The Enzyme Database

Displaying entries 1-50 of 84.

<< Previous | Next >>    printer_iconPrintable version

EC 1.1.3.17     
Accepted name: choline oxidase
Reaction: choline + 2 O2 + H2O = betaine + 2 H2O2 (overall reaction)
(1a) choline + O2 = betaine aldehyde + H2O2
(1b) betaine aldehyde + O2 + H2O = betaine + H2O2
Glossary: choline = (2-hydroxyethyl)trimethylammonium
betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
betaine = glycine betaine = N,N,N-trimethylglycine = N,N,N-trimethylammonioacetate
Systematic name: choline:oxygen 1-oxidoreductase
Comments: A flavoprotein (FAD). In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [6]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in those plants, animals and bacteria that use two separate enzymes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-67-5
References:
1.  Ikuta, S., Imamura, S., Misaki, H. and Horiuti, Y. Purification and characterization of choline oxidase from Arthrobacter globiformis. J. Biochem. (Tokyo) 82 (1977) 1741–1749. [PMID: 599154]
2.  Rozwadowski, K.L., Khachatourians, G.G. and Selvaraj, G. Choline oxidase, a catabolic enzyme in Arthrobacter pascens, facilitates adaptation to osmotic stress in Escherichia coli. J. Bacteriol. 173 (1991) 472–478. [DOI] [PMID: 1987142]
3.  Rand, T., Halkier, T. and Hansen, O.C. Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis. Biochemistry 42 (2003) 7188–7194. [DOI] [PMID: 12795615]
4.  Gadda, G., Powell, N.L. and Menon, P. The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase. Arch. Biochem. Biophys. 430 (2004) 264–273. [DOI] [PMID: 15369826]
5.  Fan, F. and Gadda, G. On the catalytic mechanism of choline oxidase. J. Am. Chem. Soc. 127 (2005) 2067–2074. [DOI] [PMID: 15713082]
6.  Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932–4942. [DOI] [PMID: 12466265]
7.  Fan, F., Ghanem, M. and Gadda, G. Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress tolerance. Arch. Biochem. Biophys. 421 (2004) 149–158. [DOI] [PMID: 14678796]
8.  Gadda, G. Kinetic mechanism of choline oxidase from Arthrobacter globiformis. Biochim. Biophys. Acta 1646 (2003) 112–118. [DOI] [PMID: 12637017]
[EC 1.1.3.17 created 1978, modified 2005, modified 2007]
 
 
EC 1.1.99.1     
Accepted name: choline dehydrogenase
Reaction: choline + acceptor = betaine aldehyde + reduced acceptor
Glossary: betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
choline = (2-hydroxyethyl)trimethylammonium
Other name(s): choline oxidase; choline-cytochrome c reductase; choline:(acceptor) oxidoreductase; choline:(acceptor) 1-oxidoreductase
Systematic name: choline:acceptor 1-oxidoreductase
Comments: A quinoprotein. In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [4]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in plants, animals and bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-67-5
References:
1.  Ameyama, M., Shinagawa, E., Matsuchita, K., Takimoto, K., Nakashima, K. and Adachi, O. Mammalian choline dehydrogenase is a quinoprotein. Agric. Biol. Chem. 49 (1985) 3623–3626.
2.  Ebisuzaki, K. and Williams, J.N. Preparation and partial purification of soluble choline dehydrogenase from liver mitochondria. Biochem. J. 60 (1955) 644–646. [PMID: 13249959]
3.  Gadda, G. and McAllister-Wilkins, E.E. Cloning, expression, and purification of choline dehydrogenase from the moderate halophile Halomonas elongata. Appl. Environ. Microbiol. 69 (2003) 2126–2132. [DOI] [PMID: 12676692]
4.  Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932–4942. [DOI] [PMID: 12466265]
[EC 1.1.99.1 created 1961, modified 1989, modified 2005]
 
 
EC 1.2.1.8     
Accepted name: betaine-aldehyde dehydrogenase
Reaction: betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
Glossary: betaine = glycine betaine = N,N,N-trimethylglycine = N,N,N-trimethylammonioacetate
betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
Other name(s): betaine aldehyde oxidase; BADH; betaine aldehyde dehydrogenase; BetB
Systematic name: betaine-aldehyde:NAD+ oxidoreductase
Comments: In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) [5]. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-90-4
References:
1.  Rothschild, H.A. and Barron, E.S.G. The oxidation of betaine aldehyde by betaine aldehyde dehydrogenase. J. Biol. Chem. 209 (1954) 511–523. [PMID: 13192104]
2.  Livingstone, J.R., Maruo, T., Yoshida, I., Tarui, Y., Hirooka, K., Yamamoto, Y., Tsutui, N. and Hirasawa, E. Purification and properties of betaine aldehyde dehydrogenase from Avena sativa. J. Plant Res. 116 (2003) 133–140. [DOI] [PMID: 12736784]
3.  Muñoz-Clares, R.A., González-Segura, L., Mújica-Jiménez, C. and Contreras-Diaz, L. Ligand-induced conformational changes of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves affecting the reactivity of the catalytic thiol. Chem. Biol. Interact. (2003) 129–137. [DOI] [PMID: 12604197]
4.  Johansson, K., El-Ahmad, M., Ramaswamy, S., Hjelmqvist, L., Jornvall, H. and Eklund, H. Structure of betaine aldehyde dehydrogenase at 2.1 Å resolution. Protein Sci. 7 (1998) 2106–2117. [DOI] [PMID: 9792097]
5.  Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932–4942. [DOI] [PMID: 12466265]
[EC 1.2.1.8 created 1961, modified 2005, modified 2011]
 
 
EC 1.3.1.35      
Transferred entry: phosphatidylcholine desaturase. Now EC 1.14.19.22, microsomal oleoyl-lipid 12-desaturase
[EC 1.3.1.35 created 1984, deleted 2015]
 
 
EC 1.14.13.26      
Transferred entry: phosphatidylcholine 12-monooxygenase. Now classified as EC 1.14.18.4, phosphatidylcholine 12-monooxygenase.
[EC 1.14.13.26 created 1984, deleted 2015]
 
 
EC 1.14.14.4      
Deleted entry:  choline monooxygenase. Identical to EC 1.14.15.7
[EC 1.14.14.4 created 2000, deleted 2002]
 
 
EC 1.14.15.7     
Accepted name: choline monooxygenase
Reaction: choline + O2 + 2 reduced ferredoxin + 2 H+ = betaine aldehyde hydrate + H2O + 2 oxidized ferredoxin
Glossary: betaine = glycine betaine = N,N,N-trimethylglycine = N,N,N-trimethylammonioacetate
betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
choline = (2-hydroxyethyl)trimethylammonium
Systematic name: choline,reduced-ferredoxin:oxygen oxidoreductase
Comments: The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+. Catalyses the first step of glycine betaine synthesis. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, the reaction is catalysed by this enzyme whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) [7]. The enzyme involved in the second step, EC 1.2.1.8 (betaine-aldehyde dehydrogenase), appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 118390-76-4
References:
1.  Brouquisse, R., Weigel, P., Rhodes, D., Yocum, C.F. and Hanson, A.D. Evidence for a ferredoxin-dependent choline monooxygenase from spinach chloroplast stroma. Plant Physiol. 90 (1989) 322–329. [PMID: 16666757]
2.  Burnet, M., Lafontaine, P.J. and Hanson, A.D. Assay, purification, and partial characterization of choline monooxygenase from spinach. Plant Physiol. 108 (1995) 581–588. [PMID: 12228495]
3.  Rathinasabapathi, B., Burnet, M., Russell, B.L., Gage, D.A., Liao, P., Nye, G.J., Scott, P., Golbeck, J.H. and Hanson, A.D. Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning. Proc. Natl. Acad. Sci. USA 94 (1997) 3454–3458. [DOI] [PMID: 9096415]
4.  Russell, B.L., Rathinasabapathi, B. and Hanson, A.D. Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth. Plant Physiol. 116 (1998) 859–865. [PMID: 9489025]
5.  Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. Glycine betaine synthesis in transgenic tobacco expressing choline monooxygenase is limited by the endogenous choline supply. Plant J. 16 (1998) 101–110.
6.  Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. The endogenous choline supply limits glycine betaine synthesis in transgenic tobacco expressing choline. Plant J. 16 (1998) 487–496. [DOI] [PMID: 9881168]
7.  Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932–4942. [DOI] [PMID: 12466265]
[EC 1.14.15.7 created 2001, modified 2002 (EC 1.14.14.4 created 2000, incorporated 2002), modified 2005, modified 2011]
 
 
EC 1.14.18.4     
Accepted name: phosphatidylcholine 12-monooxygenase
Reaction: a 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + 2 ferrocytochrome b5 + O2 + 2 H+ = a 1-acyl-2-[(12R)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + 2 ferricytochrome b5 + H2O
Glossary: ricinoleic acid = (9Z,12R)-12-hydroxyoctadec-9-enoic acid
Other name(s): ricinoleic acid synthase; oleate Δ12-hydroxylase; oleate Δ12-monooxygenase
Systematic name: 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine,ferrocytochrome-b5:oxygen oxidoreductase (12-hydroxylating)
Comments: The enzyme, characterized from the plant Ricinus communis (castor bean), is involved in production of the 12-hydroxylated fatty acid ricinoleate. The enzyme, which shares sequence similarity with fatty-acyl desaturases, requires a cytochrome b5 as the electron donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77950-95-9
References:
1.  Galliard, T. and Stumpf, P.K. Fat metabolism in higher plants. 30. Enzymatic synthesis of ricinoleic acid by a microsomal preparation from developing Ricinus communis seeds. J. Biol. Chem. 241 (1966) 5806–5812. [PMID: 4289003]
2.  Moreau, R.A. and Stumpf, P.K. Recent studies of the enzymic-synthesis of ricinoleic acid by developing castor beans. Plant Physiol. 67 (1981) 672–676. [PMID: 16661734]
3.  Smith, M.A., Jonsson, L., Stymne, S. and Stobart, K. Evidence for cytochrome b5 as an electron donor in ricinoleic acid biosynthesis in microsomal preparations from developing castor bean (Ricinus communis L.). Biochem. J. 287 (1992) 141–144. [PMID: 1417766]
4.  Lin, J.T., McKeon, T.A., Goodrich-Tanrikulu, M. and Stafford, A.E. Characterization of oleoyl-12-hydroxylase in castor microsomes using the putative substrate, 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine. Lipids 31 (1996) 571–577. [DOI] [PMID: 8784737]
5.  Broun, P. and Somerville, C. Accumulation of ricinoleic, lesquerolic, and densipolic acids in seeds of transgenic Arabidopsis plants that express a fatty acyl hydroxylase cDNA from castor bean. Plant Physiol. 113 (1997) 933–942. [PMID: 9085577]
[EC 1.14.18.4 created 1984 as EC 1.14.13.26, transferred 2015 to EC 1.14.18.4]
 
 
EC 1.14.19.16     
Accepted name: linoleoyl-lipid Δ12 conjugase (11E,13Z-forming)
Reaction: a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (9Z,11E,13Z)-octadeca-9,11,13-trienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Glossary: punicate = (9Z,11E,13Z)-octadeca-9,11,13-trienoate
linoleate = (9Z,12Z)-octadeca-9,12-dienoate
Other name(s): Fac (gene name)
Systematic name: linoleoyl-lipid,ferrocytochrome-b5:oxygen 11,14 allylic oxidase (11E,13Z-forming)
Comments: The enzyme, characterized from the plants Punica granatum (pomegranate) and Trichosanthes kirilowii (Mongolian snake-gourd), converts a single cis double bond at position 12 of linoleate incorporated into phosphatidylcholine into conjugated 11-trans and 13-cis double bonds. cf. EC 1.14.19.33, Δ12 acyl-lipid conjugase (11E,13E-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hornung, E., Pernstich, C. and Feussner, I. Formation of conjugated Δ11Δ13-double bonds by Δ12-linoleic acid (1,4)-acyl-lipid-desaturase in pomegranate seeds. Eur. J. Biochem. 269 (2002) 4852–4859. [DOI] [PMID: 12354116]
2.  Iwabuchi, M., Kohno-Murase, J. and Imamura, J. Δ12-oleate desaturase-related enzymes associated with formation of conjugated trans-Δ11, cis-Δ13 double bonds. J. Biol. Chem. 278 (2003) 4603–4610. [DOI] [PMID: 12464604]
[EC 1.14.19.16 created 2015]
 
 
EC 1.14.19.22     
Accepted name: acyl-lipid ω-6 desaturase (cytochrome b5)
Reaction: an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a linoleoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Other name(s): oleate desaturase (ambiguous); linoleate synthase (ambiguous); oleoyl-CoA desaturase (incorrect); oleoylphosphatidylcholine desaturase (ambiguous); phosphatidylcholine desaturase (ambiguous); n-6 desaturase (ambiguous); FAD2 (gene name)
Systematic name: 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine,ferrocytochrome-b5:oxygen oxidoreductase (12,13 cis-dehydrogenating)
Comments: This microsomal enzyme introduces a cis double bond in fatty acids attached to lipid molecules at a location 6 carbons away from the methyl end of the fatty acid. The distance from the carboxylic acid end of the molecule does not affect the location of the new double bond. The most common substrates are oleoyl groups attached to either the sn-1 or sn-2 position of the glycerol backbone in phosphatidylcholine. cf. EC 1.14.19.23, acyl-lipid ω-6 desaturase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72536-70-0
References:
1.  Pugh, E.L. and Kates, M. Characterization of a membrane-bound phospholipid desaturase system of Candida lipolytica. Biochim. Biophys. Acta 380 (1975) 442–453. [DOI] [PMID: 166662]
2.  Slack, C.R., Roughan, P.G. and Browse, J. Evidence for an oleoyl phosphatidylcholine desaturase in microsomal preparations from cotyledons of safflower (Carthamus tinctorius) seed. Biochem. J. 179 (1979) 649–656. [PMID: 475773]
3.  Stymne, S. and Appelqvist, L.-A. The biosynthesis of linoleate from oleoyl-CoA via oleoyl-phosphatidylcholine in microsomes of developing safflower seeds. Eur. J. Biochem. 90 (1978) 223–229. [DOI] [PMID: 710426]
4.  Smith, M.A., Cross, A.R., Jones, O.T., Griffiths, W.T., Stymne, S. and Stobart, K. Electron-transport components of the 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine Δ12-desaturase (Δ12-desaturase) in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons. Biochem. J. 272 (1990) 23–29. [PMID: 2264826]
5.  Kearns, E.V., Hugly, S. and Somerville, C.R. The role of cytochrome b5 in Δ12 desaturation of oleic acid by microsomes of safflower (Carthamus tinctorius L.). Arch. Biochem. Biophys. 284 (1991) 431–436. [DOI] [PMID: 1989527]
6.  Miquel, M. and Browse, J. Arabidopsis mutants deficient in polyunsaturated fatty acid synthesis. Biochemical and genetic characterization of a plant oleoyl-phosphatidylcholine desaturase. J. Biol. Chem. 267 (1992) 1502–1509. [PMID: 1730697]
[EC 1.14.19.22 created 1984 as EC 1.3.1.35, transferred 2015 to EC 1.14.19.22]
 
 
EC 1.14.19.23     
Accepted name: acyl-lipid (n+3)-(Z)-desaturase (ferredoxin)
Reaction: an oleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a linoleoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Other name(s): acyl-lipid ω6-desaturase (ferredoxin); oleate desaturase (ambiguous); linoleate synthase (ambiguous); oleoyl-CoA desaturase (ambiguous); oleoylphosphatidylcholine desaturase (ambiguous); phosphatidylcholine desaturase (ambiguous); FAD6 (gene name)
Systematic name: oleoyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (12,13 cis-dehydrogenating)
Comments: This plastidial enzyme is able to insert a cis double bond in monounsaturated fatty acids incorporated into glycerolipids. The enzyme introduces the new bond at a position 3 carbons away from the existing double bond, towards the methyl end of the fatty acid. The native substrates are oleoyl (18:1 Δ9) and (Z)-hexadec-7-enoyl (16:1 Δ7) groups attached to either position of the glycerol backbone in glycerolipids, resulting in the introduction of the second double bond at positions 12 and 10, respectively This prompted the suggestion that this is an ω6 desaturase. However, when acting on palmitoleoyl groups(16:1 Δ9), the enzyme introduces the second double bond at position 12 (ω4), indicating it is an (n+3) desaturase [3]. cf. EC 1.14.19.34, acyl-lipid (9+3)-(E)-desaturase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schmidt, H. and Heinz, E. Desaturation of oleoyl groups in envelope membranes from spinach chloroplasts. Proc. Natl. Acad. Sci. USA 87 (1990) 9477–9480. [DOI] [PMID: 11607123]
2.  Schmidt, H. and Heinz, E. Involvement of ferredoxin in desaturation of lipid-bound oleate in chloroplasts. Plant Physiol. 94 (1990) 214–220. [PMID: 16667689]
3.  Hitz, W.D., Carlson, T.J., Booth, J.R., Jr., Kinney, A.J., Stecca, K.L. and Yadav, N.S. Cloning of a higher-plant plastid ω-6 fatty acid desaturase cDNA and its expression in a cyanobacterium. Plant Physiol. 105 (1994) 635–641. [PMID: 8066133]
4.  Falcone, D.L., Gibson, S., Lemieux, B. and Somerville, C. Identification of a gene that complements an Arabidopsis mutant deficient in chloroplast ω 6 desaturase activity. Plant Physiol. 106 (1994) 1453–1459. [PMID: 7846158]
5.  Schmidt, H., Dresselhaus, T., Buck, F. and Heinz, E. Purification and PCR-based cDNA cloning of a plastidial n-6 desaturase. Plant Mol. Biol. 26 (1994) 631–642. [PMID: 7948918]
[EC 1.14.19.23 created 2015]
 
 
EC 1.14.19.25     
Accepted name: acyl-lipid ω-3 desaturase (cytochrome b5)
Reaction: a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an α-linolenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Glossary: linoleoyl-[glycerolipid] = (9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid]
α-linolenoyl-[glycerolipid] = (9Z,12Z,15Z)-octadeca-9,12,15-trienoyl-[glycerolipid]
Other name(s): FAD3
Systematic name: (9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase (15,16 cis-dehydrogenating)
Comments: This microsomal enzyme introduces a cis double bond three carbons away from the methyl end of a fatty acid incorporated into a glycerolipid. The distance from the carboxylic acid end of the molecule does not have an effect. The plant enzyme acts on carbon 15 of linoleoyl groups incorporated into both the sn-1 and sn-2 positions of the glycerol backbone of phosphatidylcholine and other phospholipids, converting them into α-linolenoyl groups. The enzyme from the fungus Mortierella alpina acts on γ-linolenoyl and arachidonoyl groups, converting them into stearidonoyl and icosapentaenoyl groups, respectively [3]. cf. EC 1.14.19.35, sn-2 acyl-lipid ω-3 desaturase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Browse, J., McConn, M., James, D., Jr. and Miquel, M. Mutants of Arabidopsis deficient in the synthesis of α-linolenate. Biochemical and genetic characterization of the endoplasmic reticulum linoleoyl desaturase. J. Biol. Chem. 268 (1993) 16345–16351. [PMID: 8102138]
2.  Arondel, V., Lemieux, B., Hwang, I., Gibson, S., Goodman, H.M. and Somerville, C.R. Map-based cloning of a gene controlling ω-3 fatty acid desaturation in Arabidopsis. Science 258 (1992) 1353–1355. [DOI] [PMID: 1455229]
3.  Sakuradani, E., Abe, T., Iguchi, K. and Shimizu, S. A novel fungal ω3-desaturase with wide substrate specificity from arachidonic acid-producing Mortierella alpina 1S-4. Appl. Microbiol. Biotechnol. 66 (2005) 648–654. [DOI] [PMID: 15538555]
[EC 1.14.19.25 created 2015]
 
 
EC 2.1.1.17     
Accepted name: phosphatidylethanolamine N-methyltransferase
Reaction: S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
Other name(s): PEMT; LMTase; lipid methyl transferase; phosphatidylethanolamine methyltransferase; phosphatidylethanolamine-N-methylase; phosphatidylethanolamine-S-adenosylmethionine methyltransferase
Systematic name: S-adenosyl-L-methionine:phosphatidylethanolamine N-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-91-0
References:
1.  Hirata, F., Viveros, O.H., Diliberto, E.J., Jr. and Axelrod, J. Identification and properties of two methyltransferases in conversion of phosphatidylethanolamine to phosphatidylcholine. Proc. Natl. Acad. Sci. USA 75 (1978) 1718–1721. [DOI] [PMID: 25437]
2.  Morgan, T.E. Isolation and characterization of lipid N-methyltransferase from dog lung. Biochim. Biophys. Acta 178 (1969) 21–34. [DOI] [PMID: 5773456]
3.  Schneider, W.J. and Vance, D.E. Conversion of phosphatidylethanolamine to phosphatidylcholine in rat liver. Partial purification and characterization of the enzymatic activities. J. Biol. Chem. 254 (1979) 3886–3891. [PMID: 438165]
[EC 2.1.1.17 created 1972]
 
 
EC 2.1.1.71     
Accepted name: phosphatidyl-N-methylethanolamine N-methyltransferase
Reaction: S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine
Other name(s): phosphatidylmonomethylethanolamine methyltransferase; methyltransferase II; phospholipid methyltransferase; PLMT; phosphatidyl-N-methylethanolamine methyltransferase; phosphatidyl-N-monomethylethanolamine methyltransferase; phosphatidylethanolamine methyltransferase I; phosphatidylmonomethylethanolamine methyltransferase
Systematic name: S-adenosyl-L-methionine:phosphatidyl-N-methylethanolamine N-methyltransferase
Comments: The enzyme also catalyses the transfer of a further methyl group, producing phosphatidylcholine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 67167-73-1
References:
1.  Hirata, F., Viveros, O.H., Diliberto, E.J., Jr. and Axelrod, J. Identification and properties of two methyltransferases in conversion of phosphatidylethanolamine to phosphatidylcholine. Proc. Natl. Acad. Sci. USA 75 (1978) 1718–1721. [DOI] [PMID: 25437]
2.  Schneider, W.J. and Vance, D.E. Conversion of phosphatidylethanolamine to phosphatidylcholine in rat liver. Partial purification and characterization of the enzymatic activities. J. Biol. Chem. 254 (1979) 3886–3891. [PMID: 438165]
[EC 2.1.1.71 created 1984]
 
 
EC 2.1.1.103     
Accepted name: phosphoethanolamine N-methyltransferase
Reaction: S-adenosyl-L-methionine + ethanolamine phosphate = S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
Other name(s): phosphoethanolamine methyltransferase
Systematic name: S-adenosyl-L-methionine:ethanolamine-phosphate N-methyltransferase
Comments: The enzyme may catalyse the transfer of two further methyl groups to the product.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 171040-79-2
References:
1.  Datko, A.H. and Mudd, S.H. Enzymes of phosphatidylcholine synthesis in Lemna, soybean, and carrot. Plant Physiol. 88 (1988) 1338–1348. [PMID: 16666464]
[EC 2.1.1.103 created 1992]
 
 
EC 2.3.1.6     
Accepted name: choline O-acetyltransferase
Reaction: acetyl-CoA + choline = CoA + O-acetylcholine
Other name(s): choline acetylase; choline acetyltransferase
Systematic name: acetyl-CoA:choline O-acetyltransferase
Comments: Propanoyl-CoA can act, more slowly, in place of acetyl-CoA.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9012-78-6
References:
1.  Berman, R., Wilson, I.B. and Nachmansohn, D. Choline acetylase specificity in relation to biological function. Biochim. Biophys. Acta 12 (1953) 315–324. [DOI] [PMID: 13115440]
2.  Berry, J.F. and Whittaker, V.P. The acyl-group specificity of choline acetylase. Biochem. J. 73 (1959) 447–458. [PMID: 13799882]
3.  Fritz, I.B. and Schultz, S.K. Carnitine acetyltransferase. II. Inhibition by carnitine analogues and by sulfhydryl reagents. J. Biol. Chem. 240 (1965) 2188–2192. [PMID: 14299645]
4.  Schuberth, J. Choline acetyltransferase. Purification and effect of salts on the mechanism of the enzyme-catalysed reaction. Biochim. Biophys. Acta 122 (1966) 470–481.
[EC 2.3.1.6 created 1961]
 
 
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, 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 2.3.1.25     
Accepted name: plasmalogen synthase
Reaction: acyl-CoA + 1-O-(alk-1-enyl)glycero-3-phosphocholine = CoA + plasmenylcholine
Glossary: 1-O-(alk-1-enyl)glycero-3-phosphocholine = 1-alkenylglycerophosphocholine,
plasmenylcholine = 1-alkenyl-2-acylglycerophosphocholine
Other name(s): lysoplasmenylcholine acyltransferase; O-1-alkenylglycero-3-phosphorylcholine acyltransferase; 1-alkenyl-glycero-3-phosphorylcholine:acyl-CoA acyltransferase; 1-alkenylglycerophosphocholine O-acyltransferase
Systematic name: acyl-CoA:1-O-(alk-1-enyl)-glycero-3-phosphocholine 2-O-acyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-10-6
References:
1.  Waku, K. and Lands, W.E.M. Acyl coenzyme A:1-alkenyl-glycero-3-phosphorylcholine acyltransferase action in plasmalogen biosynthesis. J. Biol. Chem. 243 (1968) 2654–2659. [PMID: 5689955]
2.  Arthur, G. and Choy, P.C. Acylation of 1-alkenyl-glycerophosphocholine and 1-acyl-glycerophosphocholine in guinea pig heart. Biochem. J. 236 (1986) 481–487. [PMID: 3753462]
[EC 2.3.1.25 created 1972, modified 2013]
 
 
EC 2.3.1.43     
Accepted name: phosphatidylcholine—sterol O-acyltransferase
Reaction: phosphatidylcholine + a sterol = 1-acylglycerophosphocholine + a sterol ester
Other name(s): lecithin—cholesterol acyltransferase; phospholipid—cholesterol acyltransferase; LCAT (lecithin-cholesterol acyltransferase); lecithin:cholesterol acyltransferase; lysolecithin acyltransferase
Systematic name: phosphatidylcholine:sterol O-acyltransferase
Comments: Palmitoyl, oleoyl and linoleoyl residues can be transferred; a number of sterols, including cholesterol, can act as acceptors. The bacterial enzyme also catalyses the reactions of EC 3.1.1.4 phospholipase A2 and EC 3.1.1.5 lysophospholipase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-14-5
References:
1.  Bartlett, K., Keat, M.J. and Mercer, E.I. Biosynthesis of sterol esters in Phycomyces blakesleeanus. Phytochemistry 13 (1974) 1107–1113.
2.  Buckley, J.T., Halasa, L.N. and Macintyre, S. Purification and partial characterization of a bacterial phospholipid: cholesterol acyltransferase. J. Biol. Chem. 257 (1982) 3320–3325. [PMID: 7061477]
3.  Glomset, J.A.J. The plasma lecithins:cholesterol acyltransferase reaction. Lipid Res. 9 (1968) 155–167. [PMID: 4868699]
4.  Vahouny, G.V. and Tradwell, C.R. Enzymatic synthesis and hydrolysis of cholesterol esters. Methods Biochem. Anal. 16 (1968) 219–272. [PMID: 4877146]
[EC 2.3.1.43 created 1972, modified 1976]
 
 
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, 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 2.3.1.52     
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
References:
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 2.3.1.52 created 1976]
 
 
EC 2.3.1.53     
Accepted name: phenylalanine N-acetyltransferase
Reaction: acetyl-CoA + L-phenylalanine = CoA + N-acetyl-L-phenylalanine
Other name(s): acetyl-CoA-L-phenylalanine α-N-acetyltransferase
Systematic name: acetyl-CoA:L-phenylalanine N-acetyltransferase
Comments: Also acts, more slowly, on L-histidine and L-alanine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-16-5
References:
1.  Leuzinger, W., Baker, A.L. and Cauvin, E. Acetylcholinesterase. II. Crystallization, absorption spectra, isoionic point. Proc. Natl. Acad. Sci. USA 59 (1968) 620–623. [DOI] [PMID: 5238989]
[EC 2.3.1.53 created 1976]
 
 
EC 2.3.1.62     
Accepted name: 2-acylglycerophosphocholine O-acyltransferase
Reaction: acyl-CoA + 2-acyl-sn-glycero-3-phosphocholine = CoA + phosphatidylcholine
Other name(s): 2-acylglycerol-3-phosphorylcholine acyltransferase; 2-acylglycerophosphocholine acyltransferase
Systematic name: acyl-CoA:2-acyl-sn-glycero-3-phosphocholine O-acyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 64295-73-4
References:
1.  Lands, W.E.M. and Hart, P. Metabolism of glycerolipids. VI. Specificities of acyl coenzyme A:phospholipid acyltransferases. J. Biol. Chem. 240 (1965) 1905–1911. [PMID: 14299609]
2.  van den Bosch, H., van Golde, L.M.G., Slotboom, A.J. and van Deenen, L.L.M. The acylation of isomeric monoacyl phosphatidylcholines. Biochim. Biophys. Acta 152 (1968) 694–703. [DOI] [PMID: 5660084]
[EC 2.3.1.62 created 1978]
 
 
EC 2.3.1.63     
Accepted name: 1-alkylglycerophosphocholine O-acyltransferase
Reaction: acyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acyl-1-alkyl-sn-glycero-3-phosphocholine
Systematic name: acyl-CoA:1-alkyl-sn-glycero-3-phosphocholine O-acyltransferase
Comments: May be identical with EC 2.3.1.23 1-acylglycerophosphocholine O-acyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 58693-63-3
References:
1.  Waku, K. and Nakazawa, Y. Acyltransferase activity to 1-O-alkyl-glycero-3-phosphorylcholine in sarcoplasmic reticulum. J. Biochem. (Tokyo) 68 (1970) 459–466. [PMID: 5488773]
2.  Waku, K. and Nakazawa, Y. Acyltransferae activity to 1-acyl-, 1-O-alkenyl-, and 1-O-alkyl-glycero-3-phosphorylcholine in Ehrlich ascites tumor cells. J. Biochem. (Tokyo) 72 (1972) 495–497. [PMID: 4644313]
[EC 2.3.1.63 created 1978]
 
 
EC 2.3.1.67     
Accepted name: 1-alkylglycerophosphocholine O-acetyltransferase
Reaction: acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
Other name(s): acetyl-CoA:1-alkyl-2-lyso-sn-glycero-3-phosphocholine 2-O-acetyltransferase; acetyl-CoA:lyso-PAF acetyltransferase; 1-alkyl-2-lysolecithin acetyltransferase; acyl-CoA:1-alkyl-sn-glycero-3-phosphocholine acyltransferase; blood platelet-activating factor acetyltransferase; lyso-GPC:acetyl CoA acetyltransferase; lyso-platelet activating factor:acetyl-CoA acetyltransferase; lysoPAF:acetyl CoA acetyltransferase; PAF acetyltransferase; platelet-activating factor acylhydrolase; platelet-activating factor-synthesizing enzyme; 1-alkyl-2-lyso-sn-glycero-3-phosphocholine acetyltransferase; lyso-platelet-activating factor:acetyl-CoA acetyltransferase
Systematic name: acetyl-CoA:1-alkyl-sn-glycero-3-phosphocholine 2-O-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 76773-96-1
References:
1.  Wykle, R.L., Malone, B. and Snyder, F. Enzymatic synthesis of 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine, a hypotensive and platelet-aggregating lipid. J. Biol. Chem. 255 (1980) 10256–10260. [PMID: 7430122]
[EC 2.3.1.67 created 1984]
 
 
EC 2.3.1.83     
Accepted name: phosphatidylcholine—dolichol O-acyltransferase
Reaction: 3-sn-phosphatidylcholine + dolichol = 1-acyl-sn-glycero-3-phosphocholine + acyldolichol
Systematic name: 3-sn-phosphatidylcholine:dolichol O-acyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 111839-04-4
References:
1.  Keenan, R. and Kruczek, H. The esterification of dolichol by rat liver microsomes. Biochemistry 15 (1976) 1586–1591. [PMID: 4095]
2.  Radominska-Pyrek, A., Chojnachi, T. and Zulezyk, W. Acyl esters of polyprenols: specificity of microsomal transacylase for polyprenols of different chain length and saturation. Acta Biochim. Pol. 26 (1979) 125–134. [PMID: 506613]
[EC 2.3.1.83 created 1984]
 
 
EC 2.3.1.91     
Accepted name: sinapoylglucose—choline O-sinapoyltransferase
Reaction: 1-O-sinapoyl-β-D-glucose + choline = D-glucose + sinapoylcholine
Glossary: sinapoyl = 4-hydroxy-3,5-dimethoxycinnamoyl
Other name(s): sinapine synthase
Systematic name: 1-O-sinapoyl-β-D-glucose:choline 1-O-sinapoyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 85205-00-1
References:
1.  Gräwe, W. and Strack, D. Partial-purification and some properties of 1-sinapoylglucose-choline sinapoyltransferase (sinapine synthase) from seeds of Raphanus sativus L. and Sinapis alba L. Z. Naturforsch. C: Biosci. 41 (1986) 28–33.
[EC 2.3.1.91 created 1986]
 
 
EC 2.3.1.104      
Deleted entry: 1-alkenylglycerophosphocholine O-acyltransferase. The activity is covered by EC 2.3.1.25, plasmalogen synthase
[EC 2.3.1.104 created 1989, deleted 2013]
 
 
EC 2.3.1.135     
Accepted name: phosphatidylcholine—retinol O-acyltransferase
Reaction: phosphatidylcholine + retinol—[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester—[cellular-retinol-binding-protein]
Glossary: phosphatidylcholine = lecithin
Other name(s): lecithin—retinol acyltransferase; phosphatidylcholine:retinol-(cellular-retinol-binding-protein) O-acyltransferase; lecithin:retinol acyltransferase; lecithin-retinol acyltransferase; retinyl ester synthase; LRAT; lecithin retinol acyl transferase
Systematic name: phosphatidylcholine:retinol—[cellular-retinol-binding-protein] O-acyltransferase
Comments: A key enzyme in retinoid metabolism, catalysing the transfer of an acyl group from the sn-1 position of phosphatidylcholine to retinol, forming retinyl esters which are then stored. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein, but has higher affinity for the bound form. Can also esterify 11-cis-retinol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 117444-03-8
References:
1.  MacDonald, P.N. and Ong, D.E. Evidence for a lecithin-retinol acyltransferase activity in the rat small intestine. J. Biol. Chem. 263 (1988) 12478–12482. [PMID: 3410848]
2.  Saari, J.C. and Bredberg, D.L. Lecithin:retinol acyltransferase in retinal pigment epithelial microsomes. J. Biol. Chem. 264 (1989) 8636. [PMID: 2722792]
3.  Saari, J.C., Bredberg, D.L. and Farrell, D.F. Retinol esterification in bovine retinal pigment epithelium: reversibility of lecithin:retinol acyltransferase. Biochem. J. 291 (1993) 697–700. [PMID: 8489497]
4.  Mata, N.L. and Tsin, A.T. Distribution of 11-cis LRAT, 11-cis RD and 11-cis REH in bovine retinal pigment epithelium membranes. Biochim. Biophys. Acta 1394 (1998) 16–22. [DOI] [PMID: 9767084]
5.  Ruiz, A., Winston, A., Lim, Y.H., Gilbert, B.A., Rando, R.R. and Bok, D. Molecular and biochemical characterization of lecithin retinol acyltransferase. J. Biol. Chem. 274 (1999) 3834–3841. [DOI] [PMID: 9920938]
[EC 2.3.1.135 created 1992, modified 2011]
 
 
EC 2.3.1.147     
Accepted name: glycerophospholipid arachidonoyl-transferase (CoA-independent)
Reaction: 1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine = 1-organyl-2-arachidonoyl-sn-glycero-3-phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine
Systematic name: 1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine arachidonoyltransferase (CoA-independent)
Comments: Catalyses the transfer of arachidonate and other polyenoic fatty acids from intact choline or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso-glycerophospholipid. The organyl group on sn-1 of the donor or acceptor molecule can be alkyl, acyl or alk-1-enyl. The term 'radyl' has sometimes been used to refer to such substituting groups. Differs from EC 2.3.1.148 glycerophospholipid acyltransferase (CoA-dependent) in not requiring CoA and in its specificity for poly-unsaturated acyl groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 102347-79-5
References:
1.  Robinson, M., Blank, M.L., Snyder, F. Acylation of lysophospholipids by rabbit alveolar macrophages. Specific CoA-dependent and CoA-independent reactions. J. Biol. Chem. 260 (1985) 7889–7895. [PMID: 4008481]
2.  Snyder, F., Lee, T.C., Blank, M.L. The role of transacylases in the metabolism of arachidonate and platelet-activating factor. Prog. Lipid Res. 31 (1992) 65–86. [DOI] [PMID: 1641397]
[EC 2.3.1.147 created 1999]
 
 
EC 2.3.1.148     
Accepted name: glycerophospholipid acyltransferase (CoA-dependent)
Reaction: 1-organyl-2-acyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine = 1-organyl-2-acyl-sn-glycero-3-phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine
Systematic name: 1-organyl-2-acyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine acyltransferase (CoA-dependent)
Comments: Catalyses the transfer of fatty acids from intact choline- or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso-glycerophospholipid. The organyl group on sn-1 of the donor or acceptor molecule can be alkyl, acyl or alk-1-enyl. The term 'radyl' has sometimes been used to refer to such substituting groups. Differs from EC 2.3.1.147 glycerophospholipid arachidonoyl-transferase (CoA-independent) in requiring CoA and not favouring the transfer of polyunsaturated acyl groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-54-0
References:
1.  Irvine, R.F., Dawson, R.M.C. Transfer of arachidonic acid between phospholipids in rat liver microsomes. Biochem. Biophys. Res. Commun. 91 (1979) 1399–1405. [DOI] [PMID: 526311]
2.  Robinson, M., Blank, M.L., Snyder, F. Acylation of lysophospholipids by rabbit alveolar macrophages. Specific CoA-dependent and CoA-independent reactions. J. Biol. Chem. 260 (1985) 7889–7895. [PMID: 4008481]
3.  Snyder, F., Lee, T.C., Blank, M.L. The role of transacylases in the metabolism of arachidonate and platelet-activating factor. Prog. Lipid Res. 31 (1992) 65–86. [DOI] [PMID: 1641397]
[EC 2.3.1.148 created 1999]
 
 
EC 2.3.1.149     
Accepted name: platelet-activating factor acetyltransferase
Reaction: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phospholipid = 1-alkyl-2-lyso-sn-glycero-3-phosphocholine + 1-organyl-2-acetyl-sn-glycero-3-phospholipid
Other name(s): PAF acetyltransferase
Systematic name: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-glycero-3-phospholipid acetyltransferase
Comments: Catalyses the transfer of the acetyl group from 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-activating factor) to the sn-2 position of lyso-glycerophospholipids containing ethanolamine, choline, serine, inositol or phosphate groups at the sn-3 position as well as to sphingosine and long-chain fatty alcohols. The organyl group can be alkyl, acyl or alk-1-enyl (sometimes also collectively referred to as ’radyl’).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9012-30-0
References:
1.  Lee, T.C., Uemura, Y., Snyder, F. A novel CoA-independent transacetylase produces the ethanolamine plasmalogen and acyl analogs of platelet-activating factor (PAF) with PAF as the acetate donor in HL-60 cells. J. Biol. Chem. 267 (1992) 19992–20001. [PMID: 1400315]
[EC 2.3.1.149 created 1999]
 
 
EC 2.3.1.251     
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, PDB
References:
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 2.3.1.251 created 2015]
 
 
EC 2.7.1.32     
Accepted name: choline kinase
Reaction: ATP + choline = ADP + phosphocholine
Other name(s): choline kinase (phosphorylating); choline phosphokinase; choline-ethanolamine kinase
Systematic name: ATP:choline phosphotransferase
Comments: Ethanolamine and its methyl and ethyl derivatives can also act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-67-9
References:
1.  Hayashi, S. and Lin, E.C.C. Purification and properties of glycerol kinase from Escherichia coli. J. Biol. Chem. 242 (1967) 1030–1035. [PMID: 5335908]
2.  Wittenberg, J. and Kornberg, A. Choline phosphokinase. J. Biol. Chem. 202 (1953) 431–444. [PMID: 13061469]
[EC 2.7.1.32 created 1961]
 
 
EC 2.7.1.82     
Accepted name: ethanolamine kinase
Reaction: ATP + ethanolamine = ADP + O-phosphoethanolamine
Other name(s): ethanolamine kinase (phosphorylating); ethanolamine phosphokinase
Systematic name: ATP:ethanolamine O-phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-78-9
References:
1.  Faulkner, A. and Turner, J.M. Phosphorylation of ethanolamine in catabolism: biodegradative adenosine triphosphate-ethanolamine phosphotransferase and related enzymes in bacteria. Biochem. Soc. Trans. 2 (1974) 133–136.
2.  Sung, C.-P. and Johnstone, R.M. Phosphorylation of choline and ethanolamine in Ehrlich ascites-carcinoma cells. Biochem. J. 105 (1967) 497–503. [PMID: 5626092]
3.  Weinhold, P.A. and Rethy, V.B. Ethanolamine phosphokinase: activity and properties during liver development. Biochim. Biophys. Acta 276 (1972) 143–154. [DOI] [PMID: 5047700]
[EC 2.7.1.82 created 1976]
 
 
EC 2.7.7.15     
Accepted name: choline-phosphate cytidylyltransferase
Reaction: CTP + phosphocholine = diphosphate + CDP-choline
Other name(s): phosphorylcholine transferase; CDP-choline pyrophosphorylase; CDP-choline synthetase; choline phosphate cytidylyltransferase; CTP-phosphocholine cytidylyltransferase; CTP:phosphorylcholine cytidylyltransferase; cytidine diphosphocholine pyrophosphorylase; phosphocholine cytidylyltransferase; phosphorylcholine cytidylyltransferase; phosphorylcholine:CTP cytidylyltransferase
Systematic name: CTP:phosphocholine cytidylyltransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-34-0
References:
1.  Borkenhagen, L.F. and Kennedy, E.P. The enzymatic synthesis of cytidine diphosphate choline. J. Biol. Chem. 227 (1957) 951–962. [PMID: 13463016]
2.  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]
3.  Williams-Ashman, H.G. and Banks, J. Participation of cytidine coenzymes in the metabolism of choline by seminal vesicles. J. Biol. Chem. 223 (1956) 509–521. [PMID: 13376620]
[EC 2.7.7.15 created 1961]
 
 
EC 2.7.7.57     
Accepted name: N-methylphosphoethanolamine cytidylyltransferase
Reaction: CTP + N-methylethanolamine phosphate = diphosphate + CDP-N-methylethanolamine
Other name(s): monomethylethanolamine phosphate cytidylyltransferase; CTP:P-MEA cytidylyltransferase
Systematic name: CTP:N-methylethanolamine-phosphate cytidylyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 119345-28-7
References:
1.  Datko, A.H. and Mudd, S.H. Enzymes of phosphatidylcholine synthesis in Lemna, soybean, and carrot. Plant Physiol. 88 (1988) 1338–1348. [PMID: 16666464]
[EC 2.7.7.57 created 1992]
 
 
EC 2.7.7.107     
Accepted name: (2-aminoethyl)phosphonate cytidylyltransferase
Reaction: CTP + (2-aminoethyl)phosphonate = diphosphate + CMP-(2-aminoethyl)phosphonate
Other name(s): pntC (gene name)
Systematic name: CTP:(2-aminoethyl)phosphonate cytidylyltransferase
Comments: This bacterial enzyme activates (2-aminoethyl)phosphonate for incorporation into cell wall phosphonoglycans and phosphonolipids, much like EC 2.7.7.15, choline-phosphate cytidylyltransferase, activates phosphocholine for the same purpose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rice, K., Batul, K., Whiteside, J., Kelso, J., Papinski, M., Schmidt, E., Pratasouskaya, A., Wang, D., Sullivan, R., Bartlett, C., Weadge, J.T., Van der Kamp, M.W., Moreno-Hagelsieb, G., Suits, M.D. and Horsman, G.P. The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis. Nat. Commun. 10:3698 (2019). [DOI] [PMID: 31420548]
[EC 2.7.7.107 created 2021]
 
 
EC 2.7.8.2     
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, PDB, CAS registry number: 9026-13-5
References:
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 2.7.8.2 created 1961, modified 1986 (EC 2.7.8.16 created 1983, incorporated 1986)]
 
 
EC 2.7.8.3     
Accepted name: ceramide cholinephosphotransferase
Reaction: CDP-choline + a ceramide = CMP + sphingomyelin
Glossary: a ceramide = an N-acylsphingosine
Other name(s): phosphorylcholine-ceramide transferase
Systematic name: CDP-choline:N-acylsphingosine cholinephosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-14-6
References:
1.  Kennedy, E.P. Phosphorylcholine-glyceride transferase. Methods Enzymol. 5 (1962) 484–486.
2.  Sribney, M. and Kennedy, E.P. The enzymatic synthesis of sphingomyelin. J. Biol. Chem. 233 (1958) 1315–1322. [PMID: 13610834]
[EC 2.7.8.3 created 1965]
 
 
EC 2.7.8.10     
Accepted name: sphingosine cholinephosphotransferase
Reaction: CDP-choline + sphingosine = CMP + sphingosyl-phosphocholine
Other name(s): CDP-choline-sphingosine cholinephosphotransferase; phosphorylcholine-sphingosine transferase; cytidine diphosphocholine-sphingosine cholinephosphotransferase; sphingosine choline phosphotransferase
Systematic name: CDP-choline:sphingosine cholinephosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9027-12-7
References:
1.  Fujino, Y., Nigishi, T. and Ito, S. Enzymic synthesis of sphingosylphosphorylcholine. Biochem. J. 109 (1968) 310–311. [PMID: 5679375]
[EC 2.7.8.10 created 1972, modified 1976]
 
 
EC 2.7.8.16      
Deleted entry:  1-alkyl-2-acetylglycerol choline phosphotransferase. Now included with EC 2.7.8.2 diacylglycerol cholinephosphotransferase
[EC 2.7.8.16 created 1983, deleted 1986]
 
 
EC 2.7.8.22     
Accepted name: 1-alkenyl-2-acylglycerol choline phosphotransferase
Reaction: CDP-choline + 1-alkenyl-2-acylglycerol = CMP + plasmenylcholine
Other name(s): CDP-choline-1-alkenyl-2-acyl-glycerol phosphocholinetransferase
Systematic name: CDP-choline:1-alkenyl-2-acylglycerol cholinephosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 113066-36-7
References:
1.  Wientzek, M., Man, R.Y.K. and Choy, P.C. Choline glycerophospholipid biosynthesis in the guinea pig heart. Biochem. Cell. Biol. 65 (1987) 860–868. [PMID: 3447597]
[EC 2.7.8.22 created 1990]
 
 
EC 2.7.8.24     
Accepted name: phosphatidylcholine synthase
Reaction: CDP-diacylglycerol + choline = CMP + phosphatidylcholine
Other name(s): CDP-diglyceride-choline O-phosphatidyltransferase
Systematic name: CDP-diacylglycerol:choline O-phosphatidyltransferase
Comments: Requires divalent cations, with Mn2+ being more effective than Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 243666-86-6
References:
1.  de Rudder, K.E.E., Sohlenkamp, C. and Geiger, O. Plant-exudated choline is used for rhizobial membrane lipid biosynthesis by phosphatidylcholine synthase. J. Biol. Chem. 274 (1999) 20011–20016. [DOI] [PMID: 10391951]
2.  Sohlenkamp, C., de Rudder, K.E.E., Röhrs, V., López-Lara, I.M. and Geiger, O. Cloning and characterization of the gene for phosphatidylcholine synthase. J. Biol. Chem. 275 (2000) 18919–18925. [DOI] [PMID: 10858449]
[EC 2.7.8.24 created 2001]
 
 
EC 2.7.8.27     
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 2.7.8.3, 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
References:
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 2.7.8.27 created 2006]
 
 
EC 2.8.2.6     
Accepted name: choline sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + choline = adenosine 3′,5′-bisphosphate + choline sulfate
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): choline sulphokinase; 3′-phosphoadenylyl-sulfate:choline sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:choline sulfonotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9047-23-8
References:
1.  Orsi, B.A. and Spencer, B. Choline sulphokinase (sulphotransferase). J. Biochem. (Tokyo) 56 (1964) 81–91. [PMID: 14202240]
[EC 2.8.2.6 created 1972]
 
 
EC 2.8.2.21     
Accepted name: keratan sulfotransferase
Reaction: 3′-phosphoadenylyl sulfate + keratan = adenosine 3′,5′-bisphosphate + keratan 6′-sulfate
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): 3′-phosphoadenylyl keratan sulfotransferase; keratan sulfate sulfotransferase; 3′-phosphoadenylylsulfate:keratan sulfotransferase; 3′-phosphoadenylyl-sulfate:keratan 6′-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:keratan 6′-sulfonotransferase
Comments: Sulfation takes place at the 6-position of galactosyl and N-acetylglucosaminyl residues in keratan, a proteoglycan. Not identical with EC 2.8.2.5 (chondroitin 4-sulfotransferase), EC 2.8.2.6 (choline sulfotransferase) or EC 2.8.2.17 (chondroitin 6-sulfotransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62168-79-0
References:
1.  Ruter, E.-R. and Kresse, H. Partial purification and characterization of 3′-phosphoadenylylsulfate:keratan sulfate sulfotransferases. J. Biol. Chem. 259 (1984) 11771–11776. [PMID: 6592165]
[EC 2.8.2.21 created 1989]
 
 
EC 3.1.1.4     
Accepted name: phospholipase A2
Reaction: phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Other name(s): lecithinase A; phosphatidase; phosphatidolipase; phospholipase A
Systematic name: phosphatidylcholine 2-acylhydrolase
Comments: Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position. Requires Ca2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-84-7
References:
1.  Doery, H.M. and Pearson, J.E. Haemolysins in venoms of Australian snakes. Observations on the haemolysins of the venoms of some Australian snakes and the separation of phospholipase A from the venom of Pseudechis porphyriacus. Biochem. J. 78 (1961) 820–827. [PMID: 13723433]
2.  Fraenkel-Conrat, H. and Fraenkel-Conrat, J. Inactivation of crotoxin by group-specific reagents. Biochim. Biophys. Acta 5 (1950) 98–104. [DOI] [PMID: 15433984]
3.  Hanahan, D.J., Brockerhoff, H. and Barron, E.J. The site of attack of phospholipase (lecithinase) A on lecithin: a re-evaluation. Position of fatty acids on lecithins and triglycerides. J. Biol. Chem. 235 (1960) 1917–1923. [PMID: 14399412]
4.  Moore, J.H. and Williams, D.L. Some observations on the specificity of phospholipase A. Biochim. Biophys. Acta 84 (1964) 41–54. [PMID: 14124755]
5.  Saito, K. and Hanahan, D.J. A study of the purification and properties of the phospholipase A of Crotalus adamanteus venom. Biochemistry 1 (1962) 521–532. [PMID: 14496116]
6.  van den Bosch, H. Intracellular phospholipases A. Biochim. Biophys. Acta 604 (1980) 191–246. [DOI] [PMID: 6252969]
[EC 3.1.1.4 created 1961, modified 1976, modified 1983]
 
 
EC 3.1.1.5     
Accepted name: lysophospholipase
Reaction: 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
Other name(s): lecithinase B; lysolecithinase; phospholipase B; lysophosphatidase; lecitholipase; phosphatidase B; lysophosphatidylcholine hydrolase; lysophospholipase A1; lysophopholipase L2; lysophospholipase transacylase; neuropathy target esterase; NTE; NTE-LysoPLA; NTE-lysophospholipase
Systematic name: 2-lysophosphatidylcholine acylhydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-85-8
References:
1.  Abe, M., Ohno, K. and Sato, R. Possible identity of lysolecithin acyl-hydrolase with lysolecithin-lysolecithin acyl-transferase in rat-lung soluble fraction. Biochim. Biophys. Acta 369 (1974) 361–370.
2.  Contardi, A. and Ercoli, A. The enzymic cleavage of lecithin and lysolecithin. Biochem. Z. 261 (1933) 275–302.
3.  Dawson, R.M.C. Studies on the hydrolysis of lecithin by Penicillium notatum phospholipase B preparation. Biochem. J. 70 (1958) 559–570. [PMID: 13607409]
4.  Fairbairn, D. The preparation and properties of a lysophospholipase from Penicillium notatum. J. Biol. Chem. 173 (1948) 705–714. [PMID: 18910725]
5.  Shapiro, B. Purification and properties of a lysolecithinase from pancreas. Biochem. J. 53 (1953) 663–666. [PMID: 13032127]
6.  van den Bosch, H., Aarsman, A.J., De Jong, J.G.N. and van Deenen, L.L.M. Studies on lysophospholipases. I. Purification and some properties of a lysophospholipase from beef pancreas. Biochim. Biophys. Acta 296 (1973) 94–104. [DOI] [PMID: 4693514]
7.  van den Bosch, H., Vianen, G.M. and van Heusden, G.P.H. Lysophospholipase-transacylase from rat lung. Methods Enzymol. 71 (1981) 513–521. [PMID: 7278668]
8.  van Tienhoven, M., Atkins, J., Li, Y. and Glynn, P. Human neuropathy target esterase catalyzes hydrolysis of membrane lipids. J. Biol. Chem. 277 (2002) 20942–20948. [DOI] [PMID: 11927584]
9.  Quistad, G.B., Barlow, C., Winrow, C.J., Sparks, S.E. and Casida, J.E. Evidence that mouse brain neuropathy target esterase is a lysophospholipase. Proc. Natl. Acad. Sci. USA 100 (2003) 7983–7987. [DOI] [PMID: 12805562]
10.  Lush, M.J., Li, Y., Read, D.J., Willis, A.C. and Glynn, P. Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from bacteria to man. Biochem. J. 332 (1998) 1–4. [PMID: 9576844]
11.  Winrow, C.J., Hemming, M.L., Allen, D.M., Quistad, G.B., Casida, J.E. and Barlow, C. Loss of neuropathy target esterase in mice links organophosphate exposure to hyperactivity. Nat. Genet. 33 (2003) 477–485. [DOI] [PMID: 12640454]
[EC 3.1.1.5 created 1961, modified 1976, modified 1983]
 
 
EC 3.1.1.7     
Accepted name: acetylcholinesterase
Reaction: acetylcholine + H2O = choline + acetate
Other name(s): true cholinesterase; choline esterase I; cholinesterase; acetylthiocholinesterase; acetylcholine hydrolase; acetyl.β-methylcholinesterase; AcCholE
Systematic name: acetylcholine acetylhydrolase
Comments: Acts on a variety of acetic esters; also catalyses transacetylations.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9000-81-1
References:
1.  Augustinsson, K.-B. Cholinesterases. A study in comparative enzymology. Acta Physiol. Scand. 15, Suppl. 2 (1948) .
2.  Bergmann, F., Rimon, S. and Segal, R. Effect of pH on the activity of eel esterase towards different substrates. Biochem. J. 68 (1958) 493–499. [PMID: 13522650]
3.  Cilliv, G. and Ozand, P.T. Human erythrocyte acetylcholinesterase purification, properties and kinetic behavior. Biochim. Biophys. Acta 284 (1972) 136–156. [DOI] [PMID: 5073758]
4.  Leuzinger, W., Baker, A.L. and Cauvin, E. Acetylcholinesterase. II. Crystallization, absorption spectra, isoionic point. Proc. Natl. Acad. Sci. USA 59 (1968) 620–623. [DOI] [PMID: 5238989]
5.  Nachmansohn, D. and Wilson, I.B. The enzymic hydrolysis and synthesis of acetylcholine. Adv. Enzymol. Relat. Subj. Biochem. 12 (1951) 259–339. [PMID: 14885021]
6.  Zittle, C.A., DellaMonica, E.S., Custer, J.H. and Krikorian, R. Purification of human red cell acetylcholinesterase by electrophoresis, ultracentrifugation and gradient extraction. Arch. Biochem. Biophys. 56 (1955) 469–475. [DOI] [PMID: 14377597]
[EC 3.1.1.7 created 1961]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald