethanolamine
-
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphoethanolamine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + ethanolamine
-
-
-
?
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphoethanolamine + H2O
1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + ethanolamine
-
-
-
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-sn-glycerol 3-phosphate + choline
-
-
-
-
?
1-palmitoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-sn-glycerol 3-phosphate + choline
-
-
-
-
?
arachidoyl-lysophosphatidylcholine + H2O
1-arachidoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
arachidoyl-lysophosphatidylcholine + H2O
1-arachidoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
behenoyl-lysophosphatidylcholine + H2O
1-behenoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
behenoyl-lysophosphatidylcholine + H2O
1-behenoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
CPF4 + H2O
?
-
fluorescence resonance energy transfer substrate derived from bis-p-nitrophenyl phosphate
-
-
?
CPF4 + H2O
?
-
i.e. 5-([4-[(4-[[(6-chloro-7-hydroxy-2-oxo-2H-chromen-4-yl)acetyl]amino]phenoxy)(hydroxy)phosphoryl]phenyl]carbamoyl)-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid, fluorescence resonance energy transfer substrate derived from bis-p-nitrophenyl phosphate
-
-
?
CPF4 + H2O
?
-
bis-pNPP-derived probe, in which both phenyl moieties are linked to coumarin and fluorescein, respectively
-
-
?
decanoyl-lysophosphatidylcholine + H2O
1-decanoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
decanoyl-lysophosphatidylcholine + H2O
1-decanoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
FS-3 + H2O
?
-
fluorogenic substrate analogue for lysophosphatidylcholine
-
-
?
hexanoyl-lysophosphatidylcholine + H2O
1-hexanoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
hexanoyl-lysophosphatidylcholine + H2O
1-hexanoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
lauroyl-lysophosphatidylcholine + H2O
1-lauroyl-sn-gycerol-3-phosphate + choline
-
-
-
?
lauroyl-lysophosphatidylcholine + H2O
1-lauroyl-sn-gycerol-3-phosphate + choline
-
-
-
?
lysophosphatidyl choline + H2O
lysophosphatidic acid + choline
-
-
-
?
lysophosphatidyl choline + H2O
lysophosphatidic acid + choline
various concentration of lysophosphatidyl choline with or without 2.5 pM of hATX S48 are exposed to HT-1080 cells and motile area is analyzed
-
-
?
lysophosphatidyl choline + H2O
lysophosphatidic acid + choline
best substrate, reaction of EC 3.1.4.5
-
-
?
lysophosphatidyl choline + H2O
lysophosphatidic acid + choline
-
-
-
?
lysophosphatidyl choline + H2O
lysophosphatidic acid + choline
best substrate, reaction of EC 3.1.4.5
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
-
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
-
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
-
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
-
6, 663457, 664939, 665229, 666223, 666527, 670114, 681769, 696397, 697080, 698987, 700238, 701580, 701638, 702025, 702693, 703104, 705057, 706456, 706577 -
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
bioactive phospholipid regulating a wide range of cellular responses
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
albumin-bound lipid
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
present in the plasma
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
radiolabeled substrate
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
lysophospholipase D activity
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
radiolabeled substrate and fluorogenic substrate FS-3
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
-
Hydrolysis of lysophospholipids by the secreted plasma protein autotaxin/lysophospholipase D (lysoPLD) is a major mechanism for generation of lysophosphatidic acid in the blood
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
-
665507, 678439, 679137, 681910, 695455, 700364, 703366, 704356, 704588, 705323, 705706, 706456, 706564 -
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
-
lysophosphatidic acid is a bioactive lysophospholipid present in circulating blood
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
lysophosphatidic acid is a bioactive phospholipid regulating a wide range of cellular responses
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
-
LPA, lysophosphatidic acid is a bioactive lysophospholipid present in circulating blood
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
-
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
-
-
?
lysophosphatidylcholine + H2O
lysophosphatidic acid + choline
-
-
-
-
?
myristoyl-lysophosphatidylcholine + H2O
1-myristoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
myristoyl-lysophosphatidylcholine + H2O
1-myristoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
N-palmitoyllysophosphatidylethanolamine + H2O
lysophosphatidic acid + N-palmitoylethanolamine
-
-
-
?
N-palmitoyllysophosphatidylethanolamine + H2O
lysophosphatidic acid + N-palmitoylethanolamine
-
-
-
?
octanoyl-lysophosphatidylcholine + H2O
1-octanoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
octanoyl-lysophosphatidylcholine + H2O
1-octanoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
oleoyl-lysophosphatidylcholine + H2O
1-oleoyl-sn-gycerol 3-phosphate + choline
-
-
-
?
oleoyl-lysophosphatidylcholine + H2O
1-oleoyl-sn-gycerol 3-phosphate + choline
-
-
-
?
palmitoyl-lysophosphatidylcholine + H2O
1-palmitoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
palmitoyl-lysophosphatidylcholine + H2O
1-palmitoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
sphingosylphosphorylcholine + H2O
sphingosine 1-phosphate + choline
-
-
-
-
?
sphingosylphosphorylcholine + H2O
sphingosine 1-phosphate + choline
-
Whereas lysoPC is present in the blood at concentrations well in excess of the measured Km of autotaxin/lysoPLD for this substrate, levels of SPC are considerably lower, suggesting that this may not be a relevant substrate in vivo
bioactive lipid with a spectrum of signaling activities broadly similar to those of lysophosphatidic acid
-
?
sphingosylphosphorylcholine + H2O
sphingosine 1-phosphate + choline
-
-
bioactive lysophospholipid, in vitro
-
?
stearoyl-lysophosphatidylcholine + H2O
1-stearoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
stearoyl-lysophosphatidylcholine + H2O
1-stearoyl-sn-gycerol-3-phosphate + choline
-
-
-
?
additional information
?
-
-
zATX preferably hydrolyzes LPC and lysophosphatidylethanolamine but does not efficiently hydrolyze lysophosphatidylserine, lysophosphatidylinositol or sphingosylphosphorylcholine
-
-
?
additional information
?
-
-
the enzyme converts lysophospholipids such as lysophosphatidylcholine to lysophosphatidic acid
-
-
?
additional information
?
-
-
zATX preferably hydrolyzes LPC and lysophosphatidylethanolamine but does not efficiently hydrolyze lysophosphatidylserine, lysophosphatidylinositol or sphingosylphosphorylcholine
-
-
?
additional information
?
-
-
the enzyme is active on human macrophages, erythrocytes, Jurkat and HeLa cells, and on chicken embryo chorioallantoic membrane
-
-
?
additional information
?
-
-
the enzyme shows slight activity with sphingomyelin, but no activity with phosphatidylcholine
-
-
?
additional information
?
-
-
the plasma enzyme hydrolyzes acyl-, alkyl- and alkenyl-lysophophatidylcholines
-
?
additional information
?
-
Catalytic ability of ATX for p-nitrophenyl thymidine 5'-monophosphate and adenosine triphosphate hydrolysis are low compared with nucleotide pyrophosphatases-1/phosphodiesterases
-
-
?
additional information
?
-
-
Catalytic ability of ATX for p-nitrophenyl thymidine 5'-monophosphate and adenosine triphosphate hydrolysis are low compared with nucleotide pyrophosphatases-1/phosphodiesterases
-
-
?
additional information
?
-
-
There are no major differences in the respective specificities of the various isoforms, main substrate is lauroyl lysophosphatidylcholine
-
-
?
additional information
?
-
There are no major differences in the respective specificities of the various isoforms, main substrate is lauroyl lysophosphatidylcholine
-
-
?
additional information
?
-
-
There are no major differences in the respective specificities of the various isoforms, main substrate is lauroyl-lysophosphatidylcholine
-
-
?
additional information
?
-
There are no major differences in the respective specificities of the various isoforms, main substrate is lauroyl-lysophosphatidylcholine
-
-
?
additional information
?
-
-
activity implicated in a large variety of biological processes (during normal development and under pathological conditions). Developmental roles include adipogenesis, intestinal cell motility and neurite morphology, a contribution to disease is described for alzheimer's disease, chronic hepatitis C, multiple sclerosis, neuropathic pain, obesity, rheumatoid arthritis
-
-
?
additional information
?
-
-
assay development devised to quantify 4-nitrophenol from hydrolysis of chromogenic substrate by serum lysoPLD without tedious lipid extraction procedures
-
-
?
additional information
?
-
-
lysophospholipase D generates lysophosphatidic acid from lysophosphatidylcholine
-
-
?
additional information
?
-
-
reaction mechanism of NBD-LPC hydrolysis, overview. Artificial substrates FS-3 and pNP-TMP are used for kinetic studies, overview
-
-
?
additional information
?
-
-
the enzyme hydrolyzes extracellular lysophospholipids into the lipid mediator lysophosphatidic acid, a ligand for specific G protein-coupled receptors
-
-
?
additional information
?
-
-
the recombinant enzyme promotes MDA-MB-231 breast cancer cell and mouse aortic vascular smooth muscle cell migration in lysophosphatidic acid-dependent and -independent ways. The enzyme also shows nucleotide phosphodiesterase activity with nucleotide derivative 4-nitrophenyl-TMP as a substrate
-
-
?
additional information
?
-
poor substrate: glycerophospho-N-palmitoylethanolamine
-
-
?
additional information
?
-
-
poor substrate: glycerophospho-N-palmitoylethanolamine
-
-
?
additional information
?
-
Loxosceles sp.
-
the enzyme hydrolyzes extracellular lysophospholipids into the lipid mediator lysophosphatidic acid, a ligand for specific G protein-coupled receptors
-
-
?
additional information
?
-
-
no major differences in the respective specificities of the various isoforms, main substrate is lauroyl lysophosphatidylcholine
-
-
?
additional information
?
-
no major differences in the respective specificities of the various isoforms, main substrate is lauroyl lysophosphatidylcholine
-
-
?
additional information
?
-
-
There are no major differences in the respective specificities of the various isoforms, main substrate is lauroyl lysophosphatidylcholine
-
-
?
additional information
?
-
There are no major differences in the respective specificities of the various isoforms, main substrate is lauroyl lysophosphatidylcholine
-
-
?
additional information
?
-
-
There are no major differences in the respective specificities of the various isoforms, main substrate is lauroyl-lysophosphatidylcholine
-
-
?
additional information
?
-
There are no major differences in the respective specificities of the various isoforms, main substrate is lauroyl-lysophosphatidylcholine
-
-
?
additional information
?
-
-
when recombinant ATX is incubated with ysophosphatidylcholine in the presence of methanol, both lysophosphatidylmethanol and lysophosphatidic acid are produced with a ratio of 1:10, showing that ATX has transphosphatidylation activity in addition to its lysophospholipase D activity
-
-
?
additional information
?
-
-
brain homogenate forms N-palmitoylethanolamine, N-oleoylethanolamine, and anandamide from their corresponding lyso-N-acylphosphatidylethanolamines by a Mg2+-dependent lysophospholipase D, substrate specificity, overview
-
-
?
additional information
?
-
the enzyme converts lysophospholipids such as lysophosphatidylcholine to lysophosphatidic acid
-
-
?
additional information
?
-
-
the enzyme hydrolyzes extracellular lysophospholipids into the lipid mediator lysophosphatidic acid, a ligand for specific G protein-coupled receptors
-
-
?
additional information
?
-
poor substrate: glycerophospho-N-palmitoylethanolamine
-
-
?
additional information
?
-
-
poor substrate: glycerophospho-N-palmitoylethanolamine
-
-
?
additional information
?
-
-
brain homogenate forms N-palmitoylethanolamine, N-oleoylethanolamine, and anandamide from their corresponding lyso-N-acylphosphatidylethanolamines by a Mg2+-dependent lysophospholipase D, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme is active on 16:0, 18:1 and 18:2-lysophosphatidylcholine, it also hydrolyzes three lysophosphatidylcholine subclasses in the following order: 16:0-acyl-lysophosphatidylcholine > 16:0-alkyl-lysophosphatidylcholine > 16:0-rich alkenyl-lysophosphatidylcholine, substrate specificity, overview
-
-
?
additional information
?
-
-
no hydrolysis of 1-acyl-2-lyso-sn-glycero-3-phosphoethanolamine or 1-acyl-2-lyso-sn-glycero-3-phosphocholine
-
-
?
additional information
?
-
-
the microsomal enzymes prefer alkyl-lysophospholipids, the extracellular enzyme prefer acyl-phospholipids, but can use alkyl-lysophospholipids
-
?
additional information
?
-
-
the product lysophosphatidic acid mediates multiple biological functions
-
?
additional information
?
-
binding of ATX to activated platelets and lymphocytes in an integrin-dependent manner mediated by the consecutive cysteine-rich somatomedin-B-like, SMB, domains
-
-
?
additional information
?
-
-
heterotrimeric G protein subunits Galphaq and Gbeta1 have lysophospholipase D activity, choline production from lysoPAF by the purified FLAG-tagged Galphaq, overview. K52A, T186A, D205A, G48A and Q209L mutant forms of Galphaq show a significant reduction of lysoPLD activity, whereas G48V does not. The decrease of lysoPLD activity of G48A and Q209L is low
-
-
?
additional information
?
-
-
protein-protein interaction with proteins via the enzyme's SMB1 domain, which binds to the PDE domain. The enzyme binds to activated lymphocytes possibly involving an enzyme lymphocyte- and alpha4beta1-specific 458LDV460 motif. Autotaxin (ATX or ENPP2) is an ectonucleotide pyrophosphatase/phosphodiesterase that functions as a secreted lysophospholipase D to produce the multifunctional lipid mediator lysophosphatidic acid from more complex lysophospholipids
-
-
?
additional information
?
-
-
the enzyme can produce bioactive lysophosphatidic acid from diverse lysophospholipid substrates, particularly lysophosphatidylcholine, the most abundant lysophospholipid in the circulation, but also from lysophosphatidylserine and lysophosphatidylethanolamine. It does not discriminate between phospholipid headgroups
-
-
?
additional information
?
-
-
the enzyme hydrolyzes extracellular lysophospholipids into the lipid mediator lysophosphatidic acid, a ligand for specific G protein-coupled receptors
-
-
?
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.
(5Z)-2-(4-ethylpiperazin-1-yl)-5-(4-fluorobenzylidene)-1,3-thiazol-4(5H)-one
93.8% inhibition at 0.01 mM
(5Z)-2-(azepan-1-yl)-5-(4-propoxybenzylidene)-1,3-thiazol-4(5H)-one
96.6% inhibition at 0.01 mM
(5Z)-2-(morpholin-4-yl)-5-[4-(pentyloxy)benzylidene]-1,3-thiazol-4(5H)-one
93.3% inhibition at 0.01 mM
(5Z)-3-benzyl-5-[(1,3-dimethyl-2-oxo-2,3-dihydro-1H-benzimidazol-5-yl)methylidene]-1,3-thiazolidine-2,4-dione
-
-
(5Z)-5-(2-chlorobenzylidene)-2-(4-methylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
96.1% inhibition at 0.01 mM
(5Z)-5-(3,4-dichlorobenzylidene)-2-(4-methylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
(5Z)-5-(3,4-dichlorobenzylidene)-2-(piperazin-1-yl)-1,3-thiazol-4(5H)-one
(5Z)-5-(3,4-dichlorobenzylidene)-2-[4-[4-(dihydroxymethyl)benzyl]piperazin-1-yl]-1,3-thiazol-4(5H)-one
(5Z)-5-(3,4-dimethoxybenzylidene)-2-[4-(2-hydroxyethyl)piperazin-1-yl]-1,3-thiazol-4(5H)-one
(5Z)-5-(3-bromobenzylidene)-2-(4-ethylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
(5Z)-5-(4-chlorobenzylidene)-2-(4-ethylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
(5Z)-5-(4-ethoxy-3-methoxybenzylidene)-2-[4-(2-hydroxyethyl)piperazin-1-yl]-1,3-thiazol-4(5H)-one
(5Z)-5-(4-hydroxy-3,5-dimethoxybenzylidene)-2-(morpholin-4-yl)-1,3-thiazol-4(5H)-one
(5Z)-5-benzylidene-2-(4-ethylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
1,10-phenantroline
-
50% inhibition at 2.5 mM, 70% inhibition
1-acyl glycerol 3-phosphate
-
also fatty alcohol phosphates (structurally 1-acyl glycerol 3-phosphate analogs)
1-arachidonoyl-lysophosphatidic acid
-
Clarification of the structural importance of acyl chain for the inhibitory effect of lysophosphatidic acid on lysoPLD activity. Lysophosphatidic acids with polyunsaturated acyl chains are more potent than those with saturated acyl chains in the inhibition of serum lysoPLD activity
1-arachidoyl-lysophosphatidic acid
-
Clarification of the structural importance of acyl chain for the inhibitory effect of lysophosphatidic acid on lysoPLD activity. Lysophosphatidic acids with polyunsaturated acyl chains are more potent than those with saturated acyl chains in the inhibition of serum lysoPLD activity
1-bromo-3(s)-hydroxy-4-(palmitoyloxy) butylphosphonate
-
inhibitory in vitro and in vivo
1-hexanoyl-lysophosphatidic acid
-
Clarification of the structural importance of acyl chain for the inhibitory effect of lysophosphatidic acid on lysoPLD activity. Lysophosphatidic acids with polyunsaturated acyl chains are more potent than those with saturated acyl chains in the inhibition of serum lysoPLD activity
1-linoleoyl-lysophosphatidic acid
-
Clarification of the structural importance of acyl chain for the inhibitory effect of lysophosphatidic acid on lysoPLD activity. Lysophosphatidic acids with polyunsaturated acyl chains are more potent than those with saturated acyl chains in the inhibition of serum lysoPLD activity
1-myristoyl-lysophosphatidic acid
1-oleoyl-lysophosphatidic acid
1-palmitoyl-lysophosphatidic acid
1-stearoyl-lysophosphatidic acid
-
Clarification of the structural importance of acyl chain for the inhibitory effect of lysophosphatidic acid on lysoPLD activity. Lysophosphatidic acids with polyunsaturated acyl chains are more potent than those with saturated acyl chains in the inhibition of serum lysoPLD activity
2,2'-methylenebis(4-chlorophenol)
-
-
2-(4-[[(2,3-dichlorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
72.3% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(2,4,6-mesitylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
53.5% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(2,5-dichlorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
mixed inhibition, 5.4% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(2-benzothiadiazolphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
63.2% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(2-chlorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
83.5% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(2-fluorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
77.3% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(2-iodophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
68.4% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(2-methoxyphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
97.6% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(2-methylesterphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
51.2% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(3,5-bis(trifluoromethyl)phenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
competitive inhibition, 34.1% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(3,5-dimethylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
competitive inhibition, 30.4% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(3-benzothiadiazolphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
competitive inhibition, 28.6% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(3-chlorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
mixed inhibition, 9.7% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(3-fluorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
40.5% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(3-iodophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
mixed inhibition, 8.6% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(3-methoxyphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
40.9% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(3-methylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
competitive inhibition, 41.9% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(3-trifluoromethylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
competitive inhibition, 0.3% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(4-carboxylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
72.7% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(4-chlorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
competitive inhibition, 42.4% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(4-dimethylaminonaphthylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
59.9% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(4-fluorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
48.9% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(4-iodophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
mixed inhibition, 32.7% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(4-methoxyphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
79.7% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(4-methylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
49.9% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(4-morpholinosulfonylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
64.1% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(4-pyrazolephenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
68.6% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(4-trifluoromethylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
noncompetitive inhibition, 36.2% residual activity at 0.001 mM using FS-3 as substrate
2-(4-[[(phenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid phenyl
-
56.4% residual activity at 0.001 mM using FS-3 as substrate
2-amino-2-(2-(4-octylphenyl) ethyl)propan-1,3-diol
-
synonyms FTY720, finolimod, competitive inhibition
2-carba cyclic phosphatidic acid
-
-
3-([4-[(Z)-(3-benzyl-2,4-dioxo-1,3-thiazolidin-5-ylidene)methyl]-3-ethoxyphenoxy]methyl)benzoic acid
-
-
3-carba cyclic phosphatidic acid
-
-
3-[(4-[(Z)-[3-(4-fluorobenzyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]-3-methoxyphenoxy)methyl]benzoic acid
-
competitive inhibition, 35% residual ATX activity at 0.005 mM
3-[(4-[(Z)-[3-(4-fluorobenzyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]phenoxy)methyl]benzoic acid
-
competitive inhibition, 7% residual ATX activity at 0.005 mM
4-(5-[(4,6-dioxo-2-thioxotetrahydropyrimidin-5(2H)-ylidene)methyl]furan-2-yl)benzenesulfonamide
90.1% inhibition at 0.01 mM
4-amino-6-(2-[4'-[(E)-(8-amino-1-hydroxy-5,7-disulfonaphthalen-2-yl)diazenyl]-3,3'-dimethoxybiphenyl-4-yl]hydrazinyl)-5-hydroxynaphthalene-1,3-disulfonic acid
99.0% inhibition at 0.01 mM
4-amino-6-(2-{4'-[(E)-(8-amino-1-hydroxy-5,7-disulfonaphthalen-2-yl)diazenyl]-3,3'-dimethoxybiphenyl-4-yl}hydrazinyl)-5-hydroxynaphthalene-1,3-disulfonic acid
-
26.2% inhibition at 0.01 mM
4-chloro-N-methyl-N-{2-[2-(methylsulfonyl)hydrazinyl]-2-oxoethyl}benzenesulfonamide
70.7% inhibition at 0.01 mM
4-chloro-N-methyl-N-{2-[2-(methylsulfonyl)hydrazinyl]-2-oxoethyl}benzenesulfonamide (non-preferred name)
-
99.9% inhibition at 0.01 mM
4-[4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]butane-1-sulfonic acid
4-{5-[(4,6-dioxo-2-thioxotetrahydropyrimidin-5(2H)-ylidene)methyl]furan-2-yl}benzenesulfonamide
-
47.1% inhibition at 0.01 mM
5-[4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]pentanoic acid
ATP
-
extracellular enzyme
bis(para-nitrophenyl)phosphate
-
inhibition above a concentration of 1 mM
bovine serum albumin
-
concentration-dependent inhibition on lysoPLD activity in egg white during 24 h incubation
-
brefeldin-A
-
inhibitor of trans-Golgi transport, inhibits secretion of ATX
cyclohexanaminium hydrogen [4-(decanoylamino)benzyl]phosphonate
-
-
cyclohexanaminium hydrogen [4-(heptanoylamino)benzyl]phosphonate
-
-
cyclohexanaminium hydrogen [4-(tetradecanoylamino)benzyl]phosphonate
-
-
cyclohexanaminium hydrogen [4-([3-[2-(2-methoxyethoxy)ethoxy]propanoyl]amino)benzyl]phosphonate
-
-
cyclohexanaminium hydrogen [fluoro[4-(heptanoylamino)phenyl]methyl]phosphonate
-
-
cyclohexanaminium hydrogen [[4-(decanoylamino)phenyl](fluoro)methyl]phosphonate
-
-
cyclohexanaminium hydrogen [[4-(decanoylamino)phenyl](hydroxy)methyl]phosphonate
-
-
cyclohexanaminium hydrogen [[4-(heptanoylamino)phenyl](hydroxy)methyl]phosphonate
-
-
D-histidine
-
15 mM, 75% inhibition
fatty alkyl phosphonate
-
-
fatty alkyl thiophosphate
-
-
FTY720P
-
binds apo-ATX and an ATX with bound FS-3/products complex, noncompetitive/mixed inhibition
G protein
-
G protein exhibits lysoPLD activity, lysoPLD activity is highly associated with heterotrimeric G protein
-
Globomycin
-
Treatment with the signal peptidase inhibitor inhibits ATX secretion by adipocytes treated for 6 h
H2L 5210574
-
mixed-mode inhibition against ATX-mediated FS-3 hydrolysis
H2L 5564949
-
mixed-mode inhibition against ATX-mediated FS-3 hydrolysis
H2L 5761473
-
competitive ATX inhibitor
H2L 7839888
-
mixed-mode inhibition against ATX-mediated FS-3 hydrolysis
H2L 7921385
-
non-competitive inhibitor
histidine methylester
-
15 mM, 65% inhibition
histidineamide
-
15 mM, 20% inhibition
Human serum albumin
could be a regulator of the circulating autotaxin. When the albumin is a fatty acid-free preparation, this slight inhibition disappears; could be a regulator of the circulating autotaxin. When the albumin is a fatty acid-free preparation, this slight inhibition disappears
-
isorhamnetin-3-O-glucoside
-
-
Ki16425
-
inhibits the migratory response of lysophosphatidic acid1-expressing cells to both lysophosphatidic acid and ATX
L-histidine amide
-
15 mM, 20% inhibition
L-histidine methylester
-
15 mM, 65% inhibition
lactacystin
-
proteasome inhibitor, restores the detection of ATX in cell homogenate of the mutants DELTAV12-V22 and DELTAV12-G27, Synthesis and secretion of ATX are highly dependent on the hydrophobic core of the signal peptide, but not on the amino acid composition the putative signal peptidase cleavage site
lysozyme
-
concentration-dependent inhibition on lysoPLD activity in egg white during 24 h incubation
-
murine serum albumin
could be a regulator of the circulating autotaxin. When the albumin is a fatty acid-free preparation, this slight inhibition disappears; could be a regulator of the circulating autotaxin. When the albumin is a fatty acid-free preparation, this slight inhibition disappears
-
N-(2-chlorophenyl)-2-([(2E)-2-[1-(pyridin-2-yl)ethylidene]hydrazinyl]carbonothioyl)hydrazinecarbothioamide
N-glycosidase
-
treatment with N-glycosidase inhibits lysophospholipase D activity of ATX. N-glycosylation of ATX strongly influences its secretion and its lysoPLD activity
-
N-methyl histidine
-
15 mM, 30% inhibition
N-methyl-L-histidine
-
15 mM, 30% inhibition
oleoyl-LPA
-
inhibition of ATX pNP-TMP hydrolysis activity
palmitoyl-lysophosphatidic acid
-
concentration-dependent inhibition of lysoPLD activity in egg white during 24 h incubation. More than 100 microM of lysophosphatidic acid needed to inhibit significantly lysoPLD activity of hen egg white
serine esterase inhibitors
-
inhibition of extracellular enzyme
-
sodium cholate
-
16 mM, 77% inhibition
sodium deoxycholate
-
6 mM, 100% inhibition
Triton X-100
-
0.3 mM, 64% inhibition
tunicamycin
-
inhibits secretion of ATX
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-(pyridin-2-ylmethoxy)phenyl]butyl]phosphonic acid
-
-
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxy-3,5-dimethylbenzyl)oxy]phenyl]butyl]phosphonic acid
-
-
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxy-3,5-dimethylpyridin-2-yl)methoxy]phenyl]butyl]phosphonic acid
-
i.e. VPC8a202
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxy-3-methylbenzyl)oxy]phenyl]butyl]phosphonic acid
-
-
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxypyridin-2-yl)methoxy]phenyl]butyl]phosphonic acid
-
-
[(2R,3S)-4-(4-[[3,5-dimethyl-4-(2,2,2-trifluoroethoxy)pyridin-2-yl]methoxy]phenyl)-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
-
[(2R,3S)-4-[4-(benzyloxy)phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
-
[(2R,3S)-4-[4-[(2,4-dichlorobenzyl)oxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
-
[(2R,3S)-4-[4-[(3,5-dimethyl-4-propoxypyridin-2-yl)methoxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
-
[(2R,3S)-4-[4-[(3,5-dimethylbenzyl)oxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
-
[(2R,3S)-4-[4-[(3,5-dimethylpyridin-2-yl)methoxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
-
[(2R,3S)-4-[4-[(4-ethoxy-3,5-dimethylpyridin-2-yl)methoxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
-
[2-([4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]methyl)phenyl]boronic acid
[3-([4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]methyl)phenyl]boronic acid
[3-[(4-[(Z)-[3-(4-fluorobenzyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]phenoxy)methyl]phenyl]boronic acid
-
mixed-type inhibition, complete inhibition at 0.005 mM
[4-(tetradecanoylamino)benzyl]phosphonic acid
[4-([4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]methyl)phenyl]boronic acid
(5Z)-5-(3,4-dichlorobenzylidene)-2-(4-methylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
-
10.5% inhibition at 0.01 mM
(5Z)-5-(3,4-dichlorobenzylidene)-2-(4-methylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
94.9% inhibition at 0.01 mM
(5Z)-5-(3,4-dichlorobenzylidene)-2-(piperazin-1-yl)-1,3-thiazol-4(5H)-one
-
-
(5Z)-5-(3,4-dichlorobenzylidene)-2-(piperazin-1-yl)-1,3-thiazol-4(5H)-one
-
(5Z)-5-(3,4-dichlorobenzylidene)-2-[4-[4-(dihydroxymethyl)benzyl]piperazin-1-yl]-1,3-thiazol-4(5H)-one
-
-
(5Z)-5-(3,4-dichlorobenzylidene)-2-[4-[4-(dihydroxymethyl)benzyl]piperazin-1-yl]-1,3-thiazol-4(5H)-one
-
(5Z)-5-(3,4-dimethoxybenzylidene)-2-[4-(2-hydroxyethyl)piperazin-1-yl]-1,3-thiazol-4(5H)-one
-
18.1% inhibition at 0.01 mM
(5Z)-5-(3,4-dimethoxybenzylidene)-2-[4-(2-hydroxyethyl)piperazin-1-yl]-1,3-thiazol-4(5H)-one
95.3% inhibition at 0.01 mM
(5Z)-5-(3-bromobenzylidene)-2-(4-ethylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
-
70.9% inhibition at 0.01 mM
(5Z)-5-(3-bromobenzylidene)-2-(4-ethylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
90.7% inhibition at 0.01 mM
(5Z)-5-(4-chlorobenzylidene)-2-(4-ethylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
-
6.2% inhibition at 0.01 mM
(5Z)-5-(4-chlorobenzylidene)-2-(4-ethylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
91.5% inhibition at 0.01 mM
(5Z)-5-(4-ethoxy-3-methoxybenzylidene)-2-[4-(2-hydroxyethyl)piperazin-1-yl]-1,3-thiazol-4(5H)-one
-
15.7% inhibition at 0.01 mM
(5Z)-5-(4-ethoxy-3-methoxybenzylidene)-2-[4-(2-hydroxyethyl)piperazin-1-yl]-1,3-thiazol-4(5H)-one
92.2% inhibition at 0.01 mM
(5Z)-5-(4-hydroxy-3,5-dimethoxybenzylidene)-2-(morpholin-4-yl)-1,3-thiazol-4(5H)-one
-
23.7% inhibition at 0.01 mM
(5Z)-5-(4-hydroxy-3,5-dimethoxybenzylidene)-2-(morpholin-4-yl)-1,3-thiazol-4(5H)-one
93.2% inhibition at 0.01 mM
(5Z)-5-benzylidene-2-(4-ethylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
-
69.4% inhibition at 0.01 mM
(5Z)-5-benzylidene-2-(4-ethylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
97.7% inhibition at 0.01 mM
1,10-phenanthroline
-
inhibitory effects of 1,10-phenanthroline at different concentrations on lysoPLD activity against palmitoyl-lysophosphatidylcholine
1,10-phenanthroline
-
extracellular enzyme
1,10-phenanthroline
-
0.5 mM
1-myristoyl-lysophosphatidic acid
-
competitive inhibition of lysoPLD. Clarification of the structural importance of acyl chain for the inhibitory effect of lysophosphatidic acid on lysoPLD activity. Lysophosphatidic acids with polyunsaturated acyl chains are more potent than those with saturated acyl chains in the inhibition of serum lysoPLD activity
1-myristoyl-lysophosphatidic acid
-
-
1-oleoyl-lysophosphatidic acid
-
Clarification of the structural importance of acyl chain for the inhibitory effect of lysophosphatidic acid on lysoPLD activity. Lysophosphatidic acids with polyunsaturated acyl chains are more potent than those with saturated acyl chains in the inhibition of serum lysoPLD activity
1-oleoyl-lysophosphatidic acid
-
-
1-palmitoyl-lysophosphatidic acid
-
Clarification of the structural importance of acyl chain for the inhibitory effect of lysophosphatidic acid on lysoPLD activity. Lysophosphatidic acids with polyunsaturated acyl chains are more potent than those with saturated acyl chains in the inhibition of serum lysoPLD activity
1-palmitoyl-lysophosphatidic acid
-
-
4-[4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]butane-1-sulfonic acid
-
-
4-[4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]butane-1-sulfonic acid
-
5-[4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]pentanoic acid
-
-
5-[4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]pentanoic acid
-
bithionol
-
-
bithionol
-
inhibitory in vitro and in vivo
bithionol
-
inhibitory in vitro and in vivo
Cu2+
-
-
Cu2+
-
the inhibition of extracellular enzyme can be prevented by 2,6-di-tert-butyl-4-hydroxy-methylphenol
EDTA
-
inhibitory effects of EDTA at different concentrations on lysoPLD activity against palmitoyl-lysophosphatidylcholine. Inhibitory effect disappears when Mn2+ or Co2+ are added with EDTA to the egg white. Co-addition of Zn2+, Ni2+, or Cu2+ with EDTA results in 2-3times higher lysoPLD activity
EDTA
-
extracellular enzyme
EDTA
All isoforms being strongly inhibited by increasing concentrations of EDTA, 100% inhibition for 100 mM of the chelating agent; All isoforms strongly inhibited by increasing concentrations of EDTA, 100% inhibition for 100 mM of the chelating agent
EDTA
All isoforms being strongly inhibited by increasing concentrations of EDTA, 100% inhibition for 100 mM of the chelating agent; All isoforms strongly inhibited by increasing concentrations of EDTA, 100% inhibition for 100 mM of the chelating agent; strongly inhibited by increasing concentrations of EDTA, 100% inhibition for 100 mM of the chelating agent
EDTA
-
inhibition of extracellular enzyme
EDTA
-
hydrolysis of 1-palmitoyl-glycerophoshorylcholine is inhibited, indicating that a divalent cation is essential for catalytic activity
EGTA
-
48% inhibition
EGTA
All isoforms being strongly inhibited by increasing concentrations of EGTA, 100% inhibition for 100 mM of the chelating agent; All isoforms strongly inhibited by increasing concentrations of EGTA, 100% inhibition for 100 mM of the chelating agent
EGTA
All isoforms being strongly inhibited by increasing concentrations of EGTA, 100% inhibition for 100 mM of the chelating agent; All isoforms strongly inhibited by increasing concentrations of EGTA, 100% inhibition for 100 mM of the chelating agent; strongly inhibited by increasing concentrations of EGTA, 100% inhibition for 100 mM of the chelating agent
H2L 7905958
-
competitive inhibition with respect to ATX-mediated FS-3 hydrolysis and non-competitive inhibition with respect to ATX-mediated 4-nitrophenyl-TMP hydrolysis
H2L 7905958
-
potent ATX inhibitor, complete inhibition of FS-3 hydrolysis at 0.01 mM, competitive inhibitor
HA155
-
-
HA155
the boron atom on one end of the inhibitor forms a reversible covalent bond with the nucleophile hydroxyl group of Thr209. One of the two boron hydroxyl groups is further stabilized between the two zinc ions, binding structure, overview
hypericin
inhibitor of autotaxin beta; new inhibitor of autotaxin beta
hypericin
inhibitor of autotaxin beta; new inhibitor of autotaxin beta; new inhibitor of autotaxin beta
L-histidine
-
15-20 mM, noncompetitive, 75% inhibition, inhibition can be reversed by 20fold lower concentrations of zinc or cobalt salts
lysophosphatic acid
-
inhibits at biologically relevant concentrations
lysophosphatidic acid
reported as an inhibitor of its own production; reported as an inhibitor of its own production
lysophosphatidic acid
-
efficacious inhibitor of ATX activity
lysophosphatidic acid
-
-
lysophosphatidic acid
-
product inhibition of autotaxin/lysoPLD by lysophosphatidic acid, which is a potent mixed (both competitive and noncompetitive) inhibitor of the hydrolysis of lysoPC by autotaxin/lysoPLD in vitro. Possibility that lysophosphatidic acid regulates its own biosynthesis through feedback inhibition of autotaxin/lysoPLD
lysophosphatidic acid
reported as an inhibitor of its own production; reported as an inhibitor of its own production
lysophosphatidic acid
-
0.001 mM, complexed to albumin, competitive and noncompetitive components
Mg2+
concentrations ranging from 0.1 to 1000 mM; concentrations ranging from 0.1 to 1000 mM
Mg2+
concentrations ranging from 0.1 to 1000 mM; manganese inhibits the catalytic activities, concentrations ranging from 0.1 to 1000 mM
N-(2-chlorophenyl)-2-([(2E)-2-[1-(pyridin-2-yl)ethylidene]hydrazinyl]carbonothioyl)hydrazinecarbothioamide
-
58.3% inhibition at 0.01 mM
N-(2-chlorophenyl)-2-([(2E)-2-[1-(pyridin-2-yl)ethylidene]hydrazinyl]carbonothioyl)hydrazinecarbothioamide
71.5% inhibition at 0.01 mM
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
the inhibition of the microsomal enzyme can be prevented by glutathione and dithiothreitol
PF8380
-
-
PF8380
-
the inhibitor shows adequate oral bioavailability and potency in reducing lysophosphatidic acid levels in plasma and at sites of infl ammation
sphingosine 1-phosphate
-
inhibits at biologically relevant concentrations
sphingosine 1-phosphate
-
-
sphingosine-1-phosphate
-
Clarification of the structural importance of acyl chain for the inhibitory effect of lysophosphatidic acid on lysoPLD activity. Lysophosphatidic acids with polyunsaturated acyl chains are more potent than those with saturated acyl chains in the inhibition of serum lysoPLD activity; competitive inhibition of lysoPLD
sphingosine-1-phosphate
-
0.001 mM, complexed to albumin
Zn2+
concentrations ranging from 0.1 to 1000 mM; concentrations ranging from 0.1 to 1000 mM
Zn2+
concentrations ranging from 0.1 to 1000 mM; zinc inhibits the catalytic activities, concentrations ranging from 0.1 to 1000 mM
[2-([4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]methyl)phenyl]boronic acid
-
binding structure, overview
[2-([4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]methyl)phenyl]boronic acid
binding structure, overview
[3-([4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]methyl)phenyl]boronic acid
-
binding structure, overview
[3-([4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]methyl)phenyl]boronic acid
binding structure, overview
[4-(tetradecanoylamino)benzyl]phosphonic acid
-
S32826
[4-(tetradecanoylamino)benzyl]phosphonic acid
-
-
[4-([4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]methyl)phenyl]boronic acid
-
binding structure, overview
[4-([4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]methyl)phenyl]boronic acid
binding structure, overview
additional information
-
several extracts from edible plant seeds (sesame, sunflower, soybean) tested for the inhibition of lysoPLD activity, show a inhibition (>80%) of lysoPLD, fluorometric assay is favored over the spectrophotometric assay, ESI-MS/MS spectrum and MRM spectrum of major lysophosphatidic acids from seed lipid
-
additional information
-
inhibitor screening of thiazolone derivatives, overview. Screening for specific enzyme inhibitors using TG-mTMP, a highly sensitive fluorescence probe for the enzyme, that consists of enzyme recognition moiety, linker moiety, and fluorophore. It is almost nonfluorescent before the enzymatic reaction, and the enzyme generates strongly fluorescent 6-hydroxy-9-(4-methoxy-2-methylphenyl)-3H-xanthen-3-one with elimination of thymidine monophosphate and formaldehyde. In vitro and In vivo studies and evaluation of optimized inhibitors. No or poor inhibition by (5Z)-2-(azepan-1-yl)-5-(4-propoxybenzylidene)-1,3-thiazol-4(5H)-one, (5Z)-2-(morpholin-4-yl)-5-[4-(pentyloxy)benzylidene]-1,3-thiazol-4(5H)-one, (5Z)-2-(4-ethylpiperazin-1-yl)-5-(4-fluorobenzylidene)-1,3-thiazol-4(5H)-one, and (5Z)-5-(2-chlorobenzylidene)-2-(4-methylpiperazin-1-yl)-1,3-thiazol-4(5H)-one
-
additional information
-
Hypothesis that a protein in hen egg white masks the lysoPLD activity in undiluted egg white, and that dilution at more than 10times results in a high decline of the inhibitory activity
-
additional information
-
not inhibited by 2-(4-[[(2-trifluoromethylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
additional information
-
inhibitor development and synthesis, anti and syn forms of the molecules show different effects on the inhibitory potency, homology model docking study, overview
-
additional information
-
no inhibition by 4 at 0.01 mM
-
additional information
-
the low hydrophobicity of an inhibitor is a critical factor in its preference for the binding to a noncatalytic binding site over a catalytic binding site in ATX. Structure-activity relationship of inhibition on lysoPLD activity by polyphenols, overview. Resveratrol, caffeine, L-amino acids, tyrosine, phenylalanine, and 3-(3,4-dihydroxyphenyl)alanine, and phenolic antioxidants (propyl gallate, BHT, BHA), methyl (R)-(þ)-2-(4-hydroxyphenoxy)propionate, 3-(4-hydroxyphenyl)-1-propanol, and 4-(4-hydroxyphenyl)-2-butanone are inactive. Also inactive are flavonols kaempferol, tamarixetin, flavones luteolin, apigenin, chrysin, flavanols (+)-catechin, (-)-epicatechin, isoflavones daidzein, genistein; the low hydrophobicity of an inhibitor is a critical factor in its preference for the binding to a noncatalytic binding site over a catalytic binding site in ATX. Structure-activity relationship of inhibition on lysoPLD activity by polyphenols, overview. Resveratrol, caffeine, L-amino acids, tyrosine, phenylalanine, and 3-(3,4-dihydroxyphenyl)alanine, and phenolic antioxidants (propyl gallate, BHT, BHA), methyl (R)-(+)-2-(4-hydroxyphenoxy)propionate, 3-(4-hydroxyphenyl)-1-propanol, and 4-(4-hydroxyphenyl)-2-butanone are inactive. Also inactive are flavonols kaempferol, tamarixetin, flavones luteolin, apigenin, chrysin, flavanols (+)-catechin, (-)-epicatechin, isoflavones daidzein, genistein
-
additional information
-
possible involement of furin in secretion of ATX by adipocytes tested, furin inhibitor decanoyl-ArgValLysArgchloromethylketone does not modify secretion or lysophospholipase D activity of ATX
-
additional information
inhibitor screening of thiazolone derivatives, overview. Screening for specific enzyme inhibitors using TG-mTMP, a highly sensitive fluorescence probe for the enzyme, that consists of enzyme recognition moiety, linker moiety, and fluorophore. It is almost nonfluorescent before the enzymatic reaction, and the enzyme generates strongly fluorescent 6-hydroxy-9-(4-methoxy-2-methylphenyl)-3H-xanthen-3-one with elimination of thymidine monophosphate and formaldehyde. In vitro and In vivo studies and evaluation of optimized inhibitors, inhibitory potencies of monosubstituted and disubstituted aryl-methyl derivatives, overview
-
additional information
-
not affected by dioleoylphosphatidic acid, 1-oleoyl-glycerol, sphingosine, glycerol 3-phosphate
-
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.
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.
0.0001
1-acyl glycerol 3-phosphate
-
CPF4 FRET assay (change of fluorescence intensity), inihibition involves both a reduction in vmax and an increase in km, binding affinity is 1000fold stronger than to 1-alkyl-sn-glycero-3-phosphoethanolamine and analogue substrates
0.00055 - 0.0034
1-arachidonoyl-lysophosphatidic acid
0.01031 - 0.06
1-arachidoyl-lysophosphatidic acid
0.01299 - 0.06
1-hexanoyl-lysophosphatidic acid
0.00021 - 0.0018
1-linoleoyl-lysophosphatidic acid
0.005 - 0.0065
1-myristoyl-lysophosphatidic acid
0.0012 - 0.0096
1-oleoyl-lysophosphatidic acid
0.00141 - 0.0104
1-palmitoyl-lysophosphatidic acid
0.00209 - 0.0258
1-stearoyl-lysophosphatidic acid
0.0034
2-(4-[[(2,5-dichlorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.004
2-(4-[[(3,5-bis(trifluoromethyl)phenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0042
2-(4-[[(3,5-dimethylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0071
2-(4-[[(3-benzothiadiazolphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0026
2-(4-[[(3-chlorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0074
2-(4-[[(3-iodophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0045
2-(4-[[(3-methylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0007
2-(4-[[(3-trifluoromethylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0057
2-(4-[[(4-chlorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0132
2-(4-[[(4-iodophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0132
2-(4-[[(4-trifluoromethylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0002
2-amino-2-(2-(4-octylphenyl) ethyl)propan-1,3-diol
-
substrate p-nitrophenyl thymidine 5-monophosphate, pH 8.0, 30 min of incubation at 37°C, measuring absorbance at 405 nm, twofold higher KI compared to inhibitor S1P
0.000018
cyclohexanaminium hydrogen [4-(decanoylamino)benzyl]phosphonate
-
pH and temperature not specified in the publication
0.000512
cyclohexanaminium hydrogen [4-(heptanoylamino)benzyl]phosphonate
-
pH and temperature not specified in the publication
0.000009
cyclohexanaminium hydrogen [4-(tetradecanoylamino)benzyl]phosphonate
-
pH and temperature not specified in the publication
0.000834
cyclohexanaminium hydrogen [fluoro[4-(heptanoylamino)phenyl]methyl]phosphonate
-
pH and temperature not specified in the publication
0.0000061 - 0.000072
cyclohexanaminium hydrogen [[4-(decanoylamino)phenyl](fluoro)methyl]phosphonate
0.000024 - 0.0000242
cyclohexanaminium hydrogen [[4-(decanoylamino)phenyl](hydroxy)methyl]phosphonate
0.001009
cyclohexanaminium hydrogen [[4-(heptanoylamino)phenyl](hydroxy)methyl]phosphonate
-
pH and temperature not specified in the publication
0.0151
H2L 5564949
-
with respect to ATX-mediated FS-3 hydrolysis
0.002
H2L 5761473
-
with respect to ATX-mediated FS-3 hydrolysis
0.0027
H2L 7839888
-
with respect to ATX-mediated FS-3 hydrolysis
0.0019 - 0.0065
H2L 7905958
0.0093
H2L 7921385
-
with respect to ATX-mediated FS-3 hydrolysis
0.00011
lysophosphatidic acid
-
-
0.00001
PF8380
-
pH and temperature not specified in the publication
0.00021 - 0.0018
sphingosine-1-phosphate
0.0225 - 0.027
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-(pyridin-2-ylmethoxy)phenyl]butyl]phosphonic acid
0.0047 - 0.2175
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxy-3,5-dimethylbenzyl)oxy]phenyl]butyl]phosphonic acid
0.001 - 0.0111
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxy-3,5-dimethylpyridin-2-yl)methoxy]phenyl]butyl]phosphonic acid
0.0088 - 0.0265
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxy-3-methylbenzyl)oxy]phenyl]butyl]phosphonic acid
0.083
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxypyridin-2-yl)methoxy]phenyl]butyl]phosphonic acid
-
anti configuration, pH and temperature not specified in the publication
0.0016 - 0.0035
[(2R,3S)-4-(4-[[3,5-dimethyl-4-(2,2,2-trifluoroethoxy)pyridin-2-yl]methoxy]phenyl)-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
0.0039 - 0.0116
[(2R,3S)-4-[4-(benzyloxy)phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
0.0889 - 0.399
[(2R,3S)-4-[4-[(2,4-dichlorobenzyl)oxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
0.0015 - 1.059
[(2R,3S)-4-[4-[(3,5-dimethyl-4-propoxypyridin-2-yl)methoxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
0.0043 - 0.0062
[(2R,3S)-4-[4-[(3,5-dimethylbenzyl)oxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
0.0044
[(2R,3S)-4-[4-[(3,5-dimethylpyridin-2-yl)methoxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
syn configuration, pH and temperature not specified in the publication
0.011 - 0.5841
[(2R,3S)-4-[4-[(4-ethoxy-3,5-dimethylpyridin-2-yl)methoxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
0.00055
1-arachidonoyl-lysophosphatidic acid
-
inhibition of lysoPLD activity, based on fluoresecent assay, same order of inhibitory potency among lysophosphatidic acid analogs with different acyl chains in the spectrophotometric assay
0.0034
1-arachidonoyl-lysophosphatidic acid
-
inhibition of lysoPLD activity, spectrophotometric assay
0.01031
1-arachidoyl-lysophosphatidic acid
-
inhibition of lysoPLD activity, fluorometric assay
0.06
1-arachidoyl-lysophosphatidic acid
-
> 60 microM, inhibition of lysoPLD activity, spectrophotometric assay
0.01299
1-hexanoyl-lysophosphatidic acid
-
inhibition of lysoPLD activity, fluorometric assay
0.06
1-hexanoyl-lysophosphatidic acid
-
inhibition of lysoPLD activity, > 60 microM, size of acyl chain is crucial for the maximal inhibitory action, spectrophotometric assay
0.00021
1-linoleoyl-lysophosphatidic acid
-
most potent in the inhibition of lysoPLD activity, based on fluoresecent assay, same order of inhibitory potency among lysophosphatidic acid analogs with different acyl chains in the spectrophotometric assay
0.0018
1-linoleoyl-lysophosphatidic acid
-
competitive inhibition, spectrophotometric assay
0.005
1-myristoyl-lysophosphatidic acid
-
most potent in inhibiting lysoPLD activity, spectrophotometric assay
0.0065
1-myristoyl-lysophosphatidic acid
-
most potent in inhibiting lysoPLD activity, fluorometric assay
0.0012
1-oleoyl-lysophosphatidic acid
-
inhibition of lysoPLD activity, based on fluoresecent assay, same order of inhibitory potency among lysophosphatidic acid analogs with different acyl chains in the spectrophotometric assay
0.0096
1-oleoyl-lysophosphatidic acid
-
inhibition of lysoPLD activity, spectrophotometric assay
0.00141
1-palmitoyl-lysophosphatidic acid
-
inhibition of lysoPLD activity,size of acyl chain is crucial for the maximal inhibitory action, fluorometric assay
0.0104
1-palmitoyl-lysophosphatidic acid
-
inhibition of lysoPLD activity,size of acyl chain is crucial for the maximal inhibitory action, spectrophotometric assay
0.00209
1-stearoyl-lysophosphatidic acid
-
inhibition of lysoPLD activity,size of acyl chain is crucial for the maximal inhibitory action, fluorometric assay
0.0258
1-stearoyl-lysophosphatidic acid
-
inhibition of lysoPLD activity,size of acyl chain is crucial for the maximal inhibitory action, spectrophotometric assay
0.0000061
cyclohexanaminium hydrogen [[4-(decanoylamino)phenyl](fluoro)methyl]phosphonate
-
pH and temperature not specified in the publication
0.000072
cyclohexanaminium hydrogen [[4-(decanoylamino)phenyl](fluoro)methyl]phosphonate
-
pH and temperature not specified in the publication
0.000024
cyclohexanaminium hydrogen [[4-(decanoylamino)phenyl](hydroxy)methyl]phosphonate
-
pH and temperature not specified in the publication
0.0000242
cyclohexanaminium hydrogen [[4-(decanoylamino)phenyl](hydroxy)methyl]phosphonate
-
pH and temperature not specified in the publication
0.0019
H2L 7905958
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0019
H2L 7905958
-
with respect to ATX-mediated FS-3 hydrolysis
0.0065
H2L 7905958
-
with respect to ATX-mediated 4-nitrophenyl-TMP hydrolysis
0.00021
sphingosine-1-phosphate
-
SIP, inhibition of lysoPLD activity, fluorometric assay
0.0018
sphingosine-1-phosphate
-
SIP, inhibition of lysoPLD activity, spectrophotometric assay
0.0225
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-(pyridin-2-ylmethoxy)phenyl]butyl]phosphonic acid
-
anti configuration, pH and temperature not specified in the publication
0.027
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-(pyridin-2-ylmethoxy)phenyl]butyl]phosphonic acid
-
syn configuration, pH and temperature not specified in the publication
0.0047
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxy-3,5-dimethylbenzyl)oxy]phenyl]butyl]phosphonic acid
-
syn configuration, pH and temperature not specified in the publication
0.2175
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxy-3,5-dimethylbenzyl)oxy]phenyl]butyl]phosphonic acid
-
anti configuration, pH and temperature not specified in the publication
0.001
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxy-3,5-dimethylpyridin-2-yl)methoxy]phenyl]butyl]phosphonic acid
-
syn configuration, pH and temperature not specified in the publication
0.0111
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxy-3,5-dimethylpyridin-2-yl)methoxy]phenyl]butyl]phosphonic acid
-
anti configuration, pH and temperature not specified in the publication
0.0088
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxy-3-methylbenzyl)oxy]phenyl]butyl]phosphonic acid
-
syn configuration, pH and temperature not specified in the publication
0.0265
[(2R,3S)-3-(hexadecanoylamino)-2-hydroxy-4-[4-[(4-methoxy-3-methylbenzyl)oxy]phenyl]butyl]phosphonic acid
-
anti configuration, pH and temperature not specified in the publication
0.0016
[(2R,3S)-4-(4-[[3,5-dimethyl-4-(2,2,2-trifluoroethoxy)pyridin-2-yl]methoxy]phenyl)-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
syn configuration, pH and temperature not specified in the publication
0.0035
[(2R,3S)-4-(4-[[3,5-dimethyl-4-(2,2,2-trifluoroethoxy)pyridin-2-yl]methoxy]phenyl)-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
anti configuration, pH and temperature not specified in the publication
0.0039
[(2R,3S)-4-[4-(benzyloxy)phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
anti configuration, pH and temperature not specified in the publication
0.0116
[(2R,3S)-4-[4-(benzyloxy)phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
syn configuration, pH and temperature not specified in the publication
0.0889
[(2R,3S)-4-[4-[(2,4-dichlorobenzyl)oxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
syn configuration, pH and temperature not specified in the publication
0.399
[(2R,3S)-4-[4-[(2,4-dichlorobenzyl)oxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
anti configuration, pH and temperature not specified in the publication
0.0015
[(2R,3S)-4-[4-[(3,5-dimethyl-4-propoxypyridin-2-yl)methoxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
syn configuration, pH and temperature not specified in the publication
1.059
[(2R,3S)-4-[4-[(3,5-dimethyl-4-propoxypyridin-2-yl)methoxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
anti configuration, pH and temperature not specified in the publication
0.0043
[(2R,3S)-4-[4-[(3,5-dimethylbenzyl)oxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
syn configuration, pH and temperature not specified in the publication
0.0062
[(2R,3S)-4-[4-[(3,5-dimethylbenzyl)oxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
anti configuration, pH and temperature not specified in the publication
0.011
[(2R,3S)-4-[4-[(4-ethoxy-3,5-dimethylpyridin-2-yl)methoxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
anti configuration, pH and temperature not specified in the publication
0.5841
[(2R,3S)-4-[4-[(4-ethoxy-3,5-dimethylpyridin-2-yl)methoxy]phenyl]-3-(hexadecanoylamino)-2-hydroxybutyl]phosphonic acid
-
syn configuration, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00011
(5Z)-3-benzyl-5-[(1,3-dimethyl-2-oxo-2,3-dihydro-1H-benzimidazol-5-yl)methylidene]-1,3-thiazolidine-2,4-dione
Mus musculus
-
in Tris-HCl buffer (pH 7.4) at 37°C
0.00017
(5Z)-5-(3,4-dichlorobenzylidene)-2-(piperazin-1-yl)-1,3-thiazol-4(5H)-one
Mus musculus
pH 9.0, 37°C
0.000025
(5Z)-5-(3,4-dichlorobenzylidene)-2-[4-[4-(dihydroxymethyl)benzyl]piperazin-1-yl]-1,3-thiazol-4(5H)-one
Mus musculus
pH 9.0, 37°C
0.0013
2-(4-[[(2,5-dichlorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0341
2-(4-[[(3,5-bis(trifluoromethyl)phenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0304
2-(4-[[(3,5-dimethylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0286
2-(4-[[(3-benzothiadiazolphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0097
2-(4-[[(3-chlorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0161
2-(4-[[(3-fluorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0016
2-(4-[[(3-iodophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0177
2-(4-[[(3-methoxyphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0135
2-(4-[[(3-methylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0009
2-(4-[[(3-trifluoromethylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0107
2-(4-[[(4-chlorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0177
2-(4-[[(4-fluorophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0015
2-(4-[[(4-iodophenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0161
2-(4-[[(4-methylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0327
2-(4-[[(4-trifluoromethylphenyl)amino]carbonothioyl]-1-piperazinyl)-8-ethyl-5-oxo-5,8-dihydropyrido[2,3-d]pyrimidine-6-carboxylic acid
Homo sapiens
-
1 mM each CaCl2 and MgCl2, 5 mM KCl, and 140 mM NaCl, in 50 mM Tris, pH 8.0, at 37°C
0.0003
2-amino-2-(2-(4-octylphenyl) ethyl)propan-1,3-diol
Homo sapiens
-
to 0.0004, substrate p-nitrophenyl thymidine 5-monophosphate, pH 8.0, 30 min of incubation at 37°C, measuring absorbance at 405 nm, compared to inhibitor S1P 0.0001 mM
0.000161
3-([4-[(Z)-(3-benzyl-2,4-dioxo-1,3-thiazolidin-5-ylidene)methyl]-3-ethoxyphenoxy]methyl)benzoic acid
Mus musculus
-
in Tris-HCl buffer (pH 7.4) at 37°C
0.0025
3-[(4-[(Z)-[3-(4-fluorobenzyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]-3-methoxyphenoxy)methyl]benzoic acid
Mus musculus
-
in Tris-HCl buffer (pH 7.4) at 37°C
0.0017
3-[(4-[(Z)-[3-(4-fluorobenzyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]phenoxy)methyl]benzoic acid
Mus musculus
-
in Tris-HCl buffer (pH 7.4) at 37°C
0.00023
4-[4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]butane-1-sulfonic acid
Mus musculus
pH 9.0, 37°C
0.00039
5-[4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]pentanoic acid
Mus musculus
pH 9.0, 37°C
0.0128
H2L 5564949
Homo sapiens
-
with respect to ATX-mediated FS-3 hydrolysis
0.0128
H2L 5761473
Homo sapiens
-
with respect to ATX-mediated FS-3 hydrolysis
0.0015 - 0.0017
H2L 7839888
0.0012 - 0.0016
H2L 7905958
0.0016
H2L 7921385
Homo sapiens
-
with respect to ATX-mediated FS-3 hydrolysis
0.0753 - 0.1035
Human serum albumin
-
0.0016 - 0.0029
hypericin
0.000016 - 0.000038
lysophosphatidic acid
0.187 - 0.317
murine serum albumin
-
0.00058
[2-([4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]methyl)phenyl]boronic acid
Mus musculus
pH 9.0, 37°C
0.000013
[3-([4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]methyl)phenyl]boronic acid
Mus musculus
pH 9.0, 37°C
0.000028
[3-[(4-[(Z)-[3-(4-fluorobenzyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]phenoxy)methyl]phenyl]boronic acid
Mus musculus
-
in Tris-HCl buffer (pH 7.4) at 37°C
0.000022
[4-([4-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-4,5-dihydro-1,3-thiazol-2-yl]piperazin-1-yl]methyl)phenyl]boronic acid
Mus musculus
pH 9.0, 37°C
0.0068
H2L 5210574
Homo sapiens
-
with respect to ATX-mediated 4-nitrophenyl-TMP hydrolysis
0.0068
H2L 5210574
Homo sapiens
-
with respect to ATX-mediated FS-3 hydrolysis
0.0015
H2L 7839888
Homo sapiens
-
with respect to ATX-mediated FS-3 hydrolysis
0.0017
H2L 7839888
Homo sapiens
-
with respect to ATX-mediated 4-nitrophenyl-TMP hydrolysis
0.0012
H2L 7905958
Homo sapiens
-
with respect to ATX-mediated 4-nitrophenyl-TMP hydrolysis
0.0016
H2L 7905958
Homo sapiens
-
-
0.0016
H2L 7905958
Homo sapiens
-
with respect to ATX-mediated FS-3 hydrolysis
0.0753
Human serum albumin
Homo sapiens
incubating human autotaxin beta with human serum albumin
-
0.1035
Human serum albumin
Homo sapiens
incubating human autotaxin gamma with human serum albumin
-
0.0016
hypericin
Mus musculus
tested on murine autotaxin alpha
0.0025
hypericin
Homo sapiens
tested on human autotaxin gamma
0.0026
hypericin
Mus musculus
tested on murine autotaxin gamma
0.0028
hypericin
Mus musculus
tested on murine autotaxin beta
0.0029
hypericin
Homo sapiens
tested on human autotaxin beta
0.000016
lysophosphatidic acid
Homo sapiens
reported as an inhibitor of its own production, incubating human autotaxin gamma with lysophosphatidic acid
0.000017
lysophosphatidic acid
Homo sapiens
reported as an inhibitor of its own production, incubating human autotaxin beta with lysophosphatidic acid
0.000018
lysophosphatidic acid
Mus musculus
reported as an inhibitor of its own production, incubating murine autotaxin beta with lysophosphatidic acid
0.00002
lysophosphatidic acid
Mus musculus
reported as an inhibitor of its own production, incubating murine autotaxin gamma with lysophosphatidic acid
0.000038
lysophosphatidic acid
Homo sapiens
reported as an inhibitor of its own production, incubating human autotaxin alpha with lysophosphatidic acid
0.000038
lysophosphatidic acid
Mus musculus
reported as an inhibitor of its own production, incubating murine autotaxin alpha with lysophosphatidic acid
0.187
murine serum albumin
Mus musculus
incubating murine autotaxin alpha with murine serum albumin
-
0.251
murine serum albumin
Mus musculus
incubating murine autotaxin gamma with murine serum albumin
-
0.317
murine serum albumin
Mus musculus
incubating murine autotaxin beta with murine serum albumin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000005 - 0.000076
-
depending on presence of divalent cations
0.0051
Murine autotaxin gamma, p-nitrophenyl phenylphosphonate as a substrate, Vmax 1.8 nmol p-nitrophenyl/min
0.00847
human autotaxin alpha, p-nitrophenyl phenylphosphonate as a substrate, Vmax 0.67 nmol p-nitrophenyl/min
0.0163
Murine autotaxin alpha, p-nitrophenyl phenylphosphonate as a substrate, Vmax 0.35 nanomol p-nitrophenyl/min
0.036
-
using isotopic assay
0.048
-
colorimetric assay, 6 h incubation, 37°C
0.0919
Murine autotaxin beta, para-nitrophenyl phenylphosphonate as a substrate, Vmax 1.9 nmol para-nitrophenyl/min
0.0997
Human autotaxin gamma, p-nitrophenyl phenylphosphonate as a substrate, Vmax 1.6 nmol p-nitrophenyl/min
0.135
Human autotaxin beta, p-nitrophenyl phenylphosphonate as a substrate, Vmax 1.9 nmol p-nitrophenyl/min
0.14
-
purified enzyme, HiTrap DEAE FF
additional information
-
Spectrophotometric assay of LysoPLD activity. Determination of lysoPLD activity by measuring the amount of choline released from exogenously added LPC. Fluorometric assay for LysoPLD activity. Determination of LysoPLD activity using a fluorogenic substrate, [5-[[(23S)-33-(4-[(E)-[4-(dimethylamino)phenyl]diazenyl]phenyl)-20,23-dihydroxy-20-oxido-15,26,33-trioxo-3,6,9,12,19,21,25-heptaoxa-16,32-diaza-20-phosphatritriacont-1-yl]carbamoyl]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)phenyl]acetic acid (FS-3)
additional information
-
lysoPLD activity of diluted or undiluted egg white measured based on enzyme-linked fluorometric measurement of choline produced together with lysophosphatidic acid from exogenous lysophosphatidylcholine. LysoPLD activity measured by determining lysophosphatidic acid and choline by MALDI-TOF-MS, mass spectrometric and enzyme-linked fluorometric analysis. Quantitative analysis of lysophosphatidic acid by MALDI-TOF-MS using a phosphate-capture molecule. Production of lysophosphatidic acid during incubation of hen egg white, changes in the levels of fatty acyl groups
additional information
-
autotaxin/lysoPLD activity is determined at the indicated substrate concentrations using conditioned medium from V5-autotaxin expressing cells as the source of enzyme and radiolabeled lysophosphatidylcholine as substrate
additional information
biochemical and cell biological activity of hATX S48 protein measured
additional information
-
biochemical and cell biological activity of hATX S48 protein measured
additional information
-
lysoPLD activity is assessed, based on the amount of choline released with lysophosphatidylcholine as the substrate, absorption spectrometry. Amounts of the substrate lysophosphatidylcholine and the product lysophosphatidic acid are also checked simultaneously. Changes in the lysoPLD activity and lysophosphatidylcholine and lysophosphatidic acid concentrations in incubated serum. Concentrations of lysophosphatidylcholine and lysophosphatidic acid increase upon incubation, the levels increase significantly as compared with those in the controls (no incubation) after 60-min incubations. Dramatic increase in the lysophosphatidic acid concentration is observed, and the lysophosphatidic acid level after 180-min incubation is about 15times higher than in the control
additional information
-
phosphodiesterase activity of recombinant autotaxin is measured by using p-nitrophenyl phenylphosphonate substrate
additional information
phosphodiesterase activity of recombinant autotaxin is measured by using p-nitrophenyl phenylphosphonate substrate
additional information
-
approx. 0 mmol/ml/min, serum from a patient with preterm labor, detection of dilution dependency of choline-producing activity of sera, diluted 100fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 0 mmol/ml/min, serum from a patient with severe pre-eclampsia, detection of dilution dependency of choline-producing activity of sera, diluted 30fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate , 37°C
additional information
-
approx. 0 mmol/ml/min, serum from a woman with normal pregnancy, detection of dilution dependency of choline-producing activity of sera, diluted 1fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 10 mmol/ml/min, serum from a woman with normal pregnancy, detection of dilution dependency of choline-producing activity of sera, diluted 30fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 100 mmol/ml/min, serum from a patient with preterm labor, detection of dilution dependency of choline-producing activity of sera, diluted 1fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate , 37°C
additional information
-
approx. 1000 mmol/ml/min, serum from a patient with preterm labor, detection of dilution dependency of choline-producing activity of sera, diluted 100fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 104 micromol/ml/min, serum from a patient with severe pre-eclampsia, diluted 3.3fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 1100 mmol/ml/min, serum from a patient with severe pre-eclampsia, detection of dilution dependency of choline-producing activity of sera, diluted 100fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 118 micromol/ml/min, serum from a patient with preterm labor (30.1 +/- 0.8 gestational weeks; n is 21), diluted 3.3fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 139 micromol/ml/min, serum from a patient with preterm labor (30.1 +/- 0.8 gestational weeks; n is 21), diluted 3.3fold (serum + saline), presence of 0.15 mM exogenous 18:2-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 146 micromol/ml/min, serum from a patient with severe pre-eclampsia, diluted 3.3fold (serum + saline), presence of 0.15 mM exogenous 18:2-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 15 mmol/ml/min, serum from a patient with severe pre-eclampsia, detection of dilution dependency of choline-producing activity of sera, diluted 100fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 15 mmol/ml/min, serum from a woman with normal pregnancy, detection of dilution dependency of choline-producing activity of sera, diluted 100fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate , 37°C
additional information
-
approx. 150 mmol/ml/min, serum from a woman with normal pregnancy, detection of dilution dependency of choline-producing activity of sera, diluted 1fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate , 37°C
additional information
-
approx. 153 micromol/ml/min, serum from a woman with normal pregnancy (35.8 +/- 0.7 gestational weeks; n is 25), diluted 3.3fold (serum + saline), presence of 0.15 mM exogenous 18:2-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 180 mmol/ml/min, serum from a patient with severe pre-eclampsia, detection of dilution dependency of choline-producing activity of sera, diluted 1fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 200 mmol/ml/min, serum from a woman with normal pregnancy, detection of dilution dependency of choline-producing activity of sera, diluted 3.3fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate , 37°C
additional information
-
approx. 300 mmol/ml/min, serum from a patient with preterm labor, detection of dilution dependency of choline-producing activity of sera, diluted 3.3fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 350 mmol/ml/min, serum from a patient with severe pre-eclampsia, detection of dilution dependency of choline-producing activity of sera, diluted 3.3fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 400 mmol/ml/min, serum from a woman with normal pregnancy, detection of dilution dependency of choline-producing activity of sera, diluted 10fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate , 37°C
additional information
-
approx. 450 mmol/ml/min, serum from a patient with preterm labor, detection of dilution dependency of choline-producing activity of sera, diluted 10fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 450 mmol/ml/min, serum from a patient with severe pre-eclampsia, detection of dilution dependency of choline-producing activity of sera, diluted 10fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 450 mmol/ml/min, serum from a woman with normal pregnancy, detection of dilution dependency of choline-producing activity of sera, diluted 30fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate , 37°C
additional information
-
approx. 49 micromol/ml/min, serum from a patient with moderate pre-eclampsia, diluted 3.3fold (serum + saline), presence of 0.15 mM exogenous 18:2-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 5 mmol/ml/min, serum from a woman with normal pregnancy, detection of dilution dependency of choline-producing activity of sera, diluted 10fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 500 mmol/ml/min, serum from a patient with preterm labor, detection of dilution dependency of choline-producing activity of sera, diluted 30fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 500 mmol/ml/min, serum from a patient with severe pre-eclampsia, detection of dilution dependency of choline-producing activity of sera, diluted 30fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 60 mmol/ml/min, serum from a patient with preterm labor, detection of dilution dependency of choline-producing activity of sera, diluted 1fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 65 mmol/ml/min, serum from a patient with preterm labor, detection of dilution dependency of choline-producing activity of sera, diluted 10fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate , 37°C
additional information
-
approx. 65 mmol/ml/min, serum from a patient with preterm labor, detection of dilution dependency of choline-producing activity of sera, diluted 3.3fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 65 mmol/ml/min, serum from a patient with severe pre-eclampsia, detection of dilution dependency of choline-producing activity of sera, diluted 1fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 700 mmol/ml/min, serum from a woman with normal pregnancy, detection of dilution dependency of choline-producing activity of sera, diluted 100fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 8 mmol/ml/min, serum from a patient with preterm labor, detection of dilution dependency of choline-producing activity of sera, diluted 30fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate , 37°C
additional information
-
approx. 8 mmol/ml/min, serum from a woman with normal pregnancy, detection of dilution dependency of choline-producing activity of sera, diluted 3.3fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate , 37°C
additional information
-
approx. 80 mmol/ml/min, serum from a patient with severe pre-eclampsia, detection of dilution dependency of choline-producing activity of sera, diluted 3.3fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 90 micromol/ml/min, serum from a woman with normal pregnancy (35.8 +/- 0.7 gestational weeks; n is 25), diluted 3.3fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx. 92 micromol/ml/min, serum from a patient with moderate pre-eclampsia, diluted 3.3fold (serum + saline), presence of 0.15 mM exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate, 37°C
additional information
-
approx.50 mmol/ml/min, serum from a patient with severe pre-eclampsia, detection of dilution dependency of choline-producing activity of sera, diluted 10fold (serum + saline), absence of exogenous 16:0-lysophosphatidylcholine, radiolabeled substrate , 37°C
additional information
-
overview of methods for determination of autotaxin/lysoPLD activity. Using radiolabeled substrates and fluorogenic substrates for measuring autotaxin/lysoPLD activity
additional information
-
lysophospholipase D activity is measured by conversion of radiolabeled lysophosphatidylcholine into radiolabeled lysophosphatidic acid
additional information
-
phosphodiesterase activity of recombinant autotaxin is measured by using p-nitrophenyl phenylphosphonate substrate
additional information
phosphodiesterase activity of recombinant autotaxin is measured by using p-nitrophenyl phenylphosphonate substrate
additional information
-
phosphodiesterase activity of recombinant autotaxin is measured by using p-nitrophenyl-phenylphosphonate substrate
additional information
phosphodiesterase activity of recombinant autotaxin is measured by using p-nitrophenyl-phenylphosphonate substrate
additional information
-
phosphodiesterase activity of recombinant autotaxin is measured by using para-nitrophenyl phenylphosphonate substrate
additional information
phosphodiesterase activity of recombinant autotaxin is measured by using para-nitrophenyl phenylphosphonate substrate
additional information
-
To deplete ATX from mouse serum, mouse serum is incubated with the 5E5-Sepharose 4B for 2 h at 4°C, and the resulting supernatant is used for measuring lysoPLD activity and lysophosphatidic acid production. Lysophospholipase D activity of plasma and amniotic fluids isolated from atx+/+ and atx+/-adult mice or atx+/+ and atx+/-embryos at different stages of development measured with immunohistochemistry. LysoPLD activity is determined by liberation of choline from lysophosphatidylcholine using myristyl-lysophosphatidylcholine as a substrate
additional information
-
approx. 400 micromol/min/ml, mice are treated with control rat IgG, plasma samples (10 microl) incubate with 4 mmol/l lysophosphatidylcholine, activity determined by enzymatic photometric method using choline oxidase at 560 nm, 37°C
additional information
-
approx. 42 micromol/min/ml, mice are treated with anti-ATX mAb, plasma samples (10 microl) incubate with 4 mmol/l lysophosphatidylcholine, activity determined by enzymatic photometric method using choline oxidase at 560 nm, 37°C
additional information
-
nuclear fraction has relatively high levels of lysoPLD activity. Both lysoPLD activity and highest band density found in microsomal fraction
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.
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.
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.
evolution
mouse and human enzymes show high structural homology
evolution
-
the enzyme belongs to the ENPP family, but ATX/ENPP2 is a unique lysoPLD with no functional redundancy within the ENPP family, overview. The enzyme and its ENPP family members can be divided into two main subgroups, namely ENPP1-3 and ENPP4-7. ATX/ENPP2 and its closest relatives, ENPP1 and ENPP3, have two N-terminal somatomedin B (SMB)-like domains, a central phosphodiesterase (PDE) domain and a C-terminal nuclease (NUC)-like domain. The second subgroup (ENPP4-7) has only the PDE domain in common. ATX/NPP2 is a secreted protein, while the other ENPPs are transmembrane proteins, either type-I (ENPP4-7) or type-II (ENPP1-3)
malfunction
-
down-regulation of endogenous autotaxin expression in 4T1 cells inhibits osteolytic bone metastasis formation independently of primary tumor growth in vivo
malfunction
-
E9.5 ATX null mutants exhibit a failure of neural tube closure, most likely independent of the circulatory failure, which correlates with decreased cell proliferation and increased cell death, obligatory deletion results to embryonic lethality most likely due to aberrant vascular branching morphogenesis and chorio-allantoic fusion
malfunction
-
in Enpp2 knockout mouse embryos, lysosomes in the visceral endoderm cells are fragmented
malfunction
-
a recombinant ATX mutant, lacking lysoPLD activity, or heat-inactived ATX also induces lung epithelial cell migration
malfunction
-
ATX SMB2 mutants with impaired binding to beta3 integrins display reduced LPA generating capacity. Mutation of a charged, surface-exposed residue at the N-terminus of the ATX SMB2 domain significantly reduces binding of ATX to platelet integrins. The effects of ATX on platelet and cell-associated LPA production, but not hydrolysis of small molecule or detergent-solubilized substrates, are attenuated by point mutations in the SMB2 that impair integrin binding
malfunction
-
knockdown of ATX in zebrafish embryos causes abnormal blood vessel formation. In ATX morphant embryos, the segmental arteries sprouted normally from the dorsal aorta but stalled in the mid-course resulting in aberrant vascular connection around the horizontal myoseptum
malfunction
-
adipocyte-specific knockout FATX-KO mice or mice treated with the lysophosphatidic acid receptor antagonist Ki16425 gain more weight and accumulate more adipose tissue than wild-type or control mice fed a high fat diet
malfunction
-
ATX inhibitor bithionol remarkably decreases lymphocyte migration to the intestine and ameliorates both dextran sodium sulfate-induced colitis and CD4-induced ileocolitis, administration of bithionol or 1-bromo-3(s)-hydroxy-4-(palmitoyloxy) butylphosphonate significantly decreases transmigration of splenocytes through high-endothelial-like vessels induced by TNF-alpha
malfunction
-
fasting decreases enzyme activity. Nutritional deficiency of 18 : 2- and 18 : 1-containing phosphatidylcholines causes selective reduction of corresponding unsaturated lysophosphatidylcholines relative to other species in the blood circulation. Prolonged fasting of rats causes a greater decrease in the level of lysophosphatidylcholine in the liver than that of phosphatidylethanolamine
malfunction
-
ATX inhibitor bithionol remarkably decreases lymphocyte migration to the intestine and ameliorates both dextran sodium sulfate-induced colitis and CD4-induced ileocolitis, administration of bithionol or 1-bromo-3(s)-hydroxy-4-(palmitoyloxy) butylphosphonate significantly decreases transmigration of splenocytes through high-endothelial-like vessels induced by TNF-alpha
-
malfunction
-
fasting decreases enzyme activity. Nutritional deficiency of 18 : 2- and 18 : 1-containing phosphatidylcholines causes selective reduction of corresponding unsaturated lysophosphatidylcholines relative to other species in the blood circulation. Prolonged fasting of rats causes a greater decrease in the level of lysophosphatidylcholine in the liver than that of phosphatidylethanolamine
-
malfunction
-
knockdown of ATX in zebrafish embryos causes abnormal blood vessel formation. In ATX morphant embryos, the segmental arteries sprouted normally from the dorsal aorta but stalled in the mid-course resulting in aberrant vascular connection around the horizontal myoseptum
-
metabolism
-
in contrast to the decreased plasma enzyme activity in fasted rats, lysophosphatidic acid production from lysophosphatidylcholine by the enzyme activity progressively increases
metabolism
-
in contrast to the decreased plasma enzyme activity in fasted rats, lysophosphatidic acid production from lysophosphatidylcholine by the enzyme activity progressively increases
-
physiological function
-
ATX expression and lysophosphatidic acid signalling are vital for the development of the nervous system, ATX and lysophosphatidic acid are necessary for embryonic HIF-1a expression
physiological function
-
ATX promotes the migrations of THP-1 and Jurkat cells via Gi-signaling pathway
physiological function
-
autotoxin promotes metastasis and tumor growth
physiological function
-
constitutive activationof the Rho-ROCK-LIM kinase pathway by extracellular production of lysophosphatidic acid by the action of autotaxin is required to maintain the large size of lysosomes in visceral endoderm cells
physiological function
-
expression of autotaxin by cancer cells controls osteolytic bone metastasis formation
physiological function
-
expression of autotaxin by cancer cells controls osteolytic bone metastasis formation
physiological function
-
the autotaxin-lysophosphatidic acid receptor axis plays a causal role in breast tumorigenesis and cancer-related inflammation
physiological function
-
the enzyme controls the blood concentration of lysophosphatidic acid
physiological function
-
ATX moderately facilitates platelet adhesion to fibrinogen, synergistic effect of platelet activation and ATX on LPA generation. ATX binding to platelet integrins enables agonist-stimulated LPA production. The lysophospholipase D generates the bioactive lipid mediator lysophosphatidic acid. Integrin-bound ATX can access cell surface substrates and deliver LPA to cell surface receptors
physiological function
ATX promotes localized LPA signaling
physiological function
-
ATX stimulates tumour-cell migration, angiogenesis and metastasis
physiological function
autotaxin exhibits lysophospholipase D activity, hydrolyzing lysophosphatidylcholine to the signalling lipid lysophosphatidic acid
physiological function
-
autotaxin is a catalytic protein, which possesses lysophospholipase D activity producing lysophosphatidic acid, and is involved in cellular membrane lipid metabolism and remodeling. It acts as a culprit protein for cancer, which potently stimulates cancer cell proliferation and tumor cell motility, augments the tumorigenicity and induces angiogenic responses. Lysophosphatidic acid is a potent mitogen, which facilitates cell proliferation and migration, neurite retraction, platelet aggregation, smooth muscle contraction, actin stress formation and cytokine and chemokine secretion. ATX also catalyzes the formation of cyclic phosphatidic acid, which have antitumor role by antimitogenic regulation of cell cycle, inhibition of cancer invasion and metastasis
physiological function
-
autotaxin is a multifunctional ecto-type phosphodiesterase that converts lysophospholipids such as lysophosphatidylcholine to lysophosphatidic acid by its lysophospholipase D activity. ATX has an essential role in embryonic blood vessel formation. Autotaxin is required for the development of intersegmental arteries in zebrafish
physiological function
-
autotaxin is a secreted lysophospholipase D that hydrolyzes lysophosphatidylcholine into lysophosphatidic acid, initiating signaling cascades leading to cancer metastasis, wound healing, and angiogenesis
physiological function
-
autotaxin is a secreted lysophospholipase D that hydrolyzes lysophosphatidylcholine to generate lysophosphatidic acid, a lipid mediator that activates G protein-coupled receptors to evoke various cellular responses. The produced LPAs are delivered from the active site to cognate G protein-coupled receptors through a hydrophobic channel
physiological function
-
autotaxin is a secreted soluble enzyme that generates lysophosphatidic acid through its lysophospholipase D activity
physiological function
-
autotaxin is an enzyme present in the blood and responsible for biosynthesis of lysophosphatidic acid
physiological function
-
GDE1 has a weak activity to generate N-palmitoylethanolamine from its corresponding 1-alkenyl-2-hydroxy-glycero-3-phospho(N-acyl)ethanolamines, suggesting that this enzyme is at least in part responsible for the lysophospholipase D activity in mouse brain
physiological function
-
lysophospholipase D hydrolyzes lysophosphatidylcholine to form the bioactive lipid lysophosphatidic acid
physiological function
-
secreted autotaxin, which exhibits lysophospholipase D activity, stimulates lung epithelial cell migration through lysophosphatidic acid generation-dependent and -independent pathways lung cell migration is a crucial step for re-epithelialization that in turn is essential for remodelling and repair after lung injury, overview. Extracellular ATX stimulates cell migration through G?i-coupled LPA receptors, cytoskeleton rearrangement, phosphorylation of PKC delta and cortactin at the leading edge of migrating cells. Cortactin regulates ATX-V5-induced cell migration
physiological function
-
Heminecrolysin induces erythrocyte hemolysis via lysophospholipase D activity. Heminecrolysin efficiently binds to erythrocyte's membrane and provokes phosphatidylserine translocation without cleavage of glycophorin A, suggesting that, unlike spider's phospholipase D, complement is activated only via the classical pathway. Heminecrolysin induces pro-inflammatory cytokine release and causes necrosis in the vascular tissue
physiological function
-
in a dextran sodium sulfate mouse model, the enzyme expression level is considerably higher in colonic mucosa of chronically developed colitis than in colonic mucosa of acute colitis. The enzyme is required for lymphocyte transmigration, but not for surface expression of b7-integrin and CD11beta on splenocytes that migrated through epithelial cells. The role of the ATX-LPA axis in leukocyte transendothelial migration through induced high endothelial venule-like vessels has no tropism for surface expression of adhesion molecules on leukocytes
physiological function
-
the enzyme and its reaction product lysophosphatidic acid have a critical role in lymphocyte migration to secondary lymphoid organs, involvement of the enzyme in inflammatory bowel disease patients, the enzyme/lysophosphatidic acid has a role in the migration of lymphocytes to the inflamed intestine
physiological function
-
the enzyme is constitutively released from corneal tissues and/or ciliary body into the aqueous humor, with no injury-induced increase in release following freeze-wounding. Wound-induced increases in lysophosphatidic acid-like biological activity are due to linoleoyl species-rich molecular composition in aqueous humor from wounded eyes, possible mechanisms, overview
physiological function
-
the enzyme is involved in synthesis of lysophosphatidic acid, a phospholipid growth factor acting via lysophosphatidic acid-specific receptors (LPA1R to LPA6R) and involved in several pathologies including obesity. Enzyme expression is up-regulated in obese patients and mice in relationship with insulin resistance and impaired glucose tolerance. Lysophosphatidic acid-specific receptor LPA1R is the most abundant receptor subtype in adipose tissue. Its expression is higher in non-adipocyte cells than in adipocytes and is not altered in obesity. The enzyme increases and receptor LPA1R decreases while preadipocytes differentiate into adipocytes (adipogenesis). Lysophosphatidic acid inhibits adipogenesis through down-regulation of the pro-adipogenic transcription factor PPARgamma2. ATX/LPA signaling impairs glucose homeostasis, regulation of obesity involves the enzyme, overview
physiological function
-
the enzyme is involved in synthesis of lysophosphatidic acid, a phospholipid growth factor acting via specific receptors (LPA1R to LPA6R) and involved in several pathologies including obesity. ATX/LPA signaling impairs glucose homeostasis, regulation of obesity involves the enzyme, overview
physiological function
-
the enzyme is involved in the formation of blood vessel networks in fertilized hen egg white through several lysophosphatidic acid receptors on various extraembryonic membranes, including the yolk sac membrane and chorioallantoic membrane
physiological function
-
the enzyme is the major lysophosphatidic acid-producing enzyme being involved in a great diversity of (patho)physiological processes. Enzyme-produced lysophosphatidic acid acts on distinct G protein-coupled receptors thereby activating multiple signaling cascades and cellular responses. The ATX-LPA signaling axis is implicated in a remarkably wide variety of physiological and pathological processes, ranging from vascular and neural development to lymphocyte homing, fibrosis and cancer
physiological function
the enzyme is the predominant contributor to lysophosphatidic acid production in the human body, especially in the blood, and therefore has important roles in various physiological functions, including development of vasculature and lymphocyte trafficking
physiological function
-
the enzyme is the primary lysophosphatidic acid-producing phospholipase. Enzyme-lysophosphatidic acid signaling is essential for development and has been implicated in a great diversity of (patho)physiological processes, ranging from lymphocyte homing to tumor progression. Isozyme ATX alpha but not ATX beta binds abundantly to cultured mammalian cells in a manner strictly dependent on heparan sulfate. By mediating bindings to heparan sulfate proteoglycans, the isozyme ATXalpha insertion loop likely serves to target LPA production close to the lysophosphatidic acid receptors
physiological function
-
the enzyme is the primary lysophosphatidic acid-producing phospholipase. Enzyme-lysophosphatidic acid, ATX-LPA, signaling is essential for development and has been implicated in a great diversity of (patho)physiological processes, ranging from lymphocyte homing to tumor progression. Isozyme ATX alpha but not ATX beta binds abundantly to cultured mammalian cells in a manner strictly dependent on heparan sulfate. By mediating bindings to heparan sulfate proteoglycans, the isozyme ATXalpha insertion loop likely serves to target LPA production close to the lysophosphatidic acid receptors
physiological function
-
the enzyme promotes MDA-MB-231 breast cancer cell and mouse aortic vascular smooth muscle cell migration in lysophosphatidic acid-dependent and -independent ways, overview. The enzyme binds to integrin adhesion receptors required for cell migration. Integrin-mediated cell surface binding results in enzyme uptake and intracellular trafficking, critical for the ability of the enzyme to promote rapid directionally persistent MDA-MB-231 cell migration
physiological function
GDE4 functions as an N-acylethanolamine-generating lysophospholipase D in living cells. The expression of GDE4 increases the levels of most species of lysophosphatidic acid in the cell
physiological function
-
in a dextran sodium sulfate mouse model, the enzyme expression level is considerably higher in colonic mucosa of chronically developed colitis than in colonic mucosa of acute colitis. The enzyme is required for lymphocyte transmigration, but not for surface expression of b7-integrin and CD11beta on splenocytes that migrated through epithelial cells. The role of the ATX-LPA axis in leukocyte transendothelial migration through induced high endothelial venule-like vessels has no tropism for surface expression of adhesion molecules on leukocytes
-
physiological function
-
GDE1 has a weak activity to generate N-palmitoylethanolamine from its corresponding 1-alkenyl-2-hydroxy-glycero-3-phospho(N-acyl)ethanolamines, suggesting that this enzyme is at least in part responsible for the lysophospholipase D activity in mouse brain
-
physiological function
-
autotaxin is a multifunctional ecto-type phosphodiesterase that converts lysophospholipids such as lysophosphatidylcholine to lysophosphatidic acid by its lysophospholipase D activity. ATX has an essential role in embryonic blood vessel formation. Autotaxin is required for the development of intersegmental arteries in zebrafish
-
additional information
-
a loop region in the catalytic domain is a major determinant for the substrate specificity of the Enpp family enzymes, Asn230 is critical for the recognition of the common phosphate moieties, structure of the ATX active site in the free-form and with bound Zn2+, overview
additional information
-
ATX interacts with integrins, possible role for the solvent-exposed surface of the N-terminal tandem somatomedin B-like domains in binding to platelet integrin alphaIIbbeta3. The opposite face of the somatomedin B-like domain interacts with the catalytic phosphodiesterase domain to form a hydrophobic channel through which lysophospholipid substrates enter and leave the active site. Integrin binding therefore localizes ATX activity to the cell surface, providing a mechanism to generate LPA in the vicinity of its receptors
additional information
-
extracelluar ATX binds to the LPA receptor and integrin beta4 complex on A-549 cell surface
additional information
structural basis of substrate discrimination and integrin binding by autotaxin, ATX, that interacts with cell-surface integrins via its N-terminal somatomedin-B-like domains, using an atypical mechanism, overview
additional information
-
the ability of ATX to drive cell migration is enhanced by the presence of the ATX substrate lysophosphocholine
additional information
-
the predicted nucleotide phosphate and Mg2+ binding sites of the protein are important for lysoPLD enzymatic activity
additional information
-
Thr210 coordinates one of the two catalytic zinc ions and hydrogen bonds with the phosphate or sulfate in the active site. Kinetics of ATX depend strongly on the substrate identity, suggesting that ATX could display different kinetic profiles for the various in vivo substrates
additional information
-
enzyme crystal structure analysis, phosphodiesterase domain and substrate binding pocket, overview, the enzyme structure is a tunnel that spans from the active site location to the opposite side of ATX. It is formed from the interaction between the SMB1 and the PDE domain. The tunnel may function as an lysophosphatidic acid binding site and, by inference, a product release site
additional information
-
Heminecrolysin does not affect glycophorin A expression
additional information
-
the catalytic domain shows shallow groove and a deep hydrophobic pocket, and an open tunnel, which forms a sort of T-junction with the shallow groove, substrate binding structure, overview. The enzyme contains a SMB domain that mediates the binding to cell surface integrins
additional information
-
the tripartite catalytic domain shows shallow groove and a deep hydrophobic pocket, and an open tunnel, which forms a sort of T-junction with the shallow groove, substrate binding structure, overview. The enzyme contains a SMB domain that mediates the binding to cell surface integrins
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
H226Q
-
the mutation impairs substrate hydrolysis, with hydrolysis of artificial substrates being disproportionately lower than that of lysophosphatidylcholine
H420Q
-
the mutation does not inhibit the wild type migration response or hydrolytic activity
H434Q
-
the mutation impairs substrate hydrolysis, with hydrolysis of artificial substrates being disproportionately lower than that of lysophosphatidylcholine
DELTA202-363
-
COS cells transfected with mutated ATX express catalytically inactive phosphodiesterase and lysophospholipase D. Lethality of the ATX-/-embryos. ATX-dependent LPA production is due to the catalytic activity of the enzyme
DELTA592-617
ATXalpha isoform, 915 amino acids total
DELTAA30-G41
-
deletion mutants are generated from plasmid pcDNA-mATX, encompasses furin site
DELTAA30-I33
-
deletion mutants are generated from plasmid pcDNA-mATX, between signal peptidase and furin site
DELTAA36-E40
-
deletion mutants are generated from plasmid pcDNA-mATX
DELTAC25
-
deletion mutants are generated from plasmid pcDNA-mATX, amino acid -3 referring to the potential signal peptidase cleavage site
DELTAE40-P43
-
deletion mutants are generated from plasmid pcDNA-mATX
DELTAG27
-
deletion mutants are generated from plasmid pcDNA-mATX, amino acid -1 referring to the potential signal peptidase cleavage site
DELTAG27-A30
-
deletion mutants are generated from plasmid pcDNA-mATX, contain potential signal peptidase clevage site
DELTAG27-R35
-
deletion mutants are generated from plasmid pcDNA-mATX, encompasses both furin and signal peptidase cleavage sites
DELTAL46-S49
-
deletion mutants are generated from plasmid pcDNA-mATX
DELTAN23
-
deletion mutants are generated from plasmid pcDNA-mATX, amino acid -5 referring to the potential signal peptidase cleavage site
DELTAN23-G27
-
deletion mutants are generated from plasmid pcDNA-mATX, encompasses -1 and -3 amino acids referring to the potential signal peptidase clevage site
DELTAN410
-
deletion mutants are generated from plasmid pcDNA-mATX, contains a N-glycosylation site, point deletion of the amino-acid N410 inhibits lysophospholipase D activity of ATX, does not modify the ATX secretion and strongly inhibits ATX activity
DELTAN53
-
deletion mutants are generated from plasmid pcDNA-mATX, contains a N-glycosylation site, does not modify the ATX secretion and slightly reduces (25%) ATX activity
DELTAN53/DELTAN410
-
deletion mutants are generated from plasmid pcDNA-mATX, two N-glycosylation sites, double point deletion of the amino-acids N53 and N410 inhibits secretion of ATX, without altering the ATX amount in cell homogenate
DELTAP43-L46
-
deletion mutants are generated from plasmid pcDNA-mATX
DELTAR32-R35
-
deletion mutants are generated from plasmid pcDNA-mATX, furine site
DELTAS49-N53
-
deletion mutants are generated from plasmid pcDNA-mATX, contains N-glycosylation site
DELTAV12-G27
-
deletion mutants are generated from plasmid pcDNA-mATX, hydrophobic domain of signal peptide and signal peptide cleavage site, ATX secretion is suppressed
DELTAV12-V22
-
deletion mutants are generated from plasmid pcDNA-mATX, hydrophobic domain of signal peptide, ATX secretion is suppressed
F249A
-
the mutant shows decreased lysoPLD activity and differences in the fatty acid preferences compared to the wild-type enzyme
F274A
-
the mutant shows decreased lysoPLD activity and differences in the fatty acid preferences compared to the wild-type enzyme
L213A
-
the mutant shows decreased lysoPLD activity and differences in the fatty acid preferences compared to the wild-type enzyme
L243A
-
the mutant shows decreased lysoPLD activity and differences in the fatty acid preferences compared to the wild-type enzyme
M512A
-
the mutant shows decreased lysoPLD activity and differences in the fatty acid preferences compared to the wild-type enzyme
N230A
-
almost inactive mutant
T209A
-
catalytically inactive
W254A
-
the mutant shows decreased lysoPLD activity and differences in the fatty acid preferences compared to the wild-type enzyme
Y306A
-
the mutant shows decreased lysoPLD activity and differences in the fatty acid preferences compared to the wild-type enzyme
A218V
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
A305E
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
C194A
-
the mutant shows a specific activity similar to the wild type enzyme
C366A
-
the mutant shows a specific activity similar to the wild type enzyme
C468A
-
the mutant shows a specific activity similar to the wild type enzyme
C513A
-
the mutant shows a specific activity similar to the wild type enzyme
C651A
-
the mutant shows a specific activity similar to the wild type enzyme
C666A
-
the mutant shows a specific activity similar to the wild type enzyme
C774A
-
the mutant shows a specific activity similar to the wild type enzyme
C784A
-
the mutant shows a specific activity similar to the wild type enzyme
F211A
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
F274E
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
F275Q
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
L214H
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
N398A
NPP2 site-directed mutagenesis
N398A/N410A/N524A/N806A
NPP2 mutant
N410A
increased mobility during SDS-PAGE is only noted following the mutation of sites N53A, N410A, and N524A, indicating that these are the only true glycosylation sites. Mutation of each of the corresponding asparagines into an alanine and examination of the effects of these mutations on the mobility of NPP2 during SDS-PAGE and on its enzymatic activities. Efficient chemoattractant for NIH-3T3 cells
N524A
mutation of N524A causes an accumulation of NPP2 in the cells, suggesting that the glycosylation of Asn-524 also contributes to the maturation and/or trafficking of NPP2. Only the mutation of N524A abolishes the nucleotide and lysophospholipid phosphodiesterase activities of NPP2, showing that the glycosylation of Asn-524 is required for the expression of catalytic activity. Increased mobility during SDS-PAGE is only noted following the mutation of sites N53A, N410A, and N524A, indicating that these are the only true glycosylation sites. Mutation of each of the corresponding asparagines into an alanine and examinations of the effects of these mutations on the mobility of NPP2 during SDS-PAGE and on its enzymatic activities. Does not measurably stimulate cell motility
N53A
increased mobility during SDS-PAGE is only noted following the mutation of sites N53A, N410A, and N524A, indicating that these are the only true glycosylation sites. Mutation of each of the corresponding asparagines into an alanine and examination of the effects of these mutations on the mobility of NPP2 during SDS-PAGE and on its enzymatic activities. Efficient chemoattractant for NIH-3T3 cells
N53A/N398A/N410A/N524A
NPP2 mutant
N53A/N398A/N410A/N524A/N806A
NPP2 with sites 15 mutated, does not measurably stimulate cell motility
N53A/N398A/N410A/N806A
NPP2 with sites 1, 2, 3 and 5 mutated,only glycosylated on Asn-524
N53A/N398A/N524A/N806A
NPP2 mutant
N53A/N410A/N524A/N806A
NPP2 mutant
N806A
NPP2, site-directed mutagenesis not appendant on catalytic domain
S170E
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
Y307Q
site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type
DELTA323-375
murine autotaxin beta isoform, 863 amino acids total
DELTA323-375
murine autotaxin gamma isoform, 889 amino acids total
T210A
-
catalytically inactive
T210A
-
inactive enzyme, generation of a mouse line displaying an inactivated ATX gene product. Lethality of the ATX-/-embryos. ATX-dependent LPA production is due to the catalytic activity of the enzyme. Clone identified, by both PCR and Southern blot as targeted at the Atx locus
additional information
-
autotaxin gamma, share 100% identity with the splice variant NPP2gamma, except for the 25-amino acid insertion located between Glu593 and Glu594
additional information
autotaxin gamma, share 100% identity with the splice variant NPP2gamma, except for the 25-amino acid insertion located between Glu593 and Glu594
additional information
rhATX S48 site-directed mutagenesis, recombinant human ATX, creation of a full-length recombinant molecule by using prokaryotic cells. Shows lysoPLD enzymatic activity. hATX S48 Ser-48-C terminal of human ATX-T (L46720) cDNA is amplified. hATX S48 protein shows both lysoPLD and PDE activity
additional information
-
rhATX S48 site-directed mutagenesis, recombinant human ATX, creation of a full-length recombinant molecule by using prokaryotic cells. Shows lysoPLD enzymatic activity. hATX S48 Ser-48-C terminal of human ATX-T (L46720) cDNA is amplified. hATX S48 protein shows both lysoPLD and PDE activity
additional information
-
deletions of the amino acids N53 and N410 lead to a reduction of the molecular weight of ATX
additional information
-
experiment with ATX-deficient mice. ATX deficiency is lethal at the embryonic stage
additional information
-
generation of adipocyte-specific knockout FATX-KO mice
additional information
five potential N-glycosylation sites of NPP2, Asn-53, Asn-398, Asn-410, Asn-524, and Asn-806. Mutagenesis and deglycosylation experiments reveal that only the glycosylation of Asn-524 is essential for the expression of the catalytic and motility-stimulating activities of NPP2
additional information
-
NPP2-(1-594) lacking the nuclease-like domain does not exhibit any lysophospholipase-D or nucleotide phosphodiesterase activities
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.
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.
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.
Ward, W.H.J.; Fersht, A.R.
Asymmetry of tyrosyl-tRNA synthetase in solution
Biochemistry
27
1041-1049
1988
Homo sapiens
brenda
Fernandez-Gallardo, S.; Gijon, M.A.; Gracia, M.D.C.; Cano, E.; Sanchez Crespo, M.
Biosynthesis of platelet-activating factor in glandular gastric mucosa. Evidence for the involvement of the de novo pathway and modulation by fatty acids
Biochem. J.
254
707-714
1988
Rattus norvegicus
brenda
Kawasaki, T.; Snyder, F.
The metabolism of lyso-platelet-activating factor (1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine) by a calcium-dependent lysophospholipase D in rabbit kidney medulla
Biochim. Biophys. Acta
920
85-93
1987
Oryctolagus cuniculus
brenda
Tokumura, A.; Harada, K.; Fukazawa, K.; Tsukatani, H.
Involvement of lysophospholipase D in the production of lysophosphatidic acid in rat plasma
Biochim. Biophys. Acta
875
31-38
1986
Rattus norvegicus
brenda
Wykle, R.L.; Kraemer, W.F.; Schremmer, J.M.
Specificity of lysophospholipase D
Biochim. Biophys. Acta
619
58-67
1980
Rattus norvegicus
brenda
Wykle, R.L.; Kraemer, W.F.; Schremmer, J.M.
Studies of lysophospholipase D of rat liver and other tissues
Arch. Biochem. Biophys.
184
149-155
1977
Rattus norvegicus
brenda
Wykle, R.L.; Schremmer, J.M.
A lysophospholipase D pathway in the metabolism of ether-linked lipids in brain microsomes
J. Biol. Chem.
249
1742-1746
1974
Rattus norvegicus
brenda
Tokumura, A.; Nishioka, Y.; Yoshimoto, O.; Shinomiya, J.; Fukazawa, K.
Substrate specificity of lysophospholipase D which produces bioactive lysophosphatidic acids in rat plasma
Biochim. Biophys. Acta
1437
235-245
1999
Rattus norvegicus
brenda
Furukawa, M.; Muguruma, k.; Frenkel, R.A.; Johnston, J.M.
Metabolic fate of platelet-activating factor in the rat enterocyte: the role of a specifiv lysophospholipase D
Arch. Biochem. Biophys.
319
274-280
1995
Rattus norvegicus
brenda
Wykle, L.; Strum, J.C.
Lysophospholipase D
Methods Enzymol.
197
583-590
1991
Rattus norvegicus
brenda
Xie, Y.; Meier, K.E.
Lysophospholipase D and its role in LPA production
Cell. Signal.
16
975-981
2004
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
brenda
Kishi, Y.; Okudaira, S.; Kishi, M.; Hama, K.; Shida, D.; Kitayama, J.; Yamori, T.; Aoki, J.; Fujimaki, T.; Arai, H.
Autotaxin is overexpressed in glioblastoma multiforme and contributes to cell motility of glioblastoma by converting lysophosphatidylcoholine to lysophosphatidic acid
J. Biol. Chem.
281
17492-17500
2006
Homo sapiens
brenda
Song, J.; Clair, T.; Noh, J.H.; Eun, J.W.; Ryu, S.Y.; Lee, S.N.; Ahn, Y.M.; Kim, S.Y.; Lee, S.H.; Park, W.S.; Yoo, N.J.; Lee, J.Y.; Nam, S.W.
Autotaxin (lysoPLD/NPP2) protects fibroblasts from apoptosis through its enzymatic product, lysophosphatidic acid, utilizing albumin-bound substrate
Biochem. Biophys. Res. Commun.
337
967-975
2005
Homo sapiens
brenda
Tanaka, M.; Kishi, Y.; Takanezawa, Y.; Kakehi, Y.; Aoki, J.; Arai, H.
Prostatic acid phosphatase degrades lysophosphatidic acid in seminal plasma
FEBS Lett.
571
197-204
2004
Homo sapiens
brenda
Koike, S.; Keino-Masu, K.; Ohto, T.; Masu, M.
The N-terminal hydrophobic sequence of autotaxin (ENPP2) functions as a signal peptide
Genes Cells
11
133-142
2006
Rattus norvegicus
brenda
Kehlen, A.; Englert, N.; Seifert, A.; Klonisch, T.; Dralle, H.; Langner, J.; Hoang-Vu, C.
Expression, regulation and function of autotaxin in thyroid carcinomas
Int. J. Cancer
109
833-838
2004
Homo sapiens
brenda
Hama, K.; Aoki, J.; Fukaya, M.; Kishi, Y.; Sakai, T.; Suzuki, R.; Ohta, H.; Yamori, T.; Watanabe, M.; Chun, J.; Arai, H.
Lysophosphatidic acid and autotaxin stimulate cell motility of neoplastic and non-neoplastic cells through LPA1
J. Biol. Chem.
279
17634-17639
2004
Mus musculus
brenda
van Meeteren, L.A.; Ruurs, P.; Christodoulou, E.; Goding, J.W.; Takakusa, H.; Kikuchi, K.; Perrakis, A.; Nagano, T.; Moolenaar, W.H.
Inhibition of autotaxin by lysophosphatidic acid and sphingosine 1-phosphate
J. Biol. Chem.
280
21155-21161
2005
Streptomyces chromofuscus
brenda
Jansen, S.; Stefan, C.; Creemers, J.W.; Waelkens, E.; Van Eynde, A.; Stalmans, W.; Bollen, M.
Proteolytic maturation and activation of autotaxin (NPP2), a secreted metastasis-enhancing lysophospholipase D
J. Cell Sci.
118
3081-3089
2005
Rattus norvegicus
brenda
Clair, T.; Koh, E.; Ptaszynska, M.; Bandle, R.W.; Liotta, L.A.; Schiffmann, E.; Stracke, M.L.
L-histidine inhibits production of lysophosphatidic acid by the tumor-associated cytokine, autotaxin
Lipids Health Dis.
4
DOI:10.1186/1476-511X-4-5
2005
Homo sapiens
-
brenda
Ferguson, C.G.; Bigman, C.S.; Richardson, R.D.; van Meeteren, L.A.; Moolenaar, W.H.; Prestwich, G.D.
Fluorogenic phospholipid substrate to detect lysophospholipase D/autotaxin activity
Org. Lett.
8
2023-2026
2006
Homo sapiens
brenda
Clair, T.; Koh, E.; Ptaszynska, M.; Bandle, R.W.; Liotta, L.A.; Schiffmann, E.; Stracke, M.L.
L-histidine inhibits production of lysophosphatidic acid by the tumor-associated cytokine, autotaxin
Lipids Health Dis.
4
5-5
2005
Homo sapiens
brenda
Sugimoto, S.; Sugimoto, H.; Aoyama, C.; Aso, C.; Mori, M.; Izumi, T.
Purification and characterization of lysophospholipase D from rat brain
Biochim. Biophys. Acta
1761
1410-1418
2006
Rattus norvegicus
brenda
Morishige, J.; Touchika, K.; Tanaka, T.; Satouchi, K.; Fukuzawa, K.; Tokumura, A.
Production of bioactive lysophosphatidic acid by lysophospholipase D in hen egg white
Biochim. Biophys. Acta
1771
491-499
2007
Gallus gallus
brenda
Pradere, J.P.; Tarnus, E.; Gres, S.; Valet, P.; Saulnier-Blache, J.S.
Secretion and lysophospholipase D activity of autotaxin by adipocytes are controlled by N-glycosylation and signal peptidase
Biochim. Biophys. Acta
1771
93-102
2007
Mus musculus
brenda
Savaskan, N.E.; Rocha, L.; Kotter, M.R.; Baer, A.; Lubec, G.; van Meeteren, L.A.; Kishi, Y.; Aoki, J.; Moolenaar, W.H.; Nitsch, R.; Braeuer, A.U.
Autotaxin (NPP-2) in the brain: cell type-specific expression and regulation during development and after neurotrauma
Cell. Mol. Life Sci.
64
230-243
2007
Mus musculus, Rattus norvegicus
brenda
Nakamura, K.; Ohkawa, R.; Okubo, S.; Tozuka, M.; Okada, M.; Aoki, S.; Aoki, J.; Arai, H.; Ikeda, H.; Yatomi, Y.
Measurement of lysophospholipase D/autotaxin activity in human serum samples
Clin. Biochem.
40
274-277
2007
Homo sapiens
brenda
Nakamura, K.; Nangaku, M.; Ohkawa, R.; Okubo, S.; Yokota, H.; Ikeda, H.; Aoki, J.; Yatomi, Y.
Analysis of serum and urinary lysophospholipase D/autotaxin in nephrotic syndrome
Clin. Chem. Lab. Med.
46
150-151
2008
Homo sapiens
brenda
Ferry, G.; Giganti, A.; Coge, F.; Bertaux, F.; Thiam, K.; Boutin, J.A.
Functional invalidation of the autotaxin gene by a single amino acid mutation in mouse is lethal
FEBS Lett.
581
3572-3578
2007
Mus musculus
brenda
Liu, X.W.; Sok, D.E.; Yook, H.S.; Sohn, C.B.; Chung, Y.J.; Kim, M.R.
Inhibition of lysophospholipase D activity by unsaturated lysophosphatidic acids or seed extracts containing 1-linoleoyl and 1-oleoyl lysophosphatidic acid
J. Agric. Food Chem.
55
8717-8722
2007
Bos taurus
brenda
Tanaka, M.; Okudaira, S.; Kishi, Y.; Ohkawa, R.; Iseki, S.; Ota, M.; Noji, S.; Yatomi, Y.; Aoki, J.; Arai, H.
Autotaxin stabilizes blood vessels and is required for embryonic vasculature by producing lysophosphatidic acid
J. Biol. Chem.
281
25822-25830
2006
Mus musculus
brenda
Jansen, S.; Callewaert, N.; Dewerte, I.; Andries, M.; Ceulemans, H.; Bollen, M.
An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D
J. Biol. Chem.
282
11084-11091
2007
Rattus norvegicus (Q64610)
brenda
Giganti, A.; Rodriguez, M.; Fould, B.; Moulharat, N.; Coge, F.; Chomarat, P.; Galizzi, J.P.; Valet, P.; Saulnier-Blache, J.S.; Boutin, J.A.; Ferry, G.
Murine and human autotaxin alpha, beta, gamma isoforms: Gene organization, tissue distribution and biochemical characterization
J. Biol. Chem.
283
7776-7789
2008
Homo sapiens, Homo sapiens (Q13822), Mus musculus, Mus musculus (Q9R1E6)
brenda
Morris, A.J.; Smyth, S.S.
Measurement of autotaxin/lysophospholipase D activity
Methods Enzymol.
434
89-104
2007
Homo sapiens, Mammalia
brenda
van Meeteren, L.A.; Ruurs, P.; Stortelers, C.; Bouwman, P.; van Rooijen, M.A.; Pradere, J.P.; Pettit, T.R.; Wakelam, M.J.; Saulnier-Blache, J.S.; Mummery, C.L.; Moolenaar, W.H.; Jonkers, J.
Autotaxin, a secreted lysophospholipase D, is essential for blood vessel formation during development
Mol. Cell. Biol.
26
5015-5022
2006
Mus musculus
brenda
Rose, T.M.; Prestwich, G.D.
Synthesis and evaluation of fluorogenic substrates for phospholipase D and phospholipase C
Org. Lett.
8
2575-2578
2006
Bacillus cereus, Clostridium perfringens
brenda
Haga, A.; Hashimoto, K.; Tanaka, N.; Nakamura, K.T.; Deyashiki, Y.
Scalable purification and characterization of the extracellular domain of human autotaxin from prokaryotic cells
Protein Expr. Purif.
59
9-17
2008
Homo sapiens (Q13822), Homo sapiens
brenda
Nakasaki, T.; Tanaka, T.; Okudaira, S.; Hirosawa, M.; Umemoto, E.; Otani, K.; Jin, S.; Bai, Z.; Hayasaka, H.; Fukui, Y.; Aozasa, K.; Fujita, N.; Tsuruo, T.; Ozono, K.; Aoki, J.; Miyasaka, M.
Involvement of the lysophosphatidic acid-generating enzyme autotaxin in lymphocyte-endothelial cell interactions
Am. J. Pathol.
173
1566-1576
2008
Mus musculus
brenda
Yuelling, L.M.; Fuss, B.
Autotaxin (ATX): a multi-functional and multi-modular protein possessing enzymatic lysoPLD activity and matricellular properties
Biochim. Biophys. Acta
1781
525-530
2008
Homo sapiens
brenda
van Meeteren, L.A.; Brinkmann, V.; Saulnier-Blache, J.S.; Lynch, K.R.; Moolenaar, W.H.
Anticancer activity of FTY720: phosphorylated FTY720 inhibits autotaxin, a metastasis-enhancing and angiogenic lysophospholipase D
Cancer Lett.
266
203-208
2008
Homo sapiens
brenda
Federico, L.; Pamuklar, Z.; Smyth, S.S.; Morris, A.J.
Therapeutic potential of autotaxin/lysophospholipase d inhibitors
Curr. Drug Targets
9
698-708
2008
Mus musculus
brenda
Pamuklar, Z.; Federico, L.; Liu, S.; Umezu-Goto, M.; Dong, A.; Panchatcharam, M.; Fulerson, Z.; Berdyshev, E.; Natarajan, V.; Fang, X.; van Meeteren, L.A.; Moolenaar, W.H.; Mills, G.B.; Morris, A.J.; Smyth, S.S.
Autotaxin/lysopholipase D and lysophosphatidic acid regulate murine hemostasis and thrombosis
J. Biol. Chem.
284
7385-7394
2009
Homo sapiens
brenda
Tokumura, A.; Kume, T.; Taira, S.; Yasuda, K.; Kanzaki, H.
Altered activity of lysophospholipase D, which produces bioactive lysophosphatidic acid and choline, in serum from women with pathological pregnancy
Mol. Hum. Reprod.
15
301-310
2009
Homo sapiens
brenda
Kanda, H.; Newton, R.; Klein, R.; Morita, Y.; Gunn, M.D.; Rosen, S.D.
Autotaxin, an ectoenzyme that produces lysophosphatidic acid, promotes the entry of lymphocytes into secondary lymphoid organs
Nat. Immunol.
9
415-423
2008
Mus musculus
brenda
Seifert, A.; Klonisch, T.; Wulfaenger, J.; Haag, F.; Dralle, H.; Langner, J.; Hoang-Vu, C.; Kehlen, A.
The cellular localization of autotaxin impacts on its biological functions in human thyroid carcinoma cells
Oncol. Rep.
19
1485-1491
2008
Homo sapiens (Q13822), Homo sapiens
brenda
Wakelam, M.; Powner, D.; Pettitt, T.
Determination of phospholipase D, lysophospholipase D and DG kinase signaling pathways in disease states by mass spectrometry
Adv. Enzyme Regul.
48
254-260
2008
Homo sapiens
brenda
Iwasawa, Y.; Fujii, T.; Nagamatsu, T.; Kawana, K.; Okudaira, S.; Miura, S.; Matsumoto, J.; Tomio, A.; Hyodo, H.; Yamashita, T.; Oda, K.; Kozuma, S.; Aoki, J.; Yatomi, Y.; Taketani, Y.
Expression of autotaxin, an ectoenzyme that produces lysophosphatidic acid, in human placenta
Am. J. Reprod. Immunol.
62
90-95
2009
Homo sapiens
brenda
Li, S.; Zhang, J.
Lipopolysaccharide induces autotaxin expression in human monocytic THP-1 cells
Biochem. Biophys. Res. Commun.
378
264-268
2009
Homo sapiens
brenda
Hoeglund, A.B.; Howard, A.L.; Wanjala, I.W.; Pham, T.C.; Parrill, A.L.; Baker, D.L.
Characterization of non-lipid autotaxin inhibitors
Bioorg. Med. Chem.
18
769-776
2010
Homo sapiens
brenda
Jansen, S.; Andries, M.; Vekemans, K.; Vanbilloen, H.; Verbruggen, A.; Bollen, M.
Rapid clearance of the circulating metastatic factor autotaxin by the scavenger receptors of liver sinusoidal endothelial cells
Cancer Lett.
284
216-221
2009
Rattus norvegicus
brenda
Liu, S.; Murph, M.; Panupinthu, N.; Mills, G.B.
ATX-LPA receptor axis in inflammation and cancer
Cell Cycle
8
3695-3701
2009
Homo sapiens
brenda
Fotopoulou, S.; Oikonomou, N.; Grigorieva, E.; Nikitopoulou, I.; Paparountas, T.; Thanassopoulou, A.; Zhao, Z.; Xu, Y.; Kontoyiannis, D.L.; Remboutsika, E.; Aidinis, V.
ATX expression and LPA signalling are vital for the development of the nervous system
Dev. Biol.
339
451-464
2010
Mus musculus
brenda
Endo, T.; Kano, K.; Motoki, R.; Hama, K.; Okudaira, S.; Ishida, M.; Ogiso, H.; Tanaka, M.; Matsuki, N.; Taguchi, R.; Kanai, M.; Shibasaki, M.; Arai, H.; Aoki, J.
Lysophosphatidylmethanol is a pan lysophosphatidic acid receptor agonist and is produced by autotaxin in blood
J. Biochem.
146
283-293
2009
Mus musculus
brenda
Jansen, S.; Andries, M.; Derua, R.; Waelkens, E.; Bollen, M.
Domain interplay mediated by an essential disulfide linkage is critical for the activity and secretion of the metastasis-promoting enzyme autotaxin
J. Biol. Chem.
284
14296-14302
2009
Rattus norvegicus
brenda
Koike, S.; Keino-Masu, K.; Ohto, T.; Sugiyama, F.; Takahashi, S.; Masu, M.
Autotaxin/lysophospholipase D-mediated lysophosphatidic acid signaling is required to form distinctive large lysosomes in the visceral endoderm cells of the mouse yolk sac
J. Biol. Chem.
284
33561-33570
2009
Mus musculus
brenda
Hoeglund, A.B.; Bostic, H.E.; Howard, A.L.; Wanjala, I.W.; Best, M.D.; Baker, D.L.; Parrill, A.L.
Optimization of a pipemidic acid autotaxin inhibitor
J. Med. Chem.
53
1056-1066
2010
Homo sapiens
brenda
Ma, L.; Uchida, H.; Nagai, J.; Inoue, M.; Aoki, J.; Ueda, H.
Evidence for de novo synthesis of lysophosphatidic acid in the spinal cord through phospholipase A2 and autotaxin in nerve injury-induced neuropathic pain
J. Pharmacol. Exp. Ther.
333
540-546
2010
Mus musculus
brenda
Koh, E.; Bandle, R.W.; Roberts, D.D.; Stracke, M.L.; Clair, T.
Novel point mutations attenuate autotaxin activity
Lipids Health Dis.
8
4-4
2009
Homo sapiens
brenda
Im, E.; Motiejunaite, R.; Aranda, J.; Park, E.Y.; Federico, L.; Kim, T.I.; Clair, T.; Stracke, M.L.; Smyth, S.; Kazlauskas, A.
PLCgamma activation drives increased production of autotaxin in endothelial cells and LPA-dependent regression
Mol. Cell. Biol.
30
2401-2410
2010
Mus musculus
brenda
David, M.; Wannecq, E.; Descotes, F.; Jansen, S.; Deux, B.; Ribeiro, J.; Serre, C.M.; Gres, S.; Bendriss-Vermare, N.; Bollen, M.; Saez, S.; Aoki, J.; Saulnier-Blache, J.S.; Clezardin, P.; Peyruchaud, O.
Cancer cell expression of autotaxin controls bone metastasis formation in mouse through lysophosphatidic acid-dependent activation of osteoclasts
PLoS ONE
5
e9741
2010
Homo sapiens, Mus musculus
brenda
Albers, H.M.; Dong, A.; van Meeteren, L.A.; Egan, D.A.; Sunkara, M.; van Tilburg, E.W.; Schuurman, K.; van Tellingen, O.; Morris, A.J.; Smyth, S.S.; Moolenaar, W.H.; Ovaa, H.
Boronic acid-based inhibitor of autotaxin reveals rapid turnover of LPA in the circulation
Proc. Natl. Acad. Sci. USA
107
7257-7262
2010
Mus musculus
brenda
Block, R.C.; Duff, R.; Lawrence, P.; Kakinami, L.; Brenna, J.T.; Shearer, G.C.; Meednu, N.; Mousa, S.; Friedman, A.; Harris, W.S.; Larson, M.; Georas, S.
The effects of EPA, DHA, and aspirin ingestion on plasma lysophospholipids and autotaxin
Prostaglandins Leukot. Essent. Fatty Acids
82
87-95
2010
Homo sapiens
brenda
Hausmann, J.; Christodoulou, E.; Kasiem, M.; De Marco, V.; van Meeteren, L.A.; Moolenaar, W.H.; Axford, D.; Owen, R.L.; Evans, G.; Perrakis, A.
Mammalian cell expression, purification, crystallization and microcrystal data collection of autotaxin/ENPP2, a secreted mammalian glycoprotein
Acta Crystallogr. Sect. F
66
1130-1135
2010
Rattus norvegicus (Q64610)
brenda
Inoue, K.; Tanaka, N.; Haga, A.; Yamasaki, K.; Umeda, T.; Kusakabe, Y.; Sakamoto, Y.; Nonaka, T.; Deyashiki, Y.; Nakamura, K.T.
Crystallization and preliminary X-ray crystallographic analysis of human autotaxin
Acta Crystallogr. Sect. F
67
450-453
2011
Homo sapiens
brenda
Tania, M.; Khan, A.; Zhang, H.; Li, J.; Song, Y.
Autotaxin: a protein with two faces
Biochem. Biophys. Res. Commun.
401
493-497
2010
Homo sapiens
brenda
Zhao, J.; He, D.; Berdyshev, E.; Zhong, M.; Salgia, R.; Morris, A.J.; Smyth, S.S.; Natarajan, V.; Zhao, Y.
Autotaxin induces lung epithelial cell migration through lysoPLD activity-dependent and -independent pathways
Biochem. J.
439
45-55
2011
Homo sapiens
brenda
Aoyama, C.; Sugimoto, H.; Ando, H.; Yamashita, S.; Horibata, Y.; Sugimoto, S.; Satou, M.
The heterotrimeric G protein subunits Galphaq and Gbeta1 have lysophospholipase D activity
Biochem. J.
440
241-250
2011
Rattus norvegicus
brenda
Tsuboi, K.; Okamoto, Y.; Ikematsu, N.; Inoue, M.; Shimizu, Y.; Uyama, T.; Wang, J.; Deutsch, D.G.; Burns, M.P.; Ulloa, N.M.; Tokumura, A.; Ueda, N.
Enzymatic formation of N-acylethanolamines from N-acylethanolamine plasmalogen through N-acylphosphatidylethanolamine-hydrolyzing phospholipase D-dependent and -independent pathways
Biochim. Biophys. Acta
1811
565-577
2011
Mus musculus
brenda
East, J.E.; Kennedy, A.J.; Tomsig, J.L.; De Leon, A.R.; Lynch, K.R.; Macdonald, T.L.
Synthesis and structure-activity relationships of tyrosine-based inhibitors of autotaxin (ATX)
Bioorg. Med. Chem. Lett.
20
7132-7136
2010
Homo sapiens
brenda
Jiang, G.; Madan, D.; Prestwich, G.D.
Aromatic phosphonates inhibit the lysophospholipase D activity of autotaxin
Bioorg. Med. Chem. Lett.
21
5098-5101
2011
Homo sapiens
brenda
Song, Y.; Dilger, E.; Bell, J.; Barton, W.A.; Fang, X.
Large scale purification and characterization of recombinant human autotaxin/lysophospholipase D from mammalian cells
BMB Rep.
43
541-546
2010
Homo sapiens
brenda
Ueda, K.; Yoshihara, M.; Nakao, M.; Tanaka, T.; Sano, S.; Fukuzawa, K.; Tokumura, A.
Evaluation of inhibitory actions of flavonols and related substances on lysophospholipase D activity of serum autotaxin by a convenient assay using a chromogenic substrate
J. Agric. Food Chem.
58
6053-6063
2010
Homo sapiens
brenda
Saunders, L.P.; Cao, W.; Chang, W.C.; Albright, R.A.; Braddock, D.T.; De La Cruz, E.M.
Kinetic analysis of autotaxin reveals substrate-specific catalytic pathways and a mechanism for lysophosphatidic acid distribution
J. Biol. Chem.
286
30130-30141
2011
Homo sapiens
brenda
Fulkerson, Z.; Wu, T.; Sunkara, M.; Kooi, C.V.; Morris, A.J.; Smyth, S.S.
Binding of autotaxin to integrins localizes lysophosphatidic acid production to platelets and mammalian cells
J. Biol. Chem.
286
34654-34663
2011
Homo sapiens
brenda
Yukiura, H.; Hama, K.; Nakanaga, K.; Tanaka, M.; Asaoka, Y.; Okudaira, S.; Arima, N.; Inoue, A.; Hashimoto, T.; Arai, H.; Kawahara, A.; Nishina, H.; Aoki, J.
Autotaxin regulates vascular development via multiple lysophosphatidic acid (LPA) receptors in zebrafish
J. Biol. Chem.
286
43972-43983
2011
Danio rerio, Danio rerio AB
brenda
Hausmann, J.; Kamtekar, S.; Christodoulou, E.; Day, J.E.; Wu, T.; Fulkerson, Z.; Albers, H.M.; van Meeteren, L.A.; Houben, A.J.; van Zeijl, L.; Jansen, S.; Andries, M.; Hall, T.; Pegg, L.E.; Benson, T.E.; Kasiem, M.; Harlos, K.; Kooi, C.W.; Smyth, S.S.; Ovaa, H.; Bollen, M.; Morris, A.J.; Moolenaar, W.H.; Perrakis, A.
Structural basis of substrate discrimination and integrin binding by autotaxin
Nat. Struct. Mol. Biol.
18
198-204
2011
Rattus norvegicus (Q64610)
brenda
Nishimasu, H.; Okudaira, S.; Hama, K.; Mihara, E.; Dohmae, N.; Inoue, A.; Ishitani, R.; Takagi, J.; Aoki, J.; Nureki, O.
Crystal structure of autotaxin and insight into GPCR activation by lipid mediators
Nat. Struct. Mol. Biol.
18
205-212
2011
Mus musculus
brenda
Kawaguchi, M.; Okabe, T.; Okudaira, S.; Nishimasu, H.; Ishitani, R.; Kojima, H.; Nureki, O.; Aoki, J.; Nagano, T.
Screening and X-ray crystal structure-based optimization of autotaxin (ENPP2) inhibitors, using a newly developed fluorescence probe
ACS Chem. Biol.
8
1713-1721
2013
Danio rerio, Mus musculus (Q9R1E6)
brenda
Hausmann, J.; Perrakis, A.; Moolenaar, W.H.
Structure-function relationships of autotaxin, a secreted lysophospholipase D
Adv. Biol. Regul.
53
112-117
2013
Rattus norvegicus
brenda
Rancoule, C.; Dusaulcy, R.; Treguer, K.; Gres, S.; Attane, C.; Saulnier-Blache, J.S.
Involvement of autotaxin/lysophosphatidic acid signaling in obesity and impaired glucose homeostasis
Biochimie
96
140-143
2014
Homo sapiens, Mus musculus
brenda
Ino, M.; Shimizu, Y.; Tanaka, T.; Tokumura, A.
Alterations of plasma levels of lysophosphatidic acid in response to fasting of rats
Biol. Pharm. Bull.
35
2059-2063
2012
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Wu, T.; Kooi, C.V.; Shah, P.; Charnigo, R.; Huang, C.; Smyth, S.S.; Morris, A.J.
Integrin-mediated cell surface recruitment of autotaxin promotes persistent directional cell migration
FASEB J.
28
861-870
2014
Homo sapiens
brenda
Perrakis, A.; Moolenaar, W.H.
Autotaxin: structure-function and signaling
J. Lipid Res.
55
1010-1018
2014
Homo sapiens, Mus musculus, Streptomyces chromofuscus, Loxosceles sp.
brenda
Hozumi, H.; Hokari, R.; Kurihara, C.; Narimatsu, K.; Sato, H.; Sato, S.; Ueda, T.; Higashiyama, M.; Okada, Y.; Watanabe, C.; Komoto, S.; Tomita, K.; Kawaguchi, A.; Nagao, S.; Miura, S.
Involvement of autotaxin/lysophospholipase D expression in intestinal vessels in aggravation of intestinal damage through lymphocyte migration
Lab. Invest.
93
508-519
2013
Homo sapiens, Mus musculus, Mus musculus BALB/c
brenda
Morishige, J.; Uto, Y.; Hori, H.; Satouchi, K.; Yoshiomoto, T.; Tokumura, A.
Lysophosphatidic acid produced by hen egg white lysophospholipase D induces vascular development on extraembryonic membranes
Lipids
48
251-262
2013
Gallus gallus
brenda
Tokumura, A.; Taira, S.; Kikuchi, M.; Tsutsumi, T.; Shimizu, Y.; Watsky, M.A.
Lysophospholipids and lysophospholipase D in rabbit aqueous humor following corneal injury
Prostaglandins Other Lipid Mediat.
97
83-89
2012
Oryctolagus cuniculus
brenda
Borchani, L.; Sassi, A.; Ben Gharsa, H.; Safra, I.; Shahbazzadeh, D.; Ben Lasfar, Z.; El Ayeb, M.
The pathological effects of heminecrolysin, a dermonecrotic toxin from Hemiscorpius lepturus scorpion venom are mediated through its lysophospholipase D activity
Toxicon
68
30-39
2013
Hemiscorpius lepturus
brenda
Tsuboi, K.; Okamoto, Y.; Rahman, I.A.; Uyama, T.; Inoue, T.; Tokumura, A.; Ueda, N.
Glycerophosphodiesterase GDE4 as a novel lysophospholipase D a possible involvement in bioactive N-acylethanolamine biosynthesis
Biochim. Biophys. Acta
1851
537-548
2015
Mus musculus (Q9CRY7), Mus musculus
brenda
Rahman, I.A.; Tsuboi, K.; Hussain, Z.; Yamashita, R.; Okamoto, Y.; Uyama, T.; Yamazaki, N.; Tanaka, T.; Tokumura, A.; Ueda, N.
Calcium-dependent generation of N-acylethanolamines and lysophosphatidic acids by glycerophosphodiesterase GDE7
Biochim. Biophys. Acta
1861
1881-1892
2016
Homo sapiens (Q7L5L3), Homo sapiens, Mus musculus (Q99LY2), Mus musculus
brenda
Kise, R.; Okasato, R.; Kano, K.; Inoue, A.; Kawahara, A.; Aoki, J.
Identification and biochemical characterization of a second zebrafish autotaxin gene
J. Biochem.
165
269-275
2019
Danio rerio
brenda
Ohshima, N.; Kudo, T.; Yamashita, Y.; Mariggio, S.; Araki, M.; Honda, A.; Nagano, T.; Isaji, C.; Kato, N.; Corda, D.; Izumi, T.; Yanaka, N.
New members of the mammalian glycerophosphodiester phosphodiesterase family GDE4 and GDE7 produce lysophosphatidic acid by lysophospholipase D activity
J. Biol. Chem.
290
4260-4271
2015
Mus musculus (Q9CRY7)
brenda
Mazzocca, A.; Schoenauer, L.M.; De Nola, R.; Lippolis, A.; Marrano, T.; Loverro, M.; Sabba, C.; Di Naro, E.
Autotaxin is a novel molecular identifier of type I endometrial cancer
Med. Oncol.
35
157
2018
Homo sapiens (Q13822), Homo sapiens
brenda