The Enzyme Database

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EC 2.3.1.23     
Accepted name: 1-acylglycerophosphocholine O-acyltransferase
Reaction: acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
Other name(s): lysolecithin acyltransferase; 1-acyl-sn-glycero-3-phosphocholine acyltransferase; acyl coenzyme A-monoacylphosphatidylcholine acyltransferase; acyl-CoA:1-acyl-glycero-3-phosphocholine transacylase; lysophosphatide acyltransferase; lysophosphatidylcholine acyltransferase
Systematic name: acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase
Comments: Acts preferentially with unsaturated acyl-CoA derivatives. 1-Acyl-sn-glycero-3-phosphoinositol can also act as acceptor.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9027-64-9
References:
1.  Bell, R.M. and Coleman, R.A. Enzymes of glycerolipid synthesis in eukaryotes. Annu. Rev. Biochem. 49 (1980) 459–487. [DOI] [PMID: 6250446]
2.  Hill, E.E. and Lands, W.E.M. Incorporation of long-chain and polyunsaturated acids into phosphatidate and phosphatidylcholine. Biochim. Biophys. Acta 152 (1968) 645–648. [DOI] [PMID: 5661029]
3.  Miki, Y., Hosaka, K., Yamashita, S., Handa, H. and Numa, S. Acyl-acceptor specificities of 1-acylglycerolphosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase resolved from rat liver microsomes. Eur. J. Biochem. 81 (1977) 433–441. [DOI] [PMID: 598375]
4.  van den Bosch, H., van Golde, L.M.G., Eibl, H. and van Deenen, L.L.M. The acylation of 1-acylglycero-3-phosphorylcholines by rat-liver microsomes. Biochim. Biophys. Acta 144 (1967) 613–623. [DOI] [PMID: 6078124]
[EC 2.3.1.23 created 1972]
 
 
EC 2.3.1.51     
Accepted name: 1-acylglycerol-3-phosphate O-acyltransferase
Reaction: acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Other name(s): 1-acyl-sn-glycero-3-phosphate acyltransferase; 1-acyl-sn-glycerol 3-phosphate acyltransferase; 1-acylglycero-3-phosphate acyltransferase; 1-acylglycerolphosphate acyltransferase; 1-acylglycerophosphate acyltransferase; lysophosphatidic acid-acyltransferase
Systematic name: acyl-CoA:1-acyl-sn-glycerol-3-phosphate 2-O-acyltransferase
Comments: Acyl-[acyl-carrier protein] can also act as an acyl donor. The animal enzyme is specific for the transfer of unsaturated fatty acyl groups.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 51901-16-7
References:
1.  Frentzen, M., Heinz, E., McKeon, T.A. and Stumpf, P.K. Specificities and selectivities of glycerol-3-phosphate acyltransferase and monoacylglycerol-3-phosphate acyltransferase from pea and spinach chloroplasts. Eur. J. Biochem. 129 (1983) 629–636. [DOI] [PMID: 6825679]
2.  Hill, E.E. and Lands, W.E.M. Incorporation of long-chain and polyunsaturated acids into phosphatidate and phosphatidylcholine. Biochim. Biophys. Acta 152 (1968) 645–648. [DOI] [PMID: 5661029]
3.  Yamashita, S., Hosaka, K. and Numa, S. Acyl-donor specificities of partially purified 1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase from rat-liver microsomes. Eur. J. Biochem. 38 (1973) 25–31. [DOI] [PMID: 4774123]
[EC 2.3.1.51 created 1976, modified 1990]
 
 
EC 2.7.1.107     
Accepted name: diacylglycerol kinase (ATP)
Reaction: ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Glossary: 1,2-diacyl-sn-glycerol 3-phosphate = phosphatidate
Other name(s): diglyceride kinase (ambiguous); 1,2-diacylglycerol kinase (phosphorylating) (ambiguous); 1,2-diacylglycerol kinase (ambiguous); sn-1,2-diacylglycerol kinase (ambiguous); DG kinase (ambiguous); DGK (ambiguous); ATP:diacylglycerol phosphotransferase; arachidonoyl-specific diacylglycerol kinase; diacylglycerol:ATP kinase; ATP:1,2-diacylglycerol 3-phosphotransferase; diacylglycerol kinase (ATP dependent)
Systematic name: ATP:1,2-diacyl-sn-glycerol 3-phosphotransferase
Comments: Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Activity is stimulated by certain phospholipids [4,7]. In plants and animals the product 1,2-diacyl-sn-glycerol 3-phosphate is an important second messenger. cf. EC 2.7.1.174, diacylglycerol kinase (CTP).
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 60382-71-0
References:
1.  Hokin, L.E. and Hokin, M.R. Diglyceride kinase and other pathways for phosphatidic acid synthesis in the erythrocyte membrane. Biochim. Biophys. Acta 67 (1963) 470–484. [PMID: 13961253]
2.  Weissbach, H., Thomas, E. and Kaback, H.R. Studies on the metabolism of ATP by isolated bacterial membranes: formation and metabolism of membrane-bound phosphatidic acid. Arch. Biochem. Biophys. 147 (1971) 249–254. [DOI] [PMID: 4940043]
3.  Daleo, G.R., Piras, M.M. and Piras, R. Diglyceride kinase activity of microtubules. Characterization and comparison with the protein kinase and ATPase activities associated with vinblastine-isolated tubulin of chick embryonic muscles. Eur. J. Biochem. 68 (1976) 339–346. [DOI] [PMID: 185051]
4.  Walsh, J.P. and Bell, R.M. sn-1,2-Diacylglycerol kinase of Escherichia coli. Structural and kinetic analysis of the lipid cofactor dependence. J. Biol. Chem. 261 (1986) 15062–15069. [PMID: 3021764]
5.  Russ, E., Kaiser, U. and Sandermann, H., Jr. Lipid-dependent membrane enzymes. Purification to homogeneity and further characterization of diacylglycerol kinase from Escherichia coli. Eur. J. Biochem. 171 (1988) 335–342. [PMID: 2828054]
6.  Walsh, J.P. and Bell, R.M. Diacylglycerol kinase from Escherichia coli. Methods Enzymol. 209 (1992) 153–162. [DOI] [PMID: 1323028]
7.  Wissing, J.B. and Wagner, K.G. Diacylglycerol kinase from suspension cultured plant cells : characterization and subcellular localization. Plant Physiol. 98 (1992) 1148–1153. [PMID: 16668739]
[EC 2.7.1.107 created 1984, modified 2013]
 
 
EC 2.7.1.174     
Accepted name: diacylglycerol kinase (CTP)
Reaction: CTP + 1,2-diacyl-sn-glycerol = CDP + 1,2-diacyl-sn-glycerol 3-phosphate
Glossary: 1,2-diacyl-sn-glycerol 3-phosphate = phosphatidate
Other name(s): DAG kinase; CTP-dependent diacylglycerol kinase; diglyceride kinase (ambiguous); DGK1 (gene name); diacylglycerol kinase (CTP dependent)
Systematic name: CTP:1,2-diacyl-sn-glycerol 3-phosphotransferase
Comments: Requires Ca2+ or Mg2+ for activity. Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Unlike the diacylglycerol kinases from bacteria, plants, and animals [cf. EC 2.7.1.107, diacylglycerol kinase (ATP)], the enzyme from Saccharomyces cerevisiae utilizes CTP. The enzyme can also use dCTP, but not ATP, GTP or UTP.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc
References:
1.  Han, G.S., O'Hara, L., Carman, G.M. and Siniossoglou, S. An unconventional diacylglycerol kinase that regulates phospholipid synthesis and nuclear membrane growth. J. Biol. Chem. 283 (2008) 20433–20442. [DOI] [PMID: 18458075]
2.  Han, G.S., O'Hara, L., Siniossoglou, S. and Carman, G.M. Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase. J. Biol. Chem. 283 (2008) 20443–20453. [DOI] [PMID: 18458076]
3.  Fakas, S., Konstantinou, C. and Carman, G.M. DGK1-encoded diacylglycerol kinase activity is required for phospholipid synthesis during growth resumption from stationary phase in Saccharomyces cerevisiae. J. Biol. Chem. 286 (2011) 1464–1474. [DOI] [PMID: 21071438]
[EC 2.7.1.174 created 2012, modified 2013]
 
 
EC 2.7.7.41     
Accepted name: phosphatidate cytidylyltransferase
Reaction: CTP + phosphatidate = diphosphate + CDP-diacylglycerol
Other name(s): CDP diglyceride pyrophosphorylase; CDP-diacylglycerol synthase; CDP-diacylglyceride synthetase; cytidine diphosphoglyceride pyrophosphorylase; phosphatidate cytidyltransferase; phosphatidic acid cytidylyltransferase; CTP:1,2-diacylglycerophosphate-cytidyl transferase; CTP-diacylglycerol synthetase; DAG synthetase; CDP-DG
Systematic name: CTP:phosphatidate cytidylyltransferase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9067-83-8
References:
1.  Carter, J.R. and Kennedy, E.P. Enzymatic synthesis of cytidine diphosphate diglyceride. J. Lipid Res. 7 (1966) 678–683. [PMID: 4291255]
2.  McCaman, R.E. and Finnerty, W.R. Biosynthesis of cytidine diphosphate-diglyceride by a particulate fraction from Micrococcus cerificans. J. Biol. Chem. 243 (1968) 5074–5080. [PMID: 5679981]
3.  Petzold, G.L. and Agranoff, B.W. The biosynthesis of cytidine diphosphate diglyceride by embryonic chick brain. J. Biol. Chem. 242 (1967) 1187–1191. [PMID: 6067194]
[EC 2.7.7.41 created 1972]
 
 
EC 3.1.1.118     
Accepted name: phospholipid sn-1 acylhydrolase
Reaction: (1) a 1-phosphatidyl-1D-myo-inositol + H2O = a 2-acyl-sn-glycero-3-phospho-1D-myo-inositol + a fatty acid
(2) a 1,2-diacyl-sn-glycerol 3-phosphate + H2O = a 2-acyl-sn-glycerol 3-phosphate + a fatty acid
Glossary: a 1,2-diacyl-sn-glycerol 3-phosphate = a phosphatidate
Other name(s): phospholipase DDHD1; phosphatidic acid-preferring phospholipase A1; PA-PLA1; DDHD1 (gene name)
Systematic name: phospholipid sn-1 acylhydrolase
Comments: The human enzyme shows broad specificity, and has a preference for phosphatidate over other phospholipids. Unlike EC 3.1.1.32, phospholipase A1, it is also active against phosphatidylinositol. It is not active towards acyl groups linked at the sn-2 position.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc
References:
1.  Yamashita, A., Kumazawa, T., Koga, H., Suzuki, N., Oka, S. and 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 (2010) 711–720. [DOI] [PMID: 20359546]
2.  Baba, T., Kashiwagi, Y., Arimitsu, N., Kogure, T., Edo, A., Maruyama, T., Nakao, K., Nakanishi, H., Kinoshita, M., Frohman, M.A., Yamamoto, A. and Tani, K. Phosphatidic acid (PA)-preferring phospholipase A1 regulates mitochondrial dynamics. J. Biol. Chem. 289 (2014) 11497–11511. [DOI] [PMID: 24599962]
[EC 3.1.1.118 created 2021]
 
 
EC 3.1.3.4     
Accepted name: phosphatidate phosphatase
Reaction: a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
Glossary: a 1,2-diacylglycerol 3-phosphate = a 3-sn-phosphatidate
a 1,2-diacyl-sn-glycerol = diacylglycerol = DAG
Other name(s): phosphatic acid phosphatase; acid phosphatidyl phosphatase; phosphatic acid phosphohydrolase; PAP; Lipin
Systematic name: diacylglycerol-3-phosphate phosphohydrolase
Comments: This enzyme catalyses the Mg2+-dependent dephosphorylation of a 1,2-diacylglycerol-3-phosphate, yielding a 1,2-diacyl-sn-glycerol (DAG), the substrate for de novo lipid synthesis via the Kennedy pathway and for the synthesis of triacylglycerol. In lipid signalling, the enzyme generates a pool of DAG to be used for protein kinase C activation. The mammalian enzymes are known as lipins.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9025-77-8
References:
1.  Smith, S.W., Weiss, S.B. and Kennedy, E.P. The enzymatic dephosphorylation of phosphatidic acids. J. Biol. Chem. 228 (1957) 915–922. [PMID: 13475370]
2.  Carman, G.M. and Han, G.S. Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis. J. Biol. Chem. 284 (2009) 2593–2597. [DOI] [PMID: 18812320]
[EC 3.1.3.4 created 1961, modified 2010]
 
 
EC 3.1.3.81      
Transferred entry: diacylglycerol diphosphate phosphatase. Now EC 3.6.1.75, diacylglycerol diphosphate phosphatase
[EC 3.1.3.81 created 2010, deleted 2022]
 
 
EC 3.1.3.106     
Accepted name: 2-lysophosphatidate phosphatase
Reaction: a 1-acyl-sn-glycerol 3-phosphate + H2O = a 1-acyl-sn-glycerol + phosphate
Other name(s): 1-acyl-sn-glycerol 3-phosphatase; CPC3 (gene name); PHM8 (gene name)
Systematic name: 1-acyl-sn-glycerol 3-phosphate phosphohydrolase
Comments: The enzyme has been studied from the plants Arachis hypogaea (peanut) and Arabidopsis thaliana (thale cress) and from the yeast Saccharomyces cerevisiae. The enzyme from yeast, but not from the plants, requires Mg2+.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
References:
1.  Shekar, S., Tumaney, A.W., Rao, T.J. and Rajasekharan, R. Isolation of lysophosphatidic acid phosphatase from developing peanut cotyledons. Plant Physiol. 128 (2002) 988–996. [PMID: 11891254]
2.  Reddy, V.S., Singh, A.K. and Rajasekharan, R. The Saccharomyces cerevisiae PHM8 gene encodes a soluble magnesium-dependent lysophosphatidic acid phosphatase. J. Biol. Chem. 283 (2008) 8846–8854. [PMID: 18234677]
3.  Reddy, V.S., Rao, D.K. and Rajasekharan, R. Functional characterization of lysophosphatidic acid phosphatase from Arabidopsis thaliana. Biochim. Biophys. Acta 1801 (2010) 455–461. [PMID: 20045079]
[EC 3.1.3.106 created 2019]
 
 
EC 3.1.4.4     
Accepted name: phospholipase D
Reaction: a phosphatidylcholine + H2O = choline + a phosphatidate
Other name(s): lipophosphodiesterase II; lecithinase D; choline phosphatase
Systematic name: phosphatidylcholine phosphatidohydrolase
Comments: Also acts on other phosphatidyl esters.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9001-87-0
References:
1.  Astrachan, L. The bond hydrolyzed by cardiolipin-specific phospholipase D. Biochim. Biophys. Acta 296 (1973) 79–88. [DOI] [PMID: 4632675]
2.  Einset, E. and Clark, W.L. The enzymatically catalyzed release of choline from lecithin. J. Biol. Chem. 231 (1958) 703–715. [PMID: 13539005]
3.  Hanahan, D.J. and Chaikoff, I.L. On the nature of the phosphorus-containing lipides of cabbage leaves and their relation to a phospholipide-splitting enzyme contained in these leaves. J. Biol. Chem. 172 (1948) 191–198. [PMID: 18920784]
4.  Tookey, H.L. and Balls, A.K. Plant phospholipase D. I. Studies on cottonseed and cabbage phospholipase D. J. Biol. Chem. 218 (1956) 213–224. [PMID: 13278329]
[EC 3.1.4.4 created 1961]
 
 
EC 3.1.4.41     
Accepted name: sphingomyelin phosphodiesterase D
Reaction: sphingomyelin + H2O = ceramide phosphate + choline
Other name(s): sphingomyelinase D
Systematic name: sphingomyelin ceramide-phosphohydrolase
Comments: Does not act on phosphatidylcholine, but hydrolyses 2-lysophosphatidylcholine to choline and 2-lysophosphatidate.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 54992-31-3
References:
1.  Carne, H.R. and Onon, E. Action of Corynebacterium ovis exotoxin on endothelial cells of blood vessels. Nature 271 (1978) 246–248. [PMID: 622164]
2.  Soucek, A., Michalec, C. and Souckov, A. Identification and characterization of a new enzyme of the group phospholipase D isolated from Corynebacterium ovis. Biochim. Biophys. Acta 227 (1971) 116–128. [DOI] [PMID: 5543581]
[EC 3.1.4.41 created 1978]
 
 
EC 3.1.4.50     
Accepted name: glycosylphosphatidylinositol phospholipase D
Reaction: 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(α-D-glucosaminyl)-1D-myo-inositol + 3-sn-phosphatidate
For diagram of glycosylphosphatidyl-myo-inositol biosynthesis, click here
Other name(s): GPI-PLD; glycoprotein phospholipase D; phosphatidylinositol phospholipase D; phosphatidylinositol-specific phospholipase D
Systematic name: glycoprotein-phosphatidylinositol phosphatidohydrolase
Comments: This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure. It therefore cleaves proteins from the lipid part of the glycosylphosphatidylinositol (GPI) anchors, but does so by hydrolysis, whereas glycosylphosphatidylinositol diacylglycerol-lyase (EC 4.6.1.14) does so by elimination. It acts on plasma membranes only after solubilization of the substrate with detergents or solvents, but it may act on intracellular membranes.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 113756-14-2
References:
1.  Low, M.G. and Prasad, A.R.S. A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma. Proc. Natl. Acad. Sci. USA 85 (1988) 980–984. [DOI] [PMID: 3422494]
2.  Malik, A.-S. and Low, M.G. Conversion of human placental alkaline phosphatase from a high Mr form to a low Mr form during butanol extraction. An investigation of the role of endogenous phosphoinositide-specific phospholipases. Biochem. J. 240 (1986) 519–527. [PMID: 3028377]
3.  Li, J.Y., Hollfelder, K., Huang, K.S. and Low, M.G. Structural features of GPI-specific phospholipase D revealed by fragmentation and Ca2+ binding studies. J. Biol. Chem. 269 (1994) 28963–28971. [PMID: 7961859]
4.  Deeg, M.A, Vierman, E.L. and Cheung, M.C. GPI-specific phospholipase D associates with an apoA-I- and apoA-IV-containing complex. J. Lipid Res. 42 (2001) 442–451. [PMID: 11254757]
[EC 3.1.4.50 created 1990, modified 2002]
 
 
EC 3.1.4.54     
Accepted name: N-acetylphosphatidylethanolamine-hydrolysing phospholipase D
Reaction: N-acylphosphatidylethanolamine + H2O = N-acylethanolamine + a 1,2-diacylglycerol 3-phosphate
Other name(s): NAPE-PLD; anandamide-generating phospholipase D; N-acyl phosphatidylethanolamine phospholipase D; NAPE-hydrolyzing phospholipase D
Systematic name: N-acetylphosphatidylethanolamine phosphatidohydrolase
Comments: This enzyme is involved in the biosynthesis of anandamide. It does not hydrolyse phosphatidylcholine and phosphatidylethanolamine [1]. No transphosphatidation [1]. The enzyme contains Zn2+ and is activated by Mg2+ or Ca2+ [2].
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
References:
1.  Okamoto, Y., Morishita, J., Tsuboi, K., Tonai, T. and Ueda, N. Molecular characterization of a phospholipase D generating anandamide and its congeners. J. Biol. Chem. 279 (2004) 5298–5305. [DOI] [PMID: 14634025]
2.  Wang, J., Okamoto, Y., Morishita, J., Tsuboi, K., Miyatake, A. and Ueda, N. Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-β-lactamase family. J. Biol. Chem. 281 (2006) 12325–12335. [DOI] [PMID: 16527816]
[EC 3.1.4.54 created 2011]
 
 
EC 3.6.1.26     
Accepted name: CDP-diacylglycerol diphosphatase
Reaction: CDP-diacylglycerol + H2O = CMP + phosphatidate
Other name(s): cytidine diphosphodiacylglycerol pyrophosphatase; CDP diacylglycerol hydrolase
Systematic name: CDP-diacylglycerol phosphatidylhydrolase
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 62213-20-1
References:
1.  Raetz, C.R.H., Hirschberg, B., Dowhan, W., Wickner, W.T. and Kennedy, E.P. A membrane-bound pyrophosphatase in Escherichia coli catalyzing the hydrolysis of cytidine diphosphate-diglyceride. J. Biol. Chem. 247 (1972) 2245–2247. [PMID: 4335869]
[EC 3.6.1.26 created 1976]
 
 
EC 3.6.1.75     
Accepted name: diacylglycerol diphosphate phosphatase
Reaction: 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate
Other name(s): DGPP phosphatase; DGPP phosphohydrolase; DPP1; DPPL1; DPPL2; PAP2; pyrophosphate phosphatase
Systematic name: 1,2-diacyl-sn-glycerol 3-phosphate phosphohydrolase
Comments: The bifunctional enzyme catalyses the dephosphorylation of diacylglycerol diphosphate to phosphatidate and the subsequent dephosphorylation of phosphatidate to diacylglycerol (cf. phosphatidate phosphatase (EC 3.1.3.4)). It regulates intracellular levels of diacylglycerol diphosphate and phosphatidate, phospholipid molecules believed to play a signalling role in stress response [6]. The phosphatase activity of the bifunctional enzyme is Mg2+-independent and N-ethylmaleimide-insensitive and is distinct from the Mg2+-dependent and N-ethylmaleimide-sensitive enzyme EC 3.1.3.4 (phosphatidate phosphatase) [5].The diacylglycerol pyrophosphate phosphatase activity in Saccharomyces cerevisiae is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase [4].
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
References:
1.  Dillon, D.A., Wu, W.I., Riedel, B., Wissing, J.B., Dowhan, W. and Carman, G.M. The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity. J. Biol. Chem. 271 (1996) 30548–30553. [DOI] [PMID: 8940025]
2.  Dillon, D.A., Chen, X., Zeimetz, G.M., Wu, W.I., Waggoner, D.W., Dewald, J., Brindley, D.N. and Carman, G.M. Mammalian Mg2+-independent phosphatidate phosphatase (PAP2) displays diacylglycerol pyrophosphate phosphatase activity. J. Biol. Chem. 272 (1997) 10361–10366. [DOI] [PMID: 9099673]
3.  Wu, W.I., Liu, Y., Riedel, B., Wissing, J.B., Fischl, A.S. and Carman, G.M. Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae. J. Biol. Chem. 271 (1996) 1868–1876. [DOI] [PMID: 8567632]
4.  Oshiro, J., Han, G.S. and Carman, G.M. Diacylglycerol pyrophosphate phosphatase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1635 (2003) 1–9. [DOI] [PMID: 14642771]
5.  Carman, G.M. Phosphatidate phosphatases and diacylglycerol pyrophosphate phosphatases in Saccharomyces cerevisiae and Escherichia coli. Biochim. Biophys. Acta 1348 (1997) 45–55. [DOI] [PMID: 9370315]
6.  Han, G.S., Johnston, C.N., Chen, X., Athenstaedt, K., Daum, G. and Carman, G.M. Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc. J. Biol. Chem. 276 (2001) 10126–10133. [DOI] [PMID: 11139591]
[EC 3.6.1.75 created 2010 as EC 3.1.3.81, 2022 transferred to EC 3.6.1.75]
 
 


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