The Enzyme Database

Your query returned 9 entries.    printer_iconPrintable version

Accepted name: very-long-chain acyl-lipid ω-9 desaturase
Reaction: (1) 1-hexacosanoyl-2-acyl-[phosphoglycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = 1-[(17Z)-hexacos-17-enoyl]-2-acyl-[phosphoglycerolipid] + 2 ferricytochrome b5 + 2 H2O
(2) 1-tetracosanoyl-2-acyl-[phosphoglycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = 1-[(15Z)-tetracos-15-enoyl]-2-acyl-[phosphoglycerolipid] + 2 ferricytochrome b5 + 2 H2O
Other name(s): ADS2 (gene name)
Systematic name: very-long-chain acyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase (ω98-cis-dehydrogenating)
Comments: The enzyme, characterized from the plant Arabidopsis thaliana, acts on both 24:0 and 26:0 fatty acids, introducing a cis double bond at a position 9 carbons from the methyl end. These very-long-chain fatty acids are found as a minor component of seed lipids, but also in the membrane phosphatidylethanolamine and phosphatidylserine, in sphingolipids, as precursors and components of cuticular and epicuticular waxes, and in suberin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Fukuchi-Mizutani, M., Tasaka, Y., Tanaka, Y., Ashikari, T., Kusumi, T. and Murata, N. Characterization of δA9 acyl-lipid desaturase homologues from Arabidopsis thaliana. Plant Cell Physiol. 39 (1998) 247–253. [PMID: 9559566]
2.  Smith, M.A., Dauk, M., Ramadan, H., Yang, H., Seamons, L.E., Haslam, R.P., Beaudoin, F., Ramirez-Erosa, I. and Forseille, L. Involvement of Arabidopsis acyl-coenzyme A desaturase-like2 (At2g31360) in the biosynthesis of the very-long-chain monounsaturated fatty acid components of membrane lipids. Plant Physiol. 161 (2013) 81–96. [PMID: 23175755]
[EC created 2018]
Accepted name: glycerone-phosphate O-acyltransferase
Reaction: acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): dihydroxyacetone phosphate acyltransferase (ambiguous)
Systematic name: acyl-CoA:glycerone-phosphate O-acyltransferase
Comments: A membrane protein. Uses CoA derivatives of palmitate, stearate and oleate, with highest activity on palmitoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-19-5
1.  Ballas, L.M. and Bell, R.M. Topography of glycerolipid synthetic enzymes. Synthesis of phosphatidylserine, phosphatidylinositol and glycerolipid intermediates occurs on the cytoplasmic surface of rat liver microsomal vesicles. Biochim. Biophys. Acta 665 (1981) 586–595. [DOI] [PMID: 6271231]
2.  Declercq, P.E., Haagsman, H.P., Van Veldhoven, P., Debeer, L.J., Van Golde, L.M.G. and Mannaerts, G.P. Rat liver dihydroxyacetone-phosphate acyltransferases and their contribution to glycerolipid synthesis. J. Biol. Chem. 259 (1984) 9064–9075. [PMID: 6746639]
3.  Hajra, A.K. Biosynthesis of acyl dihydroxyacetone phosphate in guinea pig liver mitochondria. J. Biol. Chem. 243 (1968) 3458–3465. [PMID: 5656381]
[EC created 1972]
Accepted name: lipid IVA palmitoyltransferase
Reaction: (1) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
(2) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IIA = 2-acyl-sn-glycero-3-phosphocholine + lipid IIB
(3) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA = 2-acyl-sn-glycero-3-phosphocholine + lipid IVB
For diagram of lipid IVB biosynthesis, click here
Glossary: palmitoyl = hexadecanoyl
hexa-acyl lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
hepta-acyl lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid IIA = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranose phosphate
lipid IIB = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranose phosphate
lipid IVB = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
Other name(s): PagP; crcA (gene name)
Systematic name: 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine:lipid-IVA palmitoyltransferase
Comments: Isolated from the bacteria Escherichia coli and Salmonella typhimurium. The enzyme prefers phosphatidylcholine with a palmitoyl group at the sn-1 position and palmitoyl or stearoyl groups at the sn-2 position. There is some activity with corresponding phosphatidylserines but only weak activity with other diacylphosphatidyl compounds. The enzyme also acts on Kdo-(2→4)-Kdo-(2→6)-lipid IVA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Bishop, R.E., Gibbons, H.S., Guina, T., Trent, M.S., Miller, S.I. and Raetz, C.R. Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria. EMBO J. 19 (2000) 5071–5080. [DOI] [PMID: 11013210]
2.  Cuesta-Seijo, J.A., Neale, C., Khan, M.A., Moktar, J., Tran, C.D., Bishop, R.E., Pomes, R. and Prive, G.G. PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler. Structure 18 (2010) 1210–1219. [DOI] [PMID: 20826347]
[EC created 2015]
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: L-serine-phosphatidylethanolamine phosphatidyltransferase
Reaction: L-1-phosphatidylethanolamine + L-serine = L-1-phosphatidylserine + ethanolamine
Other name(s): phosphatidylserine synthase 2; serine-exchange enzyme II; PTDSS2 (gene name)
Systematic name: L-1-phosphatidylethanolamine:L-serine phosphatidyltransferase
Comments: This mammalian enzyme catalyses an exchange reaction in which the polar head group of phosphatidylethanolamine is replaced by L-serine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Stone, S.J. and Vance, J.E. Cloning and expression of murine liver phosphatidylserine synthase (PSS)-2: differential regulation of phospholipid metabolism by PSS1 and PSS2. Biochem. J. 342 (1999) 57–64. [PMID: 10432300]
2.  Tomohiro, S., Kawaguti, A., Kawabe, Y., Kitada, S. and Kuge, O. Purification and characterization of human phosphatidylserine synthases 1 and 2. Biochem. J. 418 (2009) 421–429. [DOI] [PMID: 19014349]
[EC created 2010]
Accepted name: phosphatidylserine sn-1 acylhydrolase
Reaction: (1) a phosphatidylserine + H2O = a 2-acyl-1-lyso-phosphatidylserine + a fatty acid
(2) a 1-acyl-2-lyso-phosphatidylserine + H2O = glycerophosphoserine + a fatty acid
Glossary: phosphatidylserine = 3-sn-phosphatidyl-L-serine = 1,2-diacyl-sn-glycero-3-phospho-L-serine
glycerophosphoserine = sn-glycero-3-phospho-L-serine
Other name(s): phosphatidylserine-specific phospholipase A1; PS-PLA1; PLA1A (gene name)
Systematic name: 3-sn-phosphatidyl-L-serine sn-1 acylhydrolase
Comments: The enzyme, which has been described from mammals, is specific for phosphatidylserine and 2-lysophosphatidylserine, and does not act on phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid or phosphatidylinositol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Sato, T., Aoki, J., Nagai, Y., Dohmae, N., Takio, K., Doi, T., Arai, H. and Inoue, K. Serine phospholipid-specific phospholipase A that is secreted from activated platelets. A new member of the lipase family. J. Biol. Chem. 272 (1997) 2192–2198. [PMID: 8999922]
2.  Nagai, Y., Aoki, J., Sato, T., Amano, K., Matsuda, Y., Arai, H. and Inoue, K. An alternative splicing form of phosphatidylserine-specific phospholipase A1 that exhibits lysophosphatidylserine-specific lysophospholipase activity in humans. J. Biol. Chem. 274 (1999) 11053–11059. [PMID: 10196188]
3.  Hosono, H., Aoki, J., Nagai, Y., Bandoh, K., Ishida, M., Taguchi, R., Arai, H. and Inoue, K. Phosphatidylserine-specific phospholipase A1 stimulates histamine release from rat peritoneal mast cells through production of 2-acyl-1-lysophosphatidylserine. J. Biol. Chem. 276 (2001) 29664–29670. [PMID: 11395520]
4.  Aoki, J., Nagai, Y., Hosono, H., Inoue, K. and Arai, H. Structure and function of phosphatidylserine-specific phospholipase A1. Biochim. Biophys. Acta 1582 (2002) 26–32. [PMID: 12069807]
[EC created 2019]
Transferred entry: phospholipid-translocating ATPase. Now EC, P-type phospholipid transporter
[EC created 2000 (EC created 2000, incorporated 2001), deleted 2018]
Accepted name: phosphatidylserine decarboxylase
Reaction: phosphatidyl-L-serine = phosphatidylethanolamine + CO2
Other name(s): PS decarboxylase; phosphatidyl-L-serine carboxy-lyase
Systematic name: phosphatidyl-L-serine carboxy-lyase (phosphatidylethanolamine-forming)
Comments: A pyridoxal-phosphate protein. In Escherichia coli, the prosthetic group is a pyruvoyl group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-78-8
1.  Kanfer, J. and Kennedy, E.P. Metabolism and function of bacterial lipids. II. Biosynthesis of phospholipids in Escherichia coli. J. Biol. Chem. 239 (1964) 1720–1726. [PMID: 14213340]
2.  Satre, M. and Kennedy, E.P. Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli. J. Biol. Chem. 253 (1978) 479–483. [PMID: 338609]
[EC created 1976]
Accepted name: P-type phospholipid transporter
Reaction: ATP + H2O + phospholipid[side 1] = ADP + phosphate + phospholipid[side 2]
Other name(s): Mg2+-ATPase (ambiguous); flippase (ambiguous); aminophospholipid-transporting ATPase (ambiguous); phospholipid-translocating ATPase (ambiguous); phospholipid-transporting ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (P-type, phospholipid-flipping)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme moves phospholipids such as phosphatidylcholine, phosphatidylserine, and phosphatidylethanolamine from one membrane face to the other (’flippase’).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Morris, M.B., Auland, M.E., Xu, Y.H. and Roufogalis, B.D. Characterization of the Mg2+-ATPase activity of the human erythrocyte membrane. Biochem. Mol. Biol. Int. 31 (1993) 823–832. [PMID: 8136700]
2.  Vermeulen, W.P., Briede, J.J. and Rolofsen, B. Manipulation of the phosphatidylethanolamine pool in the human red cell membrane affects its Mg2+-ATPase activity. Mol. Membr. Biol. 13 (1996) 95–102. [PMID: 8839453]
3.  Suzuki, H., Kamakura, M., Morii, M. and Takeguchi, N. The phospholipid flippase activity of gastric vesicles. J. Biol. Chem. 272 (1997) 10429–10434. [DOI] [PMID: 9099684]
4.  Auland, M.E., Roufogalis, B.D., Devaux, P.F. and Zachowski, A. Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes. Proc. Natl. Acad. Sci. USA 91 (1994) 10938–10942. [DOI] [PMID: 7971987]
5.  Alder-Baerens, N., Lisman, Q., Luong, L., Pomorski, T. and Holthuis, J.C. Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles. Mol. Biol. Cell 17 (2006) 1632–1642. [DOI] [PMID: 16452632]
6.  Lopez-Marques, R.L., Poulsen, L.R., Hanisch, S., Meffert, K., Buch-Pedersen, M.J., Jakobsen, M.K., Pomorski, T.G. and Palmgren, M.G. Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA α-subunit. Mol. Biol. Cell 21 (2010) 791–801. [DOI] [PMID: 20053675]
[EC created 2000 as EC (EC created 2000, incorporated 2001), transferred 2018 to EC]

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