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.
1,2-diarachidonoyl-sn-phosphatidic acid + H2O
2-arachidonoyl-sn-phosphatidic acid + arachidonoate
246% activity compared to 1,2-dioleoyl-sn-phosphatidic acid
-
-
?
1,2-dielaidoyl-sn-phosphatidic acid + H2O
2-elaidoyl-sn-phosphatidic acid + elaidate
40% activity compared to 1,2-dioleoyl-sn-phosphatidic acid
-
-
?
1,2-dilinolenoyl-sn-phosphatidic acid + H2O
2-linolenoyl-sn-phosphatidic acid + linolenate
235% activity compared to 1,2-dioleoyl-sn-phosphatidic acid
-
-
?
1,2-dilinoleoyl-sn-phosphatidic acid + H2O
2-linoleoyl-sn-phosphatidic acid + linoleate
214% activity compared to 1,2-dioleoyl-sn-phosphatidic acid
-
-
?
1,2-dioleoyl-3-phosphatidylcholine + H2O
2-oleoyl-3-phosphatidylcholine + oleate
-
-
-
?
1,2-dioleoyl-3-phosphatidylethanolamine + H2O
2-oleoyl-3-phosphatidylethanolamine + oleate
-
-
-
?
1,2-dioleoyl-3-phosphatidylserine + H2O
2-oleoyl-3-phosphatidylserine + oleate
-
-
-
?
1,2-dioleoyl-phosphatidylcholine + H2O
2-oleoyl-phosphatidylcholine + oleate
-
-
-
?
1,2-dioleoyl-phosphatidylglycerol + H2O
2-oleoyl-phosphatidylglycerol + oleate
-
-
-
?
1,2-dioleoyl-sn-glycero-3-phospho-(1-rac-glycerol) + H2O
2-oleoyl-sn-glycero-3-phospho-(1-rac-glycerol) + oleate
-
-
-
-
?
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + H2O
2-oleoyl-sn-glycero-3-phosphoethanolamine + oleate
-
-
-
-
?
1,2-dioleoyl-sn-phosphatidic acid + H2O
2-oleoyl-sn-phosphatidic acid + oleate
100% activity
-
-
?
1,2-dioleoyl-sn-phosphatidylcholine + H2O
2-oleoyl-sn-phosphatidylcholine + oleate
5% activity compared to 1-dioleoyl-sn-phosphatidic acid
-
-
?
1,2-dioleoyl-sn-phosphatidylethanolamine + H2O
2-oleoyl-sn-phosphatidylethanolamine + oleate
11% activity compared to 1-dioleoyl-sn-phosphatidic acid
-
-
?
1,2-dioleoyl-sn-phosphatidylinositol + H2O
2-oleoyl-sn-phosphatidylinositol + oleate
14% activity compared to 1-dioleoyl-sn-phosphatidic acid
-
-
?
1,2-dipetroselinoyl-sn-phosphatidic acid + H2O
2-petroselinoyl-sn-phosphatidic acid + petroselinate
21% activity compared to 1-dioleoyl-sn-phosphatidic acid
-
-
?
1-oleyl-2-arachidonoyl-phosphatidylinositol + H2O
2-arachidonoyl-lysophosphatidylinositol + oleate
-
-
-
?
1-palmitoyl-2-arachidonoyl-sn-phosphatdidylcholine + H2O
2-arachidonoyl-sn-phosphatidylcholine + palmitate
-
-
-
?
1-palmitoyl-2-arachidonoyl-sn-phosphatdidylethanolamine + H2O
2-arachidonoyl-sn-phosphatidylethanolamine + palmitate
-
-
-
?
1-palmitoyl-2-oleoyl-sn-3-phosphatidic acid + H2O
2-oleoyl-sn-3-phosphatidic acid + palmitate
-
KIAA0725p possesses phospholipase A1 activity preferentially for phosphatidic acid
-
-
?
1-palmitoyl-2-oleoyl-sn-3-phosphatidylglycerol + H2O
2-oleoyl-sn-3-phosphatidylglycerol + palmitate
-
-
-
-
?
1-palmitoyl-2-oleoyl-sn-3-phosphatidylserine + H2O
2-oleoyl-sn-3-phosphatidylserine + palmitate
-
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine + H2O
2-oleoyl-sn-glycero-3-phosphatidylcholine + palmitate
-
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1-racglycerol) + H2O
2-oleoyl-sn-glycero-3-phospho-(1-rac-glycerol) + palmitate
-
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine + H2O
2-oleoyl-sn-glycero-3-phosphoethanolamine + palmitate
1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine + H2O
2-oleoyl-sn-glycerol-3-phosphocholine + palmitate
-
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphoethanolamine + H2O
2-oleoyl-sn-glycerol-3-phosphoethanolamine + palmitate
-
-
-
-
?
1-palmitoyl-2-oleoyl-sn-phosphatidic acid + H2O
2-oleoyl-sn-phosphatidic acid + palmitate
24% activity compared to 1-dioleoyl-sn-phosphatidic acid
-
-
?
1-stearoyl-2-arachidonoyl-phosphatidylinositol + H2O
2-arachidonoyl-lysophosphatidylinositol + stearate
-
-
-
?
1-stearoyl-2-arachidonoyl-sn-phosphatidic acid + H2O
2-arachidonoyl-sn-phosphatidic acid + stearate
1-stearoyl-2-arachidonoyl-sn-phosphatidylcholine + H2O
2-arachidonoyl-sn-phosphatidylcholine + stearate
-
-
-
?
1-stearoyl-2-arachidonoyl-sn-phosphatidylinositol + H2O
2-arachidonoyl-sn-phosphatidylinositol + stearate
-
-
-
?
1-stearoyl-2-oleoyl-sn-glycero-3-phospho-(1-rac-glycerol) + H2O
2-oleoyl-sn-glycero-3-phospho-(1-rac-glycerol) + stearate
-
-
-
-
?
1-stearoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine + H2O
2-oleoyl-sn-glycero-3-phosphoethanolamine + stearate
-
-
-
-
?
a 1,2-diacyl-sn-glycerol 3-phosphate + H2O
a 2-acyl-sn-glycerol 3-phosphate + a fatty acid
-
-
-
?
cardiolipin + H2O
?
-
-
-
-
?
phosphatidylinositol + H2O
lysophosphatidylinositol + ?
-
-
-
?
phosphatidylserine + H2O
lyso-phosphatidylserine + ?
-
-
-
?
sn-1,2-dioleoyl-phosphatidic acid + H2O
2-oleoyl-sn-phosphatidic acid + oleate
-
-
-
?
sn-1-palmitoyl-2-oleoyl-phosphatidic acid + H2O
2-oleoyl-sn-phosphatidic acid + palmitate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
additional information
?
-
the enzyme hydrolyzes phosphatidic acid 5fold faster than phosphatidylcholine and 3fold faster than phosphatidylinositol
-
-
-
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine + H2O
2-oleoyl-sn-glycero-3-phosphoethanolamine + palmitate
-
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine + H2O
2-oleoyl-sn-glycero-3-phosphoethanolamine + palmitate
-
-
-
-
?
1-stearoyl-2-arachidonoyl-sn-phosphatidic acid + H2O
2-arachidonoyl-sn-phosphatidic acid + stearate
-
-
-
?
1-stearoyl-2-arachidonoyl-sn-phosphatidic acid + H2O
2-arachidonoyl-sn-phosphatidic acid + stearate
31% activity compared to 1-dioleoyl-sn-phosphatidic acid
-
-
?
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.
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.
malfunction
deleterious mutations in the enzyme cause the SPG28 subtype of the neurological disease Hereditary Spastic Paraplegia which is characterized by axonal neuropathy and gait impairments. Enzyme inactivation causes a substantial decrease in polyunsaturated lysophosphatidylinositol lipids and an corresponding increase in phosphatidylinositol lipids
malfunction
enzyme depletion causes enlargement of early endosomes and stimulated tabulation of recycling endosomes positive for phosphatidic acid-binding proteins syndapin2 and MICAL-L1. Enzyme knockout enhances transferrin recycling from recycling endosomes to the cell surface
malfunction
enzyme downregulation reduces in vitro colon cancer cell viability and increases apoptosis rate, without affecting normal cells
malfunction
enzyme gene disruption in mice causes sperm malformation due to mitochondrial organization defects
malfunction
enzyme mutations are responsible for hereditary spastic paraplegia
malfunction
enzyme mutations can lead to hereditary spastic paraplegia associated with retinal dystrophy and a pattern of neurodegeneration with brain iron accumulation
malfunction
-
the misregulation of the enzyme gene by Aft1/2 transcription factors alters cardiolipin metabolism and causes mitochondrial dysfunction in the cells
metabolism
-
overexpression of KIAA0725p causes dispersion of the endoplasmic reticulum-Golgi intermediate compartment and Golgi apparatus
metabolism
the enzyme regulates brain lysophospholipid and phosphatidylinositol content in vivo
metabolism
-
the phospholipase activity of the enzyme is required to allow access of the lipase to triglyceride molecules contained in the core of the lipid droplets
physiological function
the activity of the enzyme is necessary for the prevention of neurite elongation. The enzyme negatively controls the formation of a local phosphatidic acid-rich domain in recycling endosomes that serves as a membrane source for neurite outgrowth
physiological function
the enzyme plays a regulatory role in spermatogenesis or sperm function
physiological function
the enzyme regulates mitochondrial dynamics and is involved in the organization of mitochondria during spermiogenesis
physiological function
the enzyme supports colon cancer cell proliferation and survival
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.
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.
Dard, R.; Meyniel, C.; Touitou, V.; Stevanin, G.; Lamari, F.; Durr, A.; Ewenczyk, C.; Mochel, F.
Mutations in DDHD1, encoding a phospholipase A1, is a novel cause of retinopathy and neurodegeneration with brain iron accumulation
Eur. J. Med. Genet.
60
639-642
2017
Homo sapiens (Q8NEL9)
brenda
Lin, Q.; Higgs, H.N.; Glomset, J.A.
Membrane lipids have multiple effects on interfacial catalysis by a phosphatidic acid-preferring phospholipase A1 from bovine testis
Biochemistry
39
9335-9344
2000
Bos taurus (O46606)
brenda
Inloes, J.M.; Jing, H.; Cravatt, B.F.
The spastic paraplegia-associated phospholipase DDHD1 is a primary brain phosphatidylinositol lipase
Biochemistry
57
5759-5767
2018
Mus musculus (Q80YA3), Mus musculus
brenda
Yamashita, A.; Kumazawa, T.; Koga, H.; Suzuki, N.; Oka, S.; Sugiura, T.
Generation of lysophosphatidylinositol by DDHD domain containing 1 (DDHD1) Possible involvement of phospholipase D/phosphatidic acid in the activation of DDHD1
Biochim. Biophys. Acta
1801
711-720
2010
Homo sapiens (Q8NEL9)
brenda
Maemoto, Y.; Maruyama, T.; Nemoto, K.; Baba, T.; Motohashi, M.; Ito, A.; Tagaya, M.; Tani, K.
DDHD1, but not DDHD2, suppresses neurite outgrowth in SH-SY5Y and PC12 cells by regulating protein transport from recycling endosomes
Front. Cell Dev. Biol.
8
670
2020
Rattus norvegicus (Q3ZAU5)
brenda
Higgs, H.N.; Glomset, J.A.
Purification and properties of a phosphatidic acid-preferring phospholipase A1 from bovine testis. Examination of the molecular basis of its activation
J. Biol. Chem.
271
10874-10883
1996
Bos taurus (O46606)
brenda
Nakajima, K.; Sonoda, H.; Mizoguchi, T.; Aoki, J.; Arai, H.; Nagahama, M.; Tagaya, M.; Tani, K.
A novel phospholipase A1 with sequence homology to a mammalian Sec23p-interacting protein, p125
J. Biol. Chem.
277
11329-11335
2002
Homo sapiens
brenda
Baba, T.; Kashiwagi, Y.; Arimitsu, N.; Kogure, T.; Edo, A.; Maruyama, T.; Nakao, K.; Nakanishi, H.; Kinoshita, M.; Frohman, M.A.; Yamamoto, A.; Tani, K.
Phosphatidic acid (PA)-preferring phospholipase A1 regulates mitochondrial dynamics
J. Biol. Chem.
289
11497-11511
2014
Mus musculus (Q80YA3)
brenda
Yadav, P.K.; Rajasekharan, R.
Misregulation of a DDHD domain-containing lipase causes mitochondrial dysfunction in yeast
J. Biol. Chem.
291
18562-18581
2016
Saccharomyces cerevisiae
brenda
Matsumoto, N.; Nemoto-Sasaki, Y.; Oka, S.; Arai, S.; Wada, I.; Yamashita, A.
Phosphorylation of human phospholipase A1 DDHD1 at newly identified phosphosites affects its subcellular localization
J. Biol. Chem.
297
100851
2021
Homo sapiens (Q8NEL9)
brenda
Raimondo, S.; Cristaldi, M.; Fontana, S.; Saieva, L.; Monteleone, F.; Calabrese, G.; Giavaresi, G.; Parenti, R.; Alessandro, R.
The phospholipase DDHD1 as a new target in colorectal cancer therapy
J. Exp. Clin. Cancer Res.
37
82
2018
Homo sapiens (Q8NEL9), Homo sapiens
brenda
Arrese, E.L.; Patel, R.T.; Soulages, J.L.
The main triglyceride-lipase from the insect fat body is an active phospholipase A(1) identification and characterization
J. Lipid Res.
47
2656-2667
2006
Manduca sexta
brenda
Tani, K.; Baba, T.; Inoue, H.
The structures and functions of intracellular phospholipase A1 family proteins
Phospholipases in Health and Disease (ed. Tappia P.S. and Dhalla N.S.)
10
87-99
2014
Homo sapiens (Q8NEL9)
-
brenda
Higgs, H.N.; Glomset, J.A.
Identification of a phosphatidic acid-preferring phospholipase A1 from bovine brain and testis
Proc. Natl. Acad. Sci. USA
91
9574-9578
1994
Bos taurus (O46606)
brenda