The Enzyme Database

Your query returned 29 entries.    printer_iconPrintable version

Accepted name: diacylglycerol O-acyltransferase
Reaction: acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol
Other name(s): diglyceride acyltransferase; 1,2-diacylglycerol acyltransferase; diacylglycerol acyltransferase; diglyceride O-acyltransferase; palmitoyl-CoA-sn-1,2-diacylglycerol acyltransferase; acyl-CoA:1,2-diacylglycerol O-acyltransferase
Systematic name: acyl-CoA:1,2-diacyl-sn-glycerol O-acyltransferase
Comments: Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-98-5
1.  Coleman, R. and Bell, R.M. Triacylglycerol synthesis in isolated fat cells. Studies on the microsomal diacylglycerol acyltransferase activity using ethanol-dispersed diacylglycerols. J. Biol. Chem. 251 (1976) 4537–4543. [PMID: 947894]
2.  Grigor, M.R. and Bell, R.M. Separate monoacylglycerol and diacylglycerol acyltransferases function in intestinal triacylglycerol synthesis. Biochim. Biophys. Acta 712 (1982) 464–472. [DOI] [PMID: 6289909]
3.  Kawasaki, T. and Snyder, F. Synthesis of a novel acetylated neutral lipid related to platelet-activating factor by acyl-CoA:1-O-alkyl-2-acetyl-sn-glycerol acyltransferase in HL-60 cells. J. Biol. Chem. 263 (1988) 2593–2596. [PMID: 3422635]
4.  Weiss, S.B., Kennedy, E.P. and Kiyasu, J.Y. The enzymatic synthesis of triglycerides. J. Biol. Chem. 235 (1960) 40–44. [PMID: 13843753]
[EC created 1965]
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, KEGG, MetaCyc, CAS registry number: 51901-16-7
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 created 1976, modified 1990]
Accepted name: 2-acylglycerol-3-phosphate O-acyltransferase
Reaction: acyl-CoA + 2-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Other name(s): 2-acylglycerophosphate acyltransferase
Systematic name: acyl-CoA:2-acyl-sn-glycerol 3-phosphate O-acyltransferase
Comments: Saturated acyl-CoA thioesters are the most effective acyl donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 51901-17-8
1.  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 created 1976]
Accepted name: diacylglycerol—sterol O-acyltransferase
Reaction: a 1,2-diacyl-sn-glycerol + sterol = a 1-acyl-sn-glycerol + sterol ester
Other name(s): 1,2-diacyl-sn-glycerol:sterol acyl transferase
Systematic name: 1,2-diacyl-sn-glycerol:sterol O-acyltransferase
Comments: Cholesterol, sitosterol, campesterol and diacylglycerol can act as acceptors. Transfers a number of long-chain fatty acyl groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 79586-23-5
1.  Bartlett, K., Keat, M.J. and Mercer, E.I. Biosynthesis of sterol esters in Phycomyces blakesleeanus. Phytochemistry 13 (1974) 1107–1113.
2.  Garcia, R.E. and Mudd, J.B. Metabolism of monoacylglycerol and diacylglycerol by enzyme preparations from spinach leaves. Arch. Biochem. Biophys. 191 (1978) 487–493. [DOI] [PMID: 742884]
3.  Garcia, R.E. and Mudd, J.B. 1,2-Diacyl-sn-glycerol:sterol acyl transferase from spinach leaves (Spinacia oleracea L.). Methods Enzymol. 71 (1981) 768–772.
[EC created 1984]
Accepted name: phospholipid:diacylglycerol acyltransferase
Reaction: phospholipid + 1,2-diacyl-sn-glycerol = lysophospholipid + triacylglycerol
Glossary: ricinoleic acid = (9Z,12R)-12-hydroxyoctadec-9-enoic acid
vernolic acid = (9Z,12S,13R)-12,13-epoxyoctadec-9-enoic acid
Other name(s): PDAT
Systematic name: phospholipid:1,2-diacyl-sn-glycerol O-acyltransferase
Comments: This enzyme differs from EC, diacylglycerol O-acyltransferase, by synthesising triacylglycerol using an acyl-CoA-independent mechanism. The specificity of the enzyme for the acyl group in the phospholipid varies with species, e.g., the enzyme from castor bean (Ricinus communis) preferentially incorporates vernoloyl (12,13-epoxyoctadec-9-enoyl) groups into triacylglycerol, whereas that from the hawk’s beard (Crepis palaestina) incorporates both ricinoleoyl (12-hydroxyoctadec-9-enoyl) and vernoloyl groups. The enzyme from the yeast Saccharomyces cerevisiae specifically transfers acyl groups from the sn-2 position of the phospholipid to diacylglycerol, thus forming an sn-1-lysophospholipid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 288587-47-3
1.  Dahlqvist, A., Stähl, U., Lenman, M., Banas, A., Lee, M., Sandager, L., Ronne, H. and Stymne, S. Phospholipid:diacylglycerol acyltransferase: An enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants. Proc. Natl. Acad. Sci. USA 97 (2000) 6487–6492. [DOI] [PMID: 10829075]
[EC created 2001]
Accepted name: monogalactosyldiacylglycerol synthase
Reaction: UDP-α-D-galactose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol
For diagram of galactosyl diacylglycerol, click here
Other name(s): uridine diphosphogalactose-1,2-diacylglycerol galactosyltransferase; UDP-galactose:diacylglycerol galactosyltransferase; MGDG synthase; UDP galactose-1,2-diacylglycerol galactosyltransferase; UDP-galactose-diacylglyceride galactosyltransferase; UDP-galactose:1,2-diacylglycerol 3-β-D-galactosyltransferase; 1β-MGDG; 1,2-diacylglycerol 3-β-galactosyltransferase; UDP-galactose:1,2-diacyl-sn-glycerol 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:1,2-diacyl-sn-glycerol 3-β-D-galactosyltransferase
Comments: This enzyme adds only one galactosyl group to the diacylglycerol; EC, digalactosyldiacylglycerol synthase, adds a galactosyl group to the product of the above reaction. There are three isoforms in Arabidopsis that can be divided into two types, A-type (MGD1) and B-type (MGD2 and MGD3). MGD1 is the isoform responsible for the bulk of monogalactosyldiacylglycerol (MGDG) synthesis in Arabidopsis [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-55-7
1.  Veerkamp, J.H. Biochemical changes in Bifidobacterium bifidum var. pennsylvanicus after cell-wall inhibition. VI. Biosynthesis of the galactosyldiglycerides. Biochim. Biophys. Acta 348 (1974) 23–34. [DOI] [PMID: 4838219]
2.  Wenger, D.A., Petipas, J.W. and Pieringer, R.A. The metabolism of glyceride glycolipids. II. Biosynthesis of monogalactosyl diglyceride from uridine diphosphate galactose and diglyceride in brain. Biochemistry 7 (1968) 3700–3707. [PMID: 5681471]
3.  Miège, C., Maréchal, E., Shimojima, M., Awai, K., Block, M.A., Ohta, H., Takamiya, K., Douce, R. and Joyard, J. Biochemical and topological properties of type A MGDG synthase, a spinach chloroplast envelope enzyme catalyzing the synthesis of both prokaryotic and eukaryotic MGDG. Eur. J. Biochem. 265 (1999) 990–1001. [DOI] [PMID: 10518794]
4.  Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397–2400. [DOI] [PMID: 15590685]
[EC created 1972, modified 2003, modified 2005]
Transferred entry: 1,2-diacylglycerol 3-glucosyltransferase. Now classified as EC, monoglucosyldiacylglycerol synthase, and EC, 1,2-diacylglycerol 3-α-glucosyltransferase
[EC created 1986, deleted 2015]
Accepted name: galactolipid galactosyltransferase
Reaction: 2 a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = a 1,2-diacyl-3-O-[β-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol + a 1,2-diacyl-sn-glycerol
For diagram of galactosyl diacylglycerol, click here
Glossary: a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = monogalactosyldiacylglycerol
Other name(s): galactolipid-galactolipid galactosyltransferase; galactolipid:galactolipid galactosyltransferase; interlipid galactosyltransferase; GGGT; DGDG synthase (ambiguous); digalactosyldiacylglycerol synthase (ambiguous); 3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol:mono-3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol β-D-galactosyltransferase; 3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol:3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol β-D-galactosyltransferase; SFR2 (gene name)
Systematic name: 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol:1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol β-D-galactosyltransferase
Comments: The enzyme converts monogalactosyldiacylglycerol to digalactosyldiacylglycerol, trigalactosyldiacylglycerol and tetragalactosyldiacylglycerol. All residues are connected by β linkages. The activity is localized to chloroplast envelope membranes, but it does not contribute to net galactolipid synthesis in plants, which is performed by EC, monogalactosyldiacylglycerol synthase, and EC, digalactosyldiacylglycerol synthase. Note that the β,β-digalactosyldiacylglycerol formed by this enzyme is different from the more common α,β-digalactosyldiacylglycerol formed by EC The enzyme provides an important mechanism for the stabilization of the chloroplast membranes during freezing and drought stress.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 66676-74-2
1.  Dorne, A.-J., Block, M.A., Joyard, J. and Douce, R. The galactolipid-galactolipid galactosyltransferase is located on the outer surface of the outer-membrane of the chloroplast envelope. FEBS Lett. 145 (1982) 30–34.
2.  Heemskerk, J.W.M., Wintermans, J.F.G.M., Joyard, J., Block, M.A., Dorne, A.-J. and Douce, R. Localization of galactolipid:galactolipid galactosyltransferase and acyltransferase in outer envelope membrane of spinach chloroplasts. Biochim. Biophys. Acta 877 (1986) 281–289.
3.  Heemskerk, J.W.M., Jacobs, F.H.H. and Wintermans, J.F.G.M. UDPgalactose-independent synthesis of monogalactosyldiacylglycerol. An enzymatic activity of the spinach chloroplast envelope. Biochim. Biophys. Acta 961 (1988) 38–47. [DOI]
4.  Kelly, A.A., Froehlich, J.E. and Dörmann, P. Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell 15 (2003) 2694–2706. [DOI] [PMID: 14600212]
5.  Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397–2400. [DOI] [PMID: 15590685]
6.  Fourrier, N., Bedard, J., Lopez-Juez, E., Barbrook, A., Bowyer, J., Jarvis, P., Warren, G. and Thorlby, G. A role for SENSITIVE TO FREEZING2 in protecting chloroplasts against freeze-induced damage in Arabidopsis. Plant J. 55 (2008) 734–745. [DOI] [PMID: 18466306]
7.  Moellering, E.R., Muthan, B. and Benning, C. Freezing tolerance in plants requires lipid remodeling at the outer chloroplast membrane. Science 330 (2010) 226–228. [DOI] [PMID: 20798281]
[EC created 1990, modified 2005, modified 2015]
Accepted name: digalactosyldiacylglycerol synthase
Reaction: UDP-α-D-galactose + 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = UDP + 1,2-diacyl-3-O-[α-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol
For diagram of galactosyl diacylglycerol, click here
Other name(s): DGD1; DGD2; DGDG synthase (ambiguous); UDP-galactose-dependent DGDG synthase; UDP-galactose-dependent digalactosyldiacylglycerol synthase; UDP-galactose:MGDG galactosyltransferase; UDP-galactose:3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol 6-α-galactosyltransferase
Systematic name: UDP-α-D-galactose:1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol 6-α-galactosyltransferase
Comments: Requires Mg2+. Diacylglycerol cannot serve as an acceptor molecule for galactosylation as in the reaction catalysed by EC, monogalactosyldiacylglyerol synthase. When phosphate is limiting, phospholipids in plant membranes are reduced but these are replaced, at least in part, by the glycolipids digalactosyldiacylglycerol (DGDG) and sulfoquinovosyldiacylglycerol [3]. While both DGD1 and DGD2 are increased under phosphate-limiting conditions, DGD2 does not contribute significantly under optimal growth conditions. DGD2 is responsible for the synthesis of DGDG molecular species that are rich in C16 fatty acids at sn-1 of diacylglycerol whereas DGD1 leads to molecular species rich in C18 fatty acids [3]. The enzyme has been localized to the outer side of chloroplast envelope membranes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 69913-00-4
1.  Kelly, A.A. and Dörmann, P. DGD2, an Arabidopsis gene encoding a UDP-galactose-dependent digalactosyldiacylglycerol synthase is expressed during growth under phosphate-limiting conditions. J. Biol. Chem. 277 (2002) 1166–1173. [DOI] [PMID: 11696551]
2.  Härtel, H., Dörmann, P. and Benning, C. DGD1-independent biosynthesis of extraplastidic galactolipids after phosphate deprivation in Arabidopsis. Proc. Natl. Acad. Sci. USA 97 (2000) 10649–10654. [DOI] [PMID: 10973486]
3.  Kelly, A.A., Froehlich, J.E. and Dörmann, P. Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell 15 (2003) 2694–2706. [DOI] [PMID: 14600212]
4.  Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397–2400. [DOI] [PMID: 15590685]
[EC created 2005]
Accepted name: monoglucosyldiacylglycerol synthase
Reaction: UDP-α-D-glucose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol
Glossary: a 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol = a β-monoglucosyldiacylglycerol = a GlcDG
Other name(s): mgdA (gene name)
Systematic name: UDP-α-D-glucose:1,2-diacyl-sn-glycerol 3-β-D-glucosyltransferase
Comments: The enzymes from cyanobacteria are involved in the biosynthesis of galactolipids found in their photosynthetic membranes. The enzyme belongs to the GT2 family of configuration-inverting glycosyltranferases [2]. cf. EC, 1,2-diacylglycerol 3-α-glucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Sato, N. and Murata, N. Lipid biosynthesis in the blue-green-alga (cyanobacterium), Anabaena variabilis. 3. UDP-glucose-diacylglycerol glucosyltransferase activity in vitro. Plant Cell Physiol. 23 (1982) 1115–1120.
2.  Awai, K., Kakimoto, T., Awai, C., Kaneko, T., Nakamura, Y., Takamiya, K., Wada, H. and Ohta, H. Comparative genomic analysis revealed a gene for monoglucosyldiacylglycerol synthase, an enzyme for photosynthetic membrane lipid synthesis in cyanobacteria. Plant Physiol. 141 (2006) 1120–1127. [DOI] [PMID: 16714404]
3.  Yuzawa, Y., Shimojima, M., Sato, R., Mizusawa, N., Ikeda, K., Suzuki, M., Iwai, M., Hori, K., Wada, H., Masuda, S. and Ohta, H. Cyanobacterial monogalactosyldiacylglycerol-synthesis pathway is involved in normal unsaturation of galactolipids and low-temperature adaptation of Synechocystis sp. PCC 6803. Biochim. Biophys. Acta 1841 (2014) 475–483. [DOI] [PMID: 24370445]
[EC created 2015]
Accepted name: 1,2-diacylglycerol 3-α-glucosyltransferase
Reaction: UDP-α-D-glucose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol
Other name(s): mgs (gene name); UDP-glucose:diacylglycerol glucosyltransferase; UDP-glucose:1,2-diacylglycerol glucosyltransferase; uridine diphosphoglucose-diacylglycerol glucosyltransferase; UDP-glucose-diacylglycerol glucosyltransferase; UDP-glucose:1,2-diacylglycerol 3-D-glucosyltransferase; UDP-glucose:1,2-diacyl-sn-glycerol 3-D-glucosyltransferase; 1,2-diacylglycerol 3-glucosyltransferase (ambiguous)
Systematic name: UDP-α-D-glucose:1,2-diacyl-sn-glycerol 3-α-D-glucosyltransferase
Comments: The enzyme from the bacterium Acholeplasma laidlawii, which lacks a cell wall, produces the major non-bilayer lipid in the organism. The enzyme from the bacterium Agrobacterium tumefaciens acts under phosphate deprivation, generating glycolipids as surrogates for phospholipids. The enzyme belongs to the GT4 family of configuration-retaining glycosyltransferases. Many diacylglycerols with long-chain acyl groups can act as acceptors. cf. EC, monoglucosyldiacylglycerol synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Karlsson, O.P., Dahlqvist, A., Vikstrom, S. and Wieslander, A. Lipid dependence and basic kinetics of the purified 1,2-diacylglycerol 3-glucosyltransferase from membranes of Acholeplasma laidlawii. J. Biol. Chem. 272 (1997) 929–936. [DOI] [PMID: 8995384]
2.  Li, L., Storm, P., Karlsson, O.P., Berg, S. and Wieslander, A. Irreversible binding and activity control of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii at an anionic lipid bilayer surface. Biochemistry 42 (2003) 9677–9686. [DOI] [PMID: 12911309]
3.  Berg, S., Edman, M., Li, L., Wikstrom, M. and Wieslander, A. Sequence properties of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii membranes. Recognition of a large group of lipid glycosyltransferases in eubacteria and archaea. J. Biol. Chem. 276 (2001) 22056–22063. [DOI] [PMID: 11294844]
4.  Semeniuk, A., Sohlenkamp, C., Duda, K. and Holzl, G. A bifunctional glycosyltransferase from Agrobacterium tumefaciens synthesizes monoglucosyl and glucuronosyl diacylglycerol under phosphate deprivation. J. Biol. Chem. 289 (2014) 10104–10114. [DOI] [PMID: 24558041]
[EC created 2015]
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, diacylglycerol kinase (CTP).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60382-71-0
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 created 1984, modified 2013]
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, 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, KEGG, MetaCyc
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 created 2012, modified 2013]
Accepted name: inositol phosphorylceramide synthase
Reaction: 1-phosphatidyl-1D-myo-inositol + a very-long-chain (2′R)-2′-hydroxy-phytoceramide = 1,2-diacyl-sn-glycerol + a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine
Glossary: a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine = a very-long-chain inositol phospho-α hydroxyphytoceramide = IPC
Other name(s): AUR1 (gene name); KEI1 (gene name)
Systematic name: 1-phosphatidyl-1D-myo-inositol:a very-long-chain (2′R)-2′-hydroxy-phytoceramide phosphoinositoltransferase
Comments: The enzyme, characterized from yeast, attaches a phosphoinositol headgroup to α-hydroxyphytoceramides, generating a very-long-chain inositol phospho-α hydroxyphytoceramide (IPC), the simplest of the three complex sphingolipids produced by yeast.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Nagiec, M.M., Nagiec, E.E., Baltisberger, J.A., Wells, G.B., Lester, R.L. and Dickson, R.C. Sphingolipid synthesis as a target for antifungal drugs. Complementation of the inositol phosphorylceramide synthase defect in a mutant strain of Saccharomyces cerevisiae by the AUR1 gene. J. Biol. Chem. 272 (1997) 9809–9817. [PMID: 9092515]
2.  Levine, T.P., Wiggins, C.A. and Munro, S. Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae. Mol. Biol. Cell 11 (2000) 2267–2281. [PMID: 10888667]
3.  Sato, K., Noda, Y. and Yoda, K. Kei1: a novel subunit of inositolphosphorylceramide synthase, essential for its enzyme activity and Golgi localization. Mol. Biol. Cell 20 (2009) 4444–4457. [PMID: 19726565]
[EC created 2019]
Accepted name: mannosyl-inositol-phosphoceramide inositolphosphotransferase
Reaction: 1-phosphatidyl-1D-myo-inositol + a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-{[6-O-(α-D-mannosyl)-1D-myo-inositol-1-O-yl]hydroxyphosphoryl}sphinganine = 1,2-diacyl-sn-glycerol + a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(6-O-{6-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]-α-D-mannosyl}-1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine
Glossary: a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-{[6-O-(α-D-mannosyl)-1D-myo-inositol-1-O-yl]hydroxyphosphoryl}sphinganine = a very-long-chain mannosylinositol phospho-α-hydroxyphytoceramide = MIPC
a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(6-O-{6-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]-α-D-mannosyl}-1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine = a very-long-chain mannosyl-diphosphoinositol-α-hydroxyphytoceramide = MIP2C
Other name(s): IPT1 (gene name)
Systematic name: 1-phosphatidyl-1D-myo-inositol:(4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-{[6-O-(α-D-mannosyl)-1D-myo-inositol-1-O-yl]hydroxyphosphoryl}sphinganine phosphoinositoltransferase
Comments: This enzyme catalyses the ultimate reaction in the yeast sphingolipid biosynthesis pathway. It transfers a second phosphoinositol group to mannosyl-inositol-phospho-α-hydroxyphytoceramide (MIPC), forming the final and most abundant yeast sphingolipid, mannosyl-diphosphoinositol-ceramide (MIP2C).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Dickson, R.C., Nagiec, E.E., Wells, G.B., Nagiec, M.M. and Lester, R.L. Synthesis of mannose-(inositol-P)2-ceramide, the major sphingolipid in Saccharomyces cerevisiae, requires the IPT1 (YDR072c) gene. J. Biol. Chem. 272 (1997) 29620–29625. [DOI] [PMID: 9368028]
[EC created 2019]
Accepted name: ethanolaminephosphotransferase
Reaction: CDP-ethanolamine + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylethanolamine
Other name(s): EPT; diacylglycerol ethanolaminephosphotransferase; CDPethanolamine diglyceride phosphotransferase; phosphorylethanolamine-glyceride transferase; CDP-ethanolamine:1,2-diacylglycerol ethanolaminephosphotransferase
Systematic name: CDP-ethanolamine:1,2-diacyl-sn-glycerol ethanolaminephosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-19-1
1.  Kennedy, E.P. and Weiss, S.B. The function of cytidine coenzymes in the biosynthesis of phospholipides. J. Biol. Chem. 222 (1956) 193–214. [PMID: 13366993]
[EC created 1961]
Accepted name: diacylglycerol cholinephosphotransferase
Reaction: CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine
Other name(s): phosphorylcholine-glyceride transferase; alkylacylglycerol cholinephosphotransferase; 1-alkyl-2-acetylglycerol cholinephosphotransferase; cholinephosphotransferase; CPT (ambiguous); alkylacylglycerol choline phosphotransferase; diacylglycerol choline phosphotransferase; 1-alkyl-2-acetyl-m-glycerol:CDPcholine choline phosphotransferase; CDP-choline diglyceride phosphotransferase; cytidine diphosphocholine glyceride transferase; cytidine diphosphorylcholine diglyceride transferase; phosphocholine diacylglyceroltransferase; sn-1,2-diacylglycerol cholinephosphotransferase; 1-alkyl-2-acetyl-sn-glycerol cholinephosphotransferase; CDP choline:1,2-diacylglycerol cholinephosphotransferase; CDP-choline:1,2-diacylglycerol cholinephosphotransferase
Systematic name: CDP-choline:1,2-diacyl-sn-glycerol cholinephosphotransferase
Comments: 1-Alkyl-2-acylglycerol can act as acceptor; this activity was previously listed separately.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-13-5
1.  Coleman, R. and Bell, R.M. Phospholipid synthesis in isolated fat cells. Studies of microsomal diacylglycerol cholinephosphotransferase and diacylglycerol ethanolaminephosphotransferase activities. J. Biol. Chem. 252 (1977) 3050–3056. [PMID: 192727]
2.  Lee, T.-C., Blank, M.L., Fitzgerald, V. and Snyder, F. Formation of alkylacyl- and diacylglycerophosphocholines via diradylglycerol cholinephosphotransferase in rat liver. Biochim. Biophys. Acta 713 (1982) 479–483. [DOI] [PMID: 6295501]
3.  Parsasarathy, S., Cady, R.K., Kraushaar, D.S., Sladek, N.E. and Baumann, W.J. Inhibition of diacylglycerol:CDPcholine cholinephosphotransferase activity by dimethylaminoethyl p-chlorophenoxyacetate. Lipids 13 (1978) 161–164. [DOI] [PMID: 204847]
4.  Renooij, W. and Snyder, F. Biosynthesis of 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet activating factor and a hypotensive lipid) by cholinephosphotransferase in various rat tissues. Biochim. Biophys. Acta 663 (1981) 545–556. [DOI] [PMID: 6260215]
[EC created 1961, modified 1986 (EC created 1983, incorporated 1986)]
Accepted name: CDP-diacylglycerol—glycerol-3-phosphate 1-phosphatidyltransferase
Reaction: CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 1-(3-sn-phosphatidyl)-sn-glycerol 3-phosphate
Other name(s): glycerophosphate phosphatidyltransferase; 3-phosphatidyl-1′-glycerol-3′-phosphate synthase; CDPdiacylglycerol:glycerol-3-phosphate phosphatidyltransferase; cytidine 5′-diphospho-1,2-diacyl-sn-glycerol (CDP-diglyceride):sn-glycerol-3-phosphate phosphatidyltransferase; phosphatidylglycerophosphate synthase; phosphatidylglycerolphosphate synthase; PGP synthase; CDP-diacylglycerol-sn-glycerol-3-phosphate 3-phosphatidyltransferase; CDP-diacylglycerol:sn-glycero-3-phosphate phosphatidyltransferase; glycerol phosphate phosphatidyltransferase; glycerol 3-phosphate phosphatidyltransferase; phosphatidylglycerol phosphate synthase; phosphatidylglycerol phosphate synthetase; phosphatidylglycerophosphate synthetase; sn-glycerol-3-phosphate phosphatidyltransferase
Systematic name: CDP-diacylglycerol:sn-glycerol-3-phosphate 1-(3-sn-phosphatidyl)transferase
Comments: The enzyme catalyses the committed step in the biosynthesis of acidic phospholipids known by the common names phophatidylglycerols and cardiolipins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9068-49-9
1.  Hirabayashi, T. Larson, T.J. and Dowhan, W. Membrane-associated phosphatidylglycerophosphate synthetase from Escherichia coli: Purification by substrate affinity chromatography on cytidine 5′-diphospho-1,2-diacyl-sn-glycerol sepharose. Biochemistry 15 (1976) 5205–5211. [PMID: 793612]
2.  Bleasdale, J.E. and Johnston, J.M. CMP-dependent incorporation of [14C]glycerol 3-phosphate into phosphatidylglycerol and phosphatidylglycerol phosphate by rabbit lung microsomes. Biochim. Biophys. Acta 710 (1982) 377–390. [DOI] [PMID: 7074121]
3.  Dowhan, W. Phosphatidylglycerophosphate synthase from Escherichia coli. Methods Enzymol. 209 (1992) 313–321. [DOI] [PMID: 1323047]
4.  Kawasaki, K., Kuge, O., Chang, S.C., Heacock, P.N., Rho, M., Suzuki, K., Nishijima, M. and Dowhan, W. Isolation of a chinese hamster ovary (CHO) cDNA encoding phosphatidylglycerophosphate (PGP) synthase, expression of which corrects the mitochondrial abnormalities of a PGP synthase-defective mutant of CHO-K1 cells. J. Biol. Chem. 274 (1999) 1828–1834. [DOI] [PMID: 9880566]
5.  Muller, F. and Frentzen, M. Phosphatidylglycerophosphate synthases from Arabidopsis thaliana. FEBS Lett. 509 (2001) 298–302. [DOI] [PMID: 11741606]
6.  Babiychuk, E., Muller, F., Eubel, H., Braun, H.P., Frentzen, M. and Kushnir, S. Arabidopsis phosphatidylglycerophosphate synthase 1 is essential for chloroplast differentiation, but is dispensable for mitochondrial function. Plant J. 33 (2003) 899–909. [DOI] [PMID: 12609031]
[EC created 1972, modified 1976, modified 2016]
Accepted name: CDP-diacylglycerol—serine O-phosphatidyltransferase
Reaction: CDP-diacylglycerol + L-serine = CMP + (3-sn-phosphatidyl)-L-serine
Other name(s): phosphatidylserine synthase; CDPdiglyceride-serine O-phosphatidyltransferase; PS synthase; cytidine 5′-diphospho-1,2-diacyl-sn-glycerol (CDPdiglyceride):L-serine O-phosphatidyltransferase; phosphatidylserine synthetase; CDP-diacylglycerol-L-serine O-phosphatidyltransferase; cytidine diphosphoglyceride-serine O-phosphatidyltransferase; CDP-diglyceride-L-serine phosphatidyltransferase; CDP-diglyceride:serine phosphatidyltransferase; cytidine 5′-diphospho-1,2-diacyl-sn-glycerol:L-serine O-phosphatidyltransferase; CDP-diacylglycerol:L-serine 3-O-phosphatidyltransferase
Systematic name: CDP-diacylglycerol:L-serine 3-sn-phosphatidyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9068-48-8
1.  Larson, T.J. and Dowhan, W. Ribosomal-associated phosphatidylserine synthetase from Escherichia coli: purification by substrate-specific elution from phosphocellulose using cytidine 5′-diphospho-1,2-diacyl-sn-glycerol. Biochemistry 15 (1976) 5212–5218. [PMID: 187212]
2.  Raetz, C.R.H. and Kennedy, E.P. Partial purification and properties of phosphatidylserine synthetase from Escherichia coli. J. Biol. Chem. 249 (1974) 5038–5045. [PMID: 4604873]
[EC created 1972, modified 1976]
Accepted name: CDP-diacylglycerol—inositol 3-phosphatidyltransferase
Reaction: CDP-diacylglycerol + myo-inositol = CMP + 1-phosphatidyl-1D-myo-inositol
For diagram of 1-phosphatidyl-myo-inositol metabolism, click here
Glossary: 1-phosphatidyl-1D-myo-inositol = PtdIns
Other name(s): CDP-diglyceride-inositol phosphatidyltransferase; phosphatidylinositol synthase; CDP-diacylglycerol-inositol phosphatidyltransferase; CDP-diglyceride:inositol transferase; cytidine 5′-diphospho-1,2-diacyl-sn-glycerol:myo-inositol 3-phosphatidyltransferase; CDP-DG:inositol transferase; cytidine diphosphodiglyceride-inositol phosphatidyltransferase; CDP-diacylglycerol:myo-inositol-3-phosphatidyltransferase; CDP-diglyceride-inositol transferase; cytidine diphosphoglyceride-inositol phosphatidyltransferase; cytidine diphosphoglyceride-inositol transferase
Systematic name: CDP-diacylglycerol:myo-inositol 3-phosphatidyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9027-01-4
1.  Bleasdale, J.E., Wallis, P., MacDonald, P.C. and Johnston, J.M. Characterization of the forward and reverse reactions catalyzed by CDP-diacylglycerol:inositol transferase in rabbit lung tissue. Biochim. Biophys. Acta 575 (1979) 135–147. [DOI] [PMID: 41587]
2.  Prottey, C. and Hawthorne, J.N. The biosynthesis of phosphatidic acid and phosphatidylinositol in mammalian pancreas. Biochem. J. 105 (1967) 379–392. [PMID: 4293959]
3.  Salway, J.G., Harewood, J.L., Kai, M., White, G.L. and Hawthorne, J.N. Enzymes of phosphoinositide metabolism during rat brain development. J. Neurochem. 15 (1968) 221–226. [DOI] [PMID: 4295616]
4.  Takenawa, T. and Egawa, K. CDP-diglyceride:inositol transferase from rat liver. Purification and properties. J. Biol. Chem. 252 (1977) 5419–5423. [PMID: 18462]
[EC created 1972, modified 1976]
Accepted name: phosphatidylglycerol—membrane-oligosaccharide glycerophosphotransferase
Reaction: phosphatidylglycerol + membrane-derived-oligosaccharide D-glucose = 1,2-diacyl-sn-glycerol + membrane-derived-oligosaccharide 6-(glycerophospho)-D-glucose
Other name(s): phosphoglycerol transferase; oligosaccharide glycerophosphotransferase; phosphoglycerol transferase I
Systematic name: phosphatidylglycerol:membrane-derived-oligosaccharide-D-glucose glycerophosphotransferase
Comments: 1,2-β- and 1,6-β-linked glucose residues in membrane polysaccharides and in synthetic glucosides can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 80146-86-7
1.  Jackson, B.J. and Kennedy, E.P. The biosynthesis of membrane-derived oligosaccharides. A membrane-bound phosphoglycerol transferase. J. Biol. Chem. 258 (1983) 2394–2398. [PMID: 6296144]
[EC created 1986]
Accepted name: sphingomyelin synthase
Reaction: a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol
For diagram of reaction, click here
Glossary: sphingomyelin = a ceramide-1-phosphocholine
ceramide = an N-acylsphingoid. The fatty acids of naturally occurring ceramides range in chain length from about C16 to about C26 and may contain one or more double bonds and/or hydroxy substituents at C-2
sphingoid = sphinganine, i.e. D-erythro-2-aminooctadecane-1,3-diol, and its homologues and stereoisomers (see also Lip-1.4)
Other name(s): SM synthase; SMS1; SMS2
Systematic name: ceramide:phosphatidylcholine cholinephosphotransferase
Comments: The reaction can occur in both directions [3]. This enzyme occupies a central position in sphingolipid and glycerophospholipid metabolism [4]. Up- and down-regulation of its activity has been linked to mitogenic and pro-apoptotic signalling in a variety of mammalian cell types [4]. Unlike EC, ceramide cholinephosphotransferase, CDP-choline cannot replace phosphatidylcholine as the donor of the phosphocholine moiety of sphingomyelin [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 58703-97-2
1.  Ullman, M.D. and Radin, N.S. The enzymatic formation of sphingomyelin from ceramide and lecithin in mouse liver. J. Biol. Chem. 249 (1974) 1506–1512. [PMID: 4817756]
2.  Voelker, D.R. and Kennedy, E.P. Cellular and enzymic synthesis of sphingomyelin. Biochemistry 21 (1982) 2753–2759. [PMID: 7093220]
3.  Huitema, K., van den Dikkenberg, J., Brouwers, J.F. and Holthuis, J.C. Identification of a family of animal sphingomyelin synthases. EMBO J. 23 (2004) 33–44. [DOI] [PMID: 14685263]
4.  Tafesse, F.G., Ternes, P. and Holthuis, J.C. The multigenic sphingomyelin synthase family. J. Biol. Chem. 281 (2006) 29421–29425. [DOI] [PMID: 16905542]
5.  Yamaoka, S., Miyaji, M., Kitano, T., Umehara, H. and Okazaki, T. Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells. J. Biol. Chem. 279 (2004) 18688–18693. [DOI] [PMID: 14976195]
[EC created 2006]
Accepted name: sn-1-specific diacylglycerol lipase
Reaction: a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty acid
Other name(s): DAGLA (gene name); DAGLB (gene name)
Systematic name: diacylglycerol sn-1-acylhydrolase
Comments: The enzyme, present in animals, is specific for the sn-1 position. When acting on 1-acyl-2-arachidonoyl-sn-glycerol, the enzyme forms 2-arachidonoylglycerol, the most abundant endocannabinoid in the mammalian brain.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Chau, L.Y. and Tau, H.H. Release of arachidonate from diglyceride in human platelets requires the sequential action of a diglyceride lipase and a monoglyceride lipase. Biochem. Biophys. Res. Commun. 100 (1988) 1688–1695. [DOI] [PMID: 7295321]
2.  Bisogno, T., Howell, F., Williams, G., Minassi, A., Cascio, M.G., Ligresti, A., Matias, I., Schiano-Moriello, A., Paul, P., Williams, E.J., Gangadharan, U., Hobbs, C., Di Marzo, V. and Doherty, P. Cloning of the first sn1-DAG lipases points to the spatial and temporal regulation of endocannabinoid signaling in the brain. J. Cell Biol. 163 (2003) 463–468. [DOI] [PMID: 14610053]
3.  Bisogno, T. Assay of DAGLα/β activity. Methods Mol. Biol. 1412 (2016) 149–156. [DOI] [PMID: 27245901]
[EC created 2021]
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, 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, KEGG, MetaCyc
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 created 2021]
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, KEGG, MetaCyc, CAS registry number: 9025-77-8
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 created 1961, modified 2010]
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 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 (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, KEGG, MetaCyc
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 created 2010]
Accepted name: phospholipase C
Reaction: a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
Other name(s): lipophosphodiesterase I; lecithinase C; Clostridium welchii α-toxin; Clostridium oedematiens β- and γ-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; α-toxin
Systematic name: phosphatidylcholine cholinephosphohydrolase
Comments: The bacterial enzyme, which is a zinc protein, also acts on sphingomyelin and phosphatidylinositol; that from seminal plasma does not act on phosphatidylinositol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-86-9
1.  Druzhinina, K.V. and Kritzman, M.G. [Lecithinase from animal tissues.] Biokhimiya 17 (1952) 77–81. [PMID: 13066482] (in Russian)
2.  Little, C. and Otnass, A.-B. The metal ion dependence of phospholipase C from Bacillus cereus. Biochim. Biophys. Acta 391 (1975) 326–333. [DOI] [PMID: 807246]
3.  Sheiknejad, R.G. and Srivastava, P.N. Isolation and properties of a phosphatidylcholine-specific phospholipase C from bull seminal plasma. J. Biol. Chem. 261 (1986) 7544–7549. [PMID: 3086312]
4.  Takahashi, T., Sugahara, T. and Ohsaka, A. Purification of Clostridium perfringens phospholipase C (α-toxin) by affinity chromatography on agarose-linked egg-yolk lipoprotein. Biochim. Biophys. Acta 351 (1974) 155–171. [DOI] [PMID: 4365891]
[EC created 1961]
Accepted name: phosphatidylinositol diacylglycerol-lyase
Reaction: 1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
For diagram of 1-phosphatidyl-myo-inositol metabolism, click here
Other name(s): monophosphatidylinositol phosphodiesterase; phosphatidylinositol phospholipase C; 1-phosphatidylinositol phosphodiesterase; 1-phosphatidyl-D-myo-inositol inositolphosphohydrolase (cyclic-phosphate-forming); 1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming)
Systematic name: 1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase (1D-myo-inositol-1,2-cyclic-phosphate-forming)
Comments: This enzyme is bacterial. Activity is also found in animals, but this activity is due to the presence of EC, phosphoinositide phospholipase C.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-19-0
1.  Allan, D. and Michell, R.H. Phosphatidylinositol cleavage catalysed by the soluble fraction from lymphocytes. Activity at pH5.5 and pH7.0. Biochem. J. 142 (1974) 591–597. [PMID: 4377210]
2.  Friedel, R.O., Brown, J.D. and Durell, J. Monophosphatidyl inositol inositolphosphohydrolase in guinea-pig brain. Biochim. Biophys. Acta 144 (1967) 684–686. [DOI] [PMID: 4294905]
3.  Irvine, R.F. The enzymology of stimulated inositol lipid turnover. Cell Calcium 3 (1982) 295–309. [DOI] [PMID: 6297738]
4.  Michell, R.H. and Allan, D. Inositol cyclic phosphate as a product of phosphatidylinositol breakdown by phospholipase C (Bacillus cereus). FEBS Lett. 53 (1975) 302–304. [DOI] [PMID: 236918]
5.  Low, M.G. and Finean, J.B. Release of alkaline phosphatase from membranes by a phosphatidylinositol-specific phospholipase C. Biochem. J. 167 (1977) 281–284. [PMID: 588258]
6.  Henner, D.J., Yang, M., Chen, E., Helmikss, R. and Low, M.G. Sequence of the Bacillus thuringiensis phosphatidylinositol-specific phospholipase C. Nucleic Acids Res. 16 (1988) 10383. [DOI] [PMID: 3194218]
[EC created 1972 as EC, modified 1976, transferred 2002 to EC]
Accepted name: glycosylphosphatidylinositol diacylglycerol-lyase
Reaction: 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol = 6-(α-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
For diagram of glycosylphosphatidyl-myo-inositol biosynthesis, click here
Other name(s): (glycosyl)phosphatidylinositol-specific phospholipase C; GPI-PLC; GPI-specific phospholipase C; VSG-lipase; glycosyl inositol phospholipid anchor-hydrolyzing enzyme; glycosylphosphatidylinositol-phospholipase C; glycosylphosphatidylinositol-specific phospholipase C; variant-surface-glycoprotein phospholipase C; 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming)
Systematic name: 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase [6-(α-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate-forming]
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 glycosylphostphatidylinositol (GPI) anchors. In some cases, the long-chain acyl group at the sn-1 position of glycerol is replaced by an alkyl or alk-1-enyl group. In other cases, the diacylglycerol is replaced by ceramide (see Lip-1.4 and Lip-1.5 for definition). The only characterized enzyme with this specificity is from Trypanosoma brucei, where the acyl groups are myristoyl, but the function of the trypanosome enzyme is unknown. Substitution on O-2 of the inositol blocks action of this enzyme. It is not identical with EC, glycosylphosphatidylinositol phospholipase D.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 129070-68-4
1.  Hereld, D., Krakow, J.L., Bangs, J.D., Hart, G.W. and Englund, P.T. A phospholipase C from Trypanosoma brucei which selectively cleaves the glycolipid on the variant surface glycoprotein. J. Biol. Chem. 261 (1986) 13813–13819. [PMID: 3759991]
2.  Carnall, N., Webb, H. and Carrington, M. Mutagenesis study of the glycosylphosphatidylinositol phospholipase C of Trypanosoma brucei. Mol. Biochem. Parasitol. 90 (1997) 423–432. [DOI] [PMID: 9476790]
3.  Armah, D.A. and Mensa-Wilmot, K. Tetramerization of glycosylphosphatidylinositol-specific phospholipase C from Trypanosoma brucei. J. Biol. Chem. 275 (2000) 19334–19342. [DOI] [PMID: 10764777]
[EC created 1989 as EC, transferred 2002 to EC]

Data © 2001–2022 IUBMB
Web site © 2005–2022 Andrew McDonald