EC |
1.1.1.101 |
Accepted name: |
acylglycerone-phosphate reductase |
Reaction: |
1-palmitoylglycerol 3-phosphate + NADP+ = palmitoylglycerone phosphate + NADPH + H+ |
Other name(s): |
palmitoyldihydroxyacetone-phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase; palmitoyl-dihydroxyacetone-phosphate reductase; acyldihydroxyacetone phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase |
Systematic name: |
1-palmitoylglycerol-3-phosphate:NADP+ oxidoreductase |
Comments: |
Also acts on alkylglycerone 3-phosphate and alkylglycerol 3-phosphate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-35-4 |
References: |
1. |
LaBelle, E.F., Jr. and Hajira, A.K. Enzymatic reduction of alkyl and acyl derivatives of dihydroxyacetone phosphate by reduced pyridine nucleotides. J. Biol. Chem. 247 (1972) 5825–5834. [PMID: 4403490] |
|
[EC 1.1.1.101 created 1972, modified 1976] |
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|
EC |
1.1.1.330 |
Accepted name: |
very-long-chain 3-oxoacyl-CoA reductase |
Reaction: |
a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP+ = a very-long-chain 3-oxoacyl-CoA + NADPH + H+ |
Glossary: |
a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms. |
Other name(s): |
very-long-chain 3-ketoacyl-CoA reductase; very-long-chain β-ketoacyl-CoA reductase; KCR (gene name); IFA38 (gene name) |
Systematic name: |
(3R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase |
Comments: |
The second component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. The enzyme is active with substrates with chain length of C16 to C34, depending on the species. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Beaudoin, F., Gable, K., Sayanova, O., Dunn, T. and Napier, J.A. A Saccharomyces cerevisiae gene required for heterologous fatty acid elongase activity encodes a microsomal β-keto-reductase. J. Biol. Chem. 277 (2002) 11481–11488. [DOI] [PMID: 11792704] |
2. |
Han, G., Gable, K., Kohlwein, S.D., Beaudoin, F., Napier, J.A. and Dunn, T.M. The Saccharomyces cerevisiae YBR159w gene encodes the 3-ketoreductase of the microsomal fatty acid elongase. J. Biol. Chem. 277 (2002) 35440–35449. [DOI] [PMID: 12087109] |
3. |
Beaudoin, F., Wu, X., Li, F., Haslam, R.P., Markham, J.E., Zheng, H., Napier, J.A. and Kunst, L. Functional characterization of the Arabidopsis β-ketoacyl-coenzyme A reductase candidates of the fatty acid elongase. Plant Physiol. 150 (2009) 1174–1191. [DOI] [PMID: 19439572] |
|
[EC 1.1.1.330 created 2012] |
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|
|
|
EC |
1.3.1.93 |
Accepted name: |
very-long-chain enoyl-CoA reductase |
Reaction: |
a very-long-chain acyl-CoA + NADP+ = a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+ |
Glossary: |
a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms. |
Other name(s): |
TSC13 (gene name); CER10 (gene name) |
Systematic name: |
very-long-chain acyl-CoA:NADP+ oxidoreductase |
Comments: |
This is the fourth component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kohlwein, S.D., Eder, S., Oh, C.S., Martin, C.E., Gable, K., Bacikova, D. and Dunn, T. Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae. Mol. Cell Biol. 21 (2001) 109–125. [DOI] [PMID: 11113186] |
2. |
Gable, K., Garton, S., Napier, J.A. and Dunn, T.M. Functional characterization of the Arabidopsis thaliana orthologue of Tsc13p, the enoyl reductase of the yeast microsomal fatty acid elongating system. J. Exp. Bot. 55 (2004) 543–545. [DOI] [PMID: 14673020] |
3. |
Kvam, E., Gable, K., Dunn, T.M. and Goldfarb, D.S. Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles. Mol. Biol. Cell 16 (2005) 3987–3998. [DOI] [PMID: 15958487] |
4. |
Zheng, H., Rowland, O. and Kunst, L. Disruptions of the Arabidopsis enoyl-CoA reductase gene reveal an essential role for very-long-chain fatty acid synthesis in cell expansion during plant morphogenesis. Plant Cell 17 (2005) 1467–1481. [DOI] [PMID: 15829606] |
|
[EC 1.3.1.93 created 2012] |
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|
EC |
1.3.8.8 |
Accepted name: |
long-chain acyl-CoA dehydrogenase |
Reaction: |
a long-chain acyl-CoA + electron-transfer flavoprotein = a long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein |
Glossary: |
a long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 13 to 22 carbon atoms. |
Other name(s): |
palmitoyl-CoA dehydrogenase; palmitoyl-coenzyme A dehydrogenase; long-chain acyl-coenzyme A dehydrogenase; long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase; ACADL (gene name). |
Systematic name: |
long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase |
Comments: |
Contains a tightly-bound FAD cofactor. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms. The highest activity was found with C12, and the rates with C8 and C16 were 80 and 70%, respectively [2]. The enzyme from rat can accept substrates with C8-C22. It is most active with C14 and C16, and has no activity with C4, C6 or C24 [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 59536-74-2 |
References: |
1. |
Crane, F.L., Hauge, J.G. and Beinert, H. Flavoproteins involved in the first oxidative step of the fatty acid cycle. Biochim. Biophys. Acta 17 (1955) 292–294. [DOI] [PMID: 13239683] |
2. |
Hauge, J.G., Crane, F.L. and Beinert, H. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. Palmityl CoA dehydrogenase. J. Biol. Chem. 219 (1956) 727–733. [PMID: 13319294] |
3. |
Hall, C.L., Heijkenkjold, L., Bartfai, T., Ernster, L. and Kamin, H. Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef heart mitochondria. Arch. Biochem. Biophys. 177 (1976) 402–414. [DOI] [PMID: 1015826] |
4. |
Ikeda, Y., Ikeda, K.O. and Tanaka, K. Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260 (1985) 1311–1325. [PMID: 3968063] |
5. |
Djordjevic, S., Dong, Y., Paschke, R., Frerman, F.E., Strauss, A.W. and Kim, J.J. Identification of the catalytic base in long chain acyl-CoA dehydrogenase. Biochemistry 33 (1994) 4258–4264. [PMID: 8155643] |
|
[EC 1.3.8.8 created 1989 as EC 1.3.99.13, part transferred 2012 to EC 1.3.8.8] |
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|
|
|
EC |
1.3.8.9 |
Accepted name: |
very-long-chain acyl-CoA dehydrogenase |
Reaction: |
a very-long-chain acyl-CoA + electron-transfer flavoprotein = a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein |
Glossary: |
a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms. |
Other name(s): |
ACADVL (gene name). |
Systematic name: |
very-long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase |
Comments: |
Contains a tightly-bound FAD cofactor. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme is most active toward long-chain acyl-CoAs such as C14, C16 and C18, but is also active with very-long-chain acyl-CoAs up to 24 carbons. It shows no activity for substrates of less than 12 carbons. Its specific activity towards palmitoyl-CoA is more than 10-fold that of the long-chain acyl-CoA dehydrogenase [1]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.8, long-chain acyl-CoA dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Izai, K., Uchida, Y., Orii, T., Yamamoto, S. and Hashimoto, T. Novel fatty acid β-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase. J. Biol. Chem. 267 (1992) 1027–1033. [PMID: 1730632] |
2. |
Aoyama, T., Souri, M., Ushikubo, S., Kamijo, T., Yamaguchi, S., Kelley, R.I., Rhead, W.J., Uetake, K., Tanaka, K. and Hashimoto, T. Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients. J. Clin. Invest. 95 (1995) 2465–2473. [DOI] [PMID: 7769092] |
3. |
McAndrew, R.P., Wang, Y., Mohsen, A.W., He, M., Vockley, J. and Kim, J.J. Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. J. Biol. Chem. 283 (2008) 9435–9443. [DOI] [PMID: 18227065] |
|
[EC 1.3.8.9 created 1961 as EC 1.3.2.2, transferred 1964 to EC 1.3.99.3, part transferred 2012 to EC 1.3.8.9] |
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|
EC
|
1.3.99.13
|
Transferred entry: | long-chain-acyl-CoA dehydrogenase. Now EC 1.3.8.8, long-chain-acyl-CoA dehydrogenase
|
[EC 1.3.99.13 created 1989, deleted 2012] |
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|
EC |
1.14.14.46 |
Accepted name: |
pimeloyl-[acyl-carrier protein] synthase |
Reaction: |
a long-chain acyl-[acyl-carrier protein] + 2 reduced flavodoxin + 3 O2 = pimeloyl-[acyl-carrier protein] + an n-alkanal + 2 oxidized flavodoxin + 3 H2O (overall reaction) (1a) a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O (1b) a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O (1c) a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a 7-oxoheptanoyl-[acyl-carrier protein] + an n-alkanal + oxidized flavodoxin + 2 H2O (1d) a 7-oxoheptanoyl-[acyl-carrier protein] + oxidized flavodoxin + H2O = a pimeloyl-[acyl-carrier protein] + reduced flavodoxin + H+ |
Glossary: |
a long-chain acyl-[acyl-carrier protein] = an acyl-[acyl-carrier protein] thioester where the acyl chain contains 13 to 22 carbon atoms.
palmitoyl-[acyl-carrier protein] = hexadecanoyl-[acyl-carrier protein]
pimeloyl-[acyl-carrier protein] = 6-carboxyhexanoyl-[acyl-carrier protein] |
Other name(s): |
bioI (gene name); P450BioI; CYP107H1 |
Systematic name: |
acyl-[acyl-carrier protein],reduced-flavodoxin:oxygen oxidoreductase (pimeloyl-[acyl-carrier protein]-forming) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein. The enzyme catalyses an oxidative C-C bond cleavage of long-chain acyl-[acyl-carrier protein]s of various lengths to generate pimeloyl-[acyl-carrier protein], an intermediate in the biosynthesis of biotin. The preferred substrate of the enzyme from the bacterium Bacillus subtilis is palmitoyl-[acyl-carrier protein] which then gives heptanal as the alkanal. The mechanism is similar to EC 1.14.15.6, cholesterol monooxygenase (side-chain-cleaving), followed by a hydroxylation step, which may occur spontaneously [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Stok, J.E. and De Voss, J. Expression, purification, and characterization of BioI: a carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis. Arch. Biochem. Biophys. 384 (2000) 351–360. [DOI] [PMID: 11368323] |
2. |
Cryle, M.J. and De Voss, J.J. Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1). Chem. Commun. (Camb.) (2004) 86–87. [DOI] [PMID: 14737344] |
3. |
Cryle, M.J. and Schlichting, I. Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex. Proc. Natl. Acad. Sci. USA 105 (2008) 15696–15701. [DOI] [PMID: 18838690] |
4. |
Cryle, M.J. Selectivity in a barren landscape: the P450(BioI)-ACP complex. Biochem. Soc. Trans. 38 (2010) 934–939. [DOI] [PMID: 20658980] |
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[EC 1.14.14.46 created 2013 as EC 1.14.15.12, transferred 2017 to EC 1.14.14.46] |
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|
EC
|
1.14.15.12
|
Transferred entry: | pimeloyl-[acyl-carrier protein] synthase. Now EC 1.14.14.46, pimeloyl-[acyl-carrier protein] synthase
|
[EC 1.14.15.12 created 2013, deleted 2017] |
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|
|
EC |
1.14.19.2 |
Accepted name: |
stearoyl-[acyl-carrier-protein] 9-desaturase |
Reaction: |
stearoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = oleoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
Other name(s): |
stearyl acyl carrier protein desaturase; stearyl-ACP desaturase; acyl-[acyl-carrier-protein] desaturase; acyl-[acyl-carrier protein],hydrogen-donor:oxygen oxidoreductase |
Systematic name: |
stearoyl-[acyl-carrier protein],reduced ferredoxin:oxygen oxidoreductase (9,10 cis-dehydrogenating) |
Comments: |
The enzyme is found in the lumen of plastids, where de novo biosynthesis of fatty acids occurs, and acts on freshly synthesized saturated fatty acids that are still linked to acyl-carrier protein. The enzyme determines the position of the double bond by its distance from the carboxylic acid end of the fatty acid. It also acts on palmitoyl-[acyl-carrier-protein] [4,5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-86-3 |
References: |
1. |
Jaworski, J.G. and Stumpf, P.K. Fat metabolism in higher plants. Properties of a soluble stearyl-acyl carrier protein desaturase from maturing Carthamus tinctorius. Arch. Biochem. Biophys. 162 (1974) 158–165. [DOI] [PMID: 4831331] |
2. |
Nagai, J. and Bloch, K. Enzymatic desaturation of stearyl acyl carrier protein. J. Biol. Chem. 243 (1968) 4626–4633. [PMID: 4300868] |
3. |
Shanklin, J. and Somerville, C. Stearoyl-acyl-carrier-protein desaturase from higher plants is structurally unrelated to the animal and fungal homologs. Proc. Natl. Acad. Sci. USA 88 (1991) 2510–2514. [DOI] [PMID: 2006187] |
4. |
Cahoon, E.B., Lindqvist, Y., Schneider, G. and Shanklin, J. Redesign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position. Proc. Natl. Acad. Sci. USA 94 (1997) 4872–4877. [DOI] [PMID: 9144157] |
5. |
Cao, Y., Xian, M., Yang, J., Xu, X., Liu, W. and Li, L. Heterologous expression of stearoyl-acyl carrier protein desaturase (S-ACP-DES) from Arabidopsis thaliana in Escherichia coli. Protein Expr. Purif. 69 (2010) 209–214. [DOI] [PMID: 19716420] |
|
[EC 1.14.19.2 created 1972 as EC 1.14.99.6, modified 2000, transferred 2000 to EC 1.14.19.2, modified 2015] |
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|
EC |
1.14.19.3 |
Accepted name: |
acyl-CoA 6-desaturase |
Reaction: |
(1) linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = γ-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O (2) α-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
Other name(s): |
Δ6-desaturase; Δ6-fatty acyl-CoA desaturase; Δ6-acyl CoA desaturase; fatty acid Δ6-desaturase; fatty acid 6-desaturase; linoleate desaturase; linoleic desaturase; linoleic acid desaturase; linoleoyl CoA desaturase; linoleoyl-coenzyme A desaturase; long-chain fatty acid Δ6-desaturase; linoleoyl-CoA,hydrogen-donor:oxygen oxidoreductase; linoleoyl-CoA desaturase; FADS2 (gene name) |
Systematic name: |
acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (6,7 cis-dehydrogenating) |
Comments: |
An iron protein. The enzyme introduces a cis double bond at carbon 6 of acyl-CoAs. It is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid. The human enzyme has a broad substrate range. It also acts on palmitoyl-CoA, generating sapienoyl-CoA [4], and on (9Z,12Z,15Z,18Z,21Z)-tetracosa-9,12,15,18,21-pentaenoyl-CoA, converting it to (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoyl-CoA as part of a pathway that produces docosahexaenoate [3]. The enzyme contains a cytochrome b5 domain that is assumed to act in vivo as the electron donor to the active site of the desaturase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9082-66-0 |
References: |
1. |
Okayasu, T., Nagao, M., Ishibashi, T. and Imai, Y. Purification and partial characterization of linoleoyl-CoA desaturase from rat liver microsomes. Arch. Biochem. Biophys. 206 (1981) 21–28. [DOI] [PMID: 7212717] |
2. |
Cho, H.P., Nakamura, M.T. and Clarke, S.D. Cloning, expression, and nutritional regulation of the mammalian Δ-6 desaturase. J. Biol. Chem. 274 (1999) 471–477. [DOI] [PMID: 9867867] |
3. |
Sprecher, H. Metabolism of highly unsaturated n-3 and n-6 fatty acids. Biochim. Biophys. Acta 1486 (2000) 219–231. [DOI] [PMID: 10903473] |
4. |
Ge, L., Gordon, J.S., Hsuan, C., Stenn, K. and Prouty, S.M. Identification of the Δ-6 desaturase of human sebaceous glands: expression and enzyme activity. J. Invest. Dermatol. 120 (2003) 707–714. [DOI] [PMID: 12713571] |
5. |
Domergue, F., Abbadi, A., Zähringer, U., Moreau, H. and Heinz, E. In vivo characterization of the first acyl-CoA Δ6-desaturase from a member of the plant kingdom, the microalga Ostreococcus tauri. Biochem. J. 389 (2005) 483–490. [DOI] [PMID: 15769252] |
|
[EC 1.14.19.3 created 1986 as EC 1.14.99.25, transferred 2000 to EC 1.14.19.3, modified 2015] |
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|
|
|
EC |
1.14.19.5 |
Accepted name: |
acyl-CoA 11-(Z)-desaturase |
Reaction: |
an acyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = an (11Z)-enoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
Other name(s): |
Δ11 desaturase; fatty acid Δ11-desaturase; TpDESN; Cro-PG; Δ11 fatty acid desaturase; Z/E11-desaturase; Δ11-palmitoyl-CoA desaturase; acyl-CoA,hydrogen donor:oxygen Δ11-oxidoreductase; Δ11-fatty-acid desaturase |
Systematic name: |
acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (11,12 cis-dehydrogenating) |
Comments: |
The enzyme introduces a cis double bond at position C-11 of saturated fatty acyl-CoAs. In moths the enzyme participates in the biosynthesis of their sex pheromones. The enzyme from the marine microalga Thalassiosira pseudonana is specific for palmitoyl-CoA (16:0) [4], that from the leafroller moth Choristoneura rosaceana desaturates myristoyl-CoA (14:0) [5], while that from the moth Spodoptera littoralis accepts both substrates [1]. The enzyme contains three histidine boxes that are conserved in all desaturases [2]. It is membrane-bound, and contains a cytochrome b5-like domain at the N-terminus that serves as the electron donor for the active site of the desaturase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Martinez, T., Fabrias, G. and Camps, F. Sex pheromone biosynthetic pathway in Spodoptera littoralis and its activation by a neurohormone. J. Biol. Chem. 265 (1990) 1381–1387. [PMID: 2295634] |
2. |
Rodriguez, F., Hallahan, D.L., Pickett, J.A. and Camps, F. Characterization of the Δ11-palmitoyl-CoA-desaturase from Spodoptera littoralis (Lepidoptera:Noctuidae). Insect Biochem. Mol. Biol. 22 (1992) 143–148. |
3. |
Navarro, I., Font, I., Fabrias, G. and Camps, F. Stereospecificity of the (E)- and (Z)-11 myristoyl desaturases in the biosynthesis of Spodoptera littoralis sex pheromone. J. Am. Chem. Soc. 119 (1997) 11335–11336. |
4. |
Tonon, T., Harvey, D., Qing, R., Li, Y., Larson, T.R. and Graham, I.A. Identification of a fatty acid Δ11-desaturase from the microalga Thalassiosira pseudonana. FEBS Lett. 563 (2004) 28–34. [DOI] [PMID: 15063718] |
5. |
Hao, G., O'Connor, M., Liu, W. and Roelofs, W.L. Characterization of Z/E11- and Z9-desaturases from the obliquebanded leafroller moth, Choristoneura rosaceana. J. Insect Sci. 2:26 (2002) 1–7. [PMID: 15455060] |
|
[EC 1.14.19.5 created 2008 (EC 1.14.99.32 created 2000, incorporated 2015), modified 2015] |
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|
|
EC |
1.14.19.11 |
Accepted name: |
acyl-[acyl-carrier-protein] 4-desaturase |
Reaction: |
palmitoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = (4Z)-hexadec-4-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
Other name(s): |
Δ4-palmitoyl-[acyl carrier protein] desaturase |
Systematic name: |
palmitoyl-[acyl-carrier protein],reduced acceptor:oxygen oxidoreductase (4,5 cis-dehydrogenating) |
Comments: |
The enzymes from the plants Coriandrum sativum (coriander) and Hedera helix (English ivy) are involved in biosynthesis of petroselinate [(6Z)-octadec-6-enoate], which is formed by elongation of (4Z)-hexadec-4-enoate. The ivy enzyme can also act on oleoyl-[acyl-carrier protein] and palmitoleoyl-[acyl-carrier protein], generating the corresponding 4,9-diene. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Cahoon, E.B., Shanklin, J. and Ohlrogge, J.B. Expression of a coriander desaturase results in petroselinic acid production in transgenic tobacco. Proc. Natl. Acad. Sci. USA 89 (1992) 11184–11188. [DOI] [PMID: 1454797] |
2. |
Cahoon, E.B. and Ohlrogge, J.B. Metabolic evidence for the involvement of a Δ4-palmitoyl-acyl carrier protein desaturase in petroselinic acid synthesis in coriander endosperm and transgenic tobacco cells. Plant Physiol. 104 (1994) 827–837. [PMID: 12232129] |
3. |
Whittle, E., Cahoon, E.B., Subrahmanyam, S. and Shanklin, J. A multifunctional acyl-acyl carrier protein desaturase from Hedera helix L. (English ivy) can synthesize 16- and 18-carbon monoene and diene products. J. Biol. Chem. 280 (2005) 28169–28176. [DOI] [PMID: 15939740] |
|
[EC 1.14.19.11 created 2015] |
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|
|
|
EC |
1.14.19.26 |
Accepted name: |
acyl-[acyl-carrier-protein] 6-desaturase |
Reaction: |
palmitoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = (6Z)-hexadec-6-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
Glossary: |
(6Z)-hexadec-6-enoyl-[acyl-carrier protein] = Δ6-hexadecenoyl-[acyl-carrier protein] = sapienoyl-[acyl-carrier-protein]
an [acyl-carrier protein] = ACP = [acp] |
Other name(s): |
DELTA6 palmitoyl-ACP desaturase; DELTA6 16:0-ACP desaturase |
Systematic name: |
palmitoyl-[acyl-carrier protein],reduced ferredoxin:oxygen oxidoreductase (6,7 cis-dehydrogenating) |
Comments: |
The enzyme, characterized from the endosperm of the plant Thunbergia alata (black-eyed Susan vine), introduces a cis double bond at carbon 6 of several saturated acyl-[acp]s. It is most active with palmitoyl-[acp] (16:0), but can also act on myristoyl-[acp] (14:0) and stearoyl-[acp] (18:0). The position of the double bond is determined by its distance from the carboxyl end of the fatty acid. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Cahoon, E.B., Cranmer, A.M., Shanklin, J. and Ohlrogge, J.B. Δ6 Hexadecenoic acid is synthesized by the activity of a soluble Δ6 palmitoyl-acyl carrier protein desaturase in Thunbergia alata endosperm. J. Biol. Chem. 269 (1994) 27519–27526. [PMID: 7961667] |
2. |
Cahoon, E.B., Lindqvist, Y., Schneider, G. and Shanklin, J. Redesign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position. Proc. Natl. Acad. Sci. USA 94 (1997) 4872–4877. [DOI] [PMID: 9144157] |
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[EC 1.14.19.26 created 2015] |
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EC |
1.14.19.27 |
Accepted name: |
sn-2 palmitoyl-lipid 9-desaturase |
Reaction: |
a 1-acyl-2-palmitoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a 1-acyl-2-palmitoleoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
Other name(s): |
DesC2 |
Systematic name: |
1-acyl-2-palmitoyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (9,10 cis-dehydrogenating) |
Comments: |
The enzyme, characterized from the cyanobacterium Nostoc sp. 36, introduces a cis double bond at carbon 9 of palmitoyl groups (16:0) attached to the sn-2 position of glycerolipids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Chintalapati, S., Prakash, J.S., Gupta, P., Ohtani, S., Suzuki, I., Sakamoto, T., Murata, N. and Shivaji, S. A novel Δ9 acyl-lipid desaturase, DesC2, from cyanobacteria acts on fatty acids esterified to the sn-2 position of glycerolipids. Biochem. J. 398 (2006) 207–214. [DOI] [PMID: 16689682] |
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[EC 1.14.19.27 created 2015] |
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EC |
1.14.19.32 |
Accepted name: |
palmitoyl-CoA 14-(E/Z)-desaturase |
Reaction: |
(1) palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = (14E)-hexadec-14-enoyl-CoA + 2 ferricytochrome b5 + 2 H2O (2) palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = (14Z)-hexadec-14-enoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
Systematic name: |
palmitoyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (14,15 cis/trans-dehydrogenating) |
Comments: |
The enzyme, found in the moth Ostrinia furnacalis (Asian corn borer), produces a mixture of (E)- and (Z)- isomers. The products are subsequently truncated by partial β-oxidation to a blend of 12(E/Z)-tetradec-12-enoyl-CoA, which are converted to the species-specific sex pheromones (E)- and (Z)-tetradec-12-enoyl acetates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Roelofs, W.L., Liu, W., Hao, G., Jiao, H., Rooney, A.P. and Linn, C.E., Jr. Evolution of moth sex pheromones via ancestral genes. Proc. Natl. Acad. Sci. USA 99 (2002) 13621–13626. [DOI] [PMID: 12237399] |
2. |
Xue, B., Rooney, A.P., Kajikawa, M., Okada, N. and Roelofs, W.L. Novel sex pheromone desaturases in the genomes of corn borers generated through gene duplication and retroposon fusion. Proc. Natl. Acad. Sci. USA 104 (2007) 4467–4472. [DOI] [PMID: 17360547] |
3. |
Sakai, R., Fukuzawa, M., Nakano, R., Tatsuki, S. and Ishikawa, Y. Alternative suppression of transcription from two desaturase genes is the key for species-specific sex pheromone biosynthesis in two Ostrinia moths. Insect Biochem. Mol. Biol. 39 (2009) 62–67. [DOI] [PMID: 18992816] |
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[EC 1.14.19.32 created 2015] |
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EC |
1.14.19.37 |
Accepted name: |
acyl-CoA 5-desaturase |
Reaction: |
(1) (11Z,14Z)-icosa-11,14-dienoyl-CoA + reduced acceptor + O2 = (5Z,11Z,14Z)-icosa-5,11,14-trienoyl-CoA + acceptor + 2 H2O (2) (11Z,14Z,17Z)-icosa-11,14,17-trienoyl-CoA + reduced acceptor + O2 = (5Z,11Z,14Z,17Z)-icosa-5,11,14,17-tetraenoyl-CoA + acceptor + 2 H2O |
Glossary: |
(5Z,11Z,14Z)-icosa-5,11,14-trienoate = sciadonate
(5Z,11Z,14Z,17Z)-icosa-5,11,14,17-tetraenoate = juniperonate
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Other name(s): |
acyl-CoA 5-desaturase (non-methylene-interrupted) |
Systematic name: |
acyl-CoA,acceptor:oxygen oxidoreductase (5,6 cis-dehydrogenating) |
Comments: |
The enzyme, characterized from the plant Anemone leveillei, introduces a cis double bond at carbon 5 of acyl-CoAs that do not contain a double bond at position 8. In vivo it forms non-methylene-interrupted polyunsaturated fatty acids such as sciadonate and juniperonate. When expressed in Arabidopsis thaliana the enzyme could also act on unsaturated substrates such as palmitoyl-CoA. cf. EC 1.14.19.44, acyl-CoA (8-3)-desaturase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Sayanova, O., Haslam, R., Venegas Caleron, M. and Napier, J.A. Cloning and characterization of unusual fatty acid desaturases from Anemone leveillei: identification of an acyl-coenzyme A C20 Δ5-desaturase responsible for the synthesis of sciadonic acid. Plant Physiol. 144 (2007) 455–467. [DOI] [PMID: 17384161] |
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[EC 1.14.19.37 created 2015] |
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EC |
1.14.19.42 |
Accepted name: |
palmitoyl-[glycerolipid] 7-desaturase |
Reaction: |
a 1-acyl-2-palmitoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a 1-acyl-2-[(7Z)-hexadec-7-enoyl]-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
Other name(s): |
FAD5 |
Systematic name: |
1-acyl-2-palmitoyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (7,8-cis-dehydrogenating) |
Comments: |
The enzyme introduces a cis double bond at carbon 7 of a palmitoyl group attached to the sn-2 position of glycerolipids. The enzyme from the plant Arabidopsis thaliana is specific for palmitate in monogalactosyldiacylglycerol. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kunst, L., Browse, J., Somerville, C.R. A mutant of Arabidopsis deficient in desaturation of palmitic acid in leaf lipids. Plant Physiol. 90 (1989) 943–947. [PMID: 16666902] |
2. |
Heilmann, I., Mekhedov, S., King, B., Browse, J. and Shanklin, J. Identification of the Arabidopsis palmitoyl-monogalactosyldiacylglycerol Δ7-desaturase gene FAD5, and effects of plastidial retargeting of Arabidopsis desaturases on the fad5 mutant phenotype. Plant Physiol. 136 (2004) 4237–4245. [DOI] [PMID: 15579662] |
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[EC 1.14.19.42 created 2015] |
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EC |
1.14.19.43 |
Accepted name: |
palmitoyl-[glycerolipid] 3-(E)-desaturase |
Reaction: |
a 1-acyl-2-palmitoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a 1-acyl-2-[(3E)-hexadec-3-enoyl]-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
Other name(s): |
FAD4 |
Systematic name: |
1-acyl-2-palmitoyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (3,4-trans -dehydrogenating) |
Comments: |
The enzyme introduces an unusual trans double bond at carbon 3 of a palmitoyl group attached to the sn-2 position of glycerolipids. The enzyme from the plant Arabidopsis thaliana is specific for palmitate in phosphatidylglycerol. The enzyme from tobacco can also accept oleate and α-linolenate if present at the sn-2 position of phosphatidylglycerol [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Fritz, M., Lokstein, H., Hackenberg, D., Welti, R., Roth, M., Zähringer, U., Fulda, M., Hellmeyer, W., Ott, C., Wolter, F.P. and Heinz, E. Channeling of eukaryotic diacylglycerol into the biosynthesis of plastidial phosphatidylglycerol. J. Biol. Chem. 282 (2007) 4613–4625. [DOI] [PMID: 17158889] |
2. |
Gao, J., Ajjawi, I., Manoli, A., Sawin, A., Xu, C., Froehlich, J.E., Last, R.L. and Benning, C. FATTY ACID DESATURASE4 of Arabidopsis encodes a protein distinct from characterized fatty acid desaturases. Plant J. 60 (2009) 832–839. [DOI] [PMID: 19682287] |
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[EC 1.14.19.43 created 2015] |
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EC |
2.3.1.7 |
Accepted name: |
carnitine O-acetyltransferase |
Reaction: |
acetyl-CoA + carnitine = CoA + O-acetylcarnitine |
Other name(s): |
acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC |
Systematic name: |
acetyl-CoA:carnitine O-acetyltransferase |
Comments: |
Also acts on propanoyl-CoA and butanoyl-CoA (cf. EC 2.3.1.21 carnitine O-palmitoyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9029-90-7 |
References: |
1. |
Chase, J.F.A., Pearson, D.J. and Tubbs, P.K. The preparation of crystalline carnitine acetyltransferase. Biochim. Biophys. Acta 96 (1965) 162–165. [DOI] [PMID: 14285260] |
2. |
Friedman, S. and Fraenkel, G. Reversible enzymatic acetylation of carnitine. Arch. Biochem. Biophys. 59 (1955) 491–501. [DOI] [PMID: 13275966] |
3. |
Miyazawa, S., Ozasa, H., Furuta, S., Osumi, T. and Hashimoto, T. Purification and properties of carnitine acetyl transferase from rat liver. J. Biochem. (Tokyo) 93 (1983) 439–451. [PMID: 6404901] |
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[EC 2.3.1.7 created 1961] |
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EC |
2.3.1.20 |
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, PDB, CAS registry number: 9029-98-5 |
References: |
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] |
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[EC 2.3.1.20 created 1965] |
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EC |
2.3.1.21 |
Accepted name: |
carnitine O-palmitoyltransferase |
Reaction: |
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine |
Other name(s): |
CPT (ambiguous); CPTo; outer malonyl-CoA inhibitable carnitine palmitoyltransferase; CPTi; CPT I (outer membrane carnitine palmitoyl transferase); carnitine palmitoyltransferase I; carnitine palmitoyltransferase II; CPT-A; CPT-B; acylcarnitine transferase; carnitine palmitoyltransferase; carnitine palmitoyltransferase-A; L-carnitine palmitoyltransferase; palmitoylcarnitine transferase |
Systematic name: |
palmitoyl-CoA:L-carnitine O-palmitoyltransferase |
Comments: |
Broad specificity to acyl group, over the range C8 to C18; optimal activity with palmitoyl-CoA. cf. EC 2.3.1.7 carnitine O-acetyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9068-41-1 |
References: |
1. |
Derrick, J.P., Tubbs, P.K. and Ramsay, R.R. Purification and properties of an easily solubilized L-carnitine palmitoyltransferase from beef-liver mitochondria. Biochem. Soc. Trans. 14 (1986) 698. |
2. |
Healy, M.J., Kerner, J. and Bieber, L.L. Enzymes of carnitine acylation. Is overt carnitine palmitoyltransferase of liver peroxisomal carnitine octanoyltransferase? Biochem. J. 249 (1988) 231–237. [PMID: 3342008] |
3. |
Miyazawa, S., Ozasa, H., Osumi, T. and Hashimoto, T. Purification and properties of carnitine octanoyltransferase and carnitine palmitoyltransferase from rat liver. J. Biochem. (Tokyo) 94 (1983) 529–542. [PMID: 6630173] |
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[EC 2.3.1.21 created 1972] |
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EC |
2.3.1.22 |
Accepted name: |
2-acylglycerol O-acyltransferase |
Reaction: |
acyl-CoA + 2-acylglycerol = CoA + diacylglycerol |
Other name(s): |
acylglycerol palmitoyltransferase; monoglyceride acyltransferase; acyl coenzyme A-monoglyceride acyltransferase; monoacylglycerol acyltransferase |
Systematic name: |
acyl-CoA:2-acylglycerol O-acyltransferase |
Comments: |
Various 2-acylglycerols can act as acceptor; palmitoyl-CoA and other long-chain acyl-CoAs can act as donors. The sn-1 position and the sn-3 position are both acylated, at about the same rate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9055-17-8 |
References: |
1. |
Manganaro, F. and Kuksis, A. Purification and preliminary characterization of 2-monoacylglycerol acyltransferase from rat intestinal villus cells. Can. J. Biochem. Cell Biol. 63 (1985) 341–347. [DOI] [PMID: 4016575] |
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[EC 2.3.1.22 created 1972, modified 1986, modified 1989] |
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EC |
2.3.1.42 |
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 |
References: |
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] |
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[EC 2.3.1.42 created 1972] |
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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] |
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[EC 2.3.1.43 created 1972, modified 1976] |
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EC |
2.3.1.50 |
Accepted name: |
serine C-palmitoyltransferase |
Reaction: |
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 |
Other name(s): |
serine palmitoyltransferase; SPT; 3-oxosphinganine synthetase; acyl-CoA:serine C-2 acyltransferase decarboxylating |
Systematic name: |
palmitoyl-CoA:L-serine C-palmitoyltransferase (decarboxylating) |
Comments: |
A pyridoxal-phosphate protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-50-7 |
References: |
1. |
Brady, R.N., DiMari, S.J. and Snell, E.E. Biosynthesis of sphingolipid bases. 3. Isolation and characterization of ketonic intermediates in the synthesis of sphingosine and dihydrosphingosine by cell-free extracts of Hansenula ciferri. J. Biol. Chem. 244 (1969) 491–496. [PMID: 4388074] |
2. |
Stoffel, W., Le Kim, D. and Sticht, G. Biosynthesis of dihydrosphingosine in vitro. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 664–670. [PMID: 4386961] |
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[EC 2.3.1.50 created 1976, modified 1982] |
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EC |
2.3.1.76 |
Accepted name: |
retinol O-fatty-acyltransferase |
Reaction: |
acyl-CoA + retinol = CoA + retinyl ester |
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For diagram of biosynthesis of retinal and derivatives, click here |
Other name(s): |
retinol acyltransferase; retinol fatty-acyltransferase |
Systematic name: |
acyl-CoA:retinol O-acyltransferase |
Comments: |
Acts on palmitoyl-CoA and other long-chain fatty-acyl derivatives of CoA. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81295-48-9 |
References: |
1. |
Helgerud, P., Petersen, L.B. and Norum, K.R. Retinol esterification by microsomes from the mucosa of human small intestine. Evidence for acyl-Coenzyme A retinol acyltransferase activity. J. Clin. Invest. 71 (1983) 747–753. [DOI] [PMID: 6826734] |
2. |
Ross, A.C. Retinol esterification by rat liver microsomes. Evidence for a fatty acyl coenzyme A: retinol acyltransferase. J. Biol. Chem. 257 (1982) 2453–2459. [PMID: 7061433] |
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[EC 2.3.1.76 created 1984] |
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EC |
2.3.1.77 |
Accepted name: |
triacylglycerol—sterol O-acyltransferase |
Reaction: |
triacylglycerol + a 3β-hydroxysteroid = diacylglycerol + a 3β-hydroxysteroid ester |
Other name(s): |
triacylglycerol:sterol acyltransferase |
Systematic name: |
triacylglycerol:3β-hydroxysteroid O-acyltransferase |
Comments: |
Tripalmitoylglycerol and, more slowly, other triacylglycerols containing C6 to C22 fatty acids, can act as donors. The best acceptors are 3β-hydroxysteroids with a planar ring system. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 80487-96-3 |
References: |
1. |
Zimowski, J. and Wojciechowski, Z.A. Acyl donors for sterol esterification by cell-free preparations from Sinapis alba roots. Phytochemistry 20 (1981) 1799–1803. |
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[EC 2.3.1.77 created 1984] |
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EC |
2.3.1.86 |
Accepted name: |
fatty-acyl-CoA synthase system |
Reaction: |
acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H+ = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+ |
Other name(s): |
yeast fatty acid synthase; FAS1 (gene name); FAS2 (gene name); fatty-acyl-CoA synthase |
Systematic name: |
acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing) |
Comments: |
The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits. One subunit catalyses the reactions EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase and EC 2.3.1.41, β-ketoacyl-[acyl-carrier-protein] synthase I, while the other subunit catalyses the reactions of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, EC 4.2.1.59, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.1.1.279, (R)-3-hydroxyacid-ester dehydrogenase. The enzyme system differs from the animal system (EC 2.3.1.85, fatty-acid synthase system) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 94219-29-1 |
References: |
1. |
Schweitzer, E., Kniep, B., Castorph, H. and Holzner, U. Pantetheine-free mutants of the yeast fatty-acid-synthetase complex. Eur. J. Biochem. 39 (1973) 353–362. [DOI] [PMID: 4590449] |
2. |
Wakil, S.J., Stoops, J.K. and Joshi, V.C. Fatty acid synthesis and its regulation. Annu. Rev. Biochem. 52 (1983) 537–579. [DOI] [PMID: 6137188] |
3. |
Tehlivets, O., Scheuringer, K. and Kohlwein, S.D. Fatty acid synthesis and elongation in yeast. Biochim. Biophys. Acta 1771 (2007) 255–270. [DOI] [PMID: 16950653] |
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[EC 2.3.1.86 created 1984, modified 2003, modified 2013, modified 2019] |
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EC
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2.3.1.96
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Deleted entry: | glycoprotein N-palmitoyltransferase |
[EC 2.3.1.96 created 1989, deleted 2018] |
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EC |
2.3.1.100 |
Accepted name: |
[myelin-proteolipid] O-palmitoyltransferase |
Reaction: |
palmitoyl-CoA + [myelin proteolipid] = CoA + O-palmitoyl-[myelin proteolipid] |
Other name(s): |
myelin PLP acyltransferase; acyl-protein synthetase; myelin-proteolipid O-palmitoyltransferase |
Systematic name: |
palmitoyl-CoA:[myelin-proteolipid] O-palmitoyltransferase |
Comments: |
The enzyme in brain transfers long-chain acyl residues to the endogenous myelin proteolipid |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82657-98-5 |
References: |
1. |
Bizzozero, O.A., McGarry, J.F. and Lees, M.B. Acylation of endogenous myelin proteolipid protein with different acyl-CoAs. J. Biol. Chem. 262 (1987) 2138–2145. [PMID: 3818589] |
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[EC 2.3.1.100 created 1989] |
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EC |
2.3.1.123 |
Accepted name: |
dolichol O-acyltransferase |
Reaction: |
palmitoyl-CoA + dolichol = CoA + dolichyl palmitate |
Other name(s): |
acyl-CoA:dolichol acyltransferase |
Systematic name: |
palmitoyl-CoA:dolichol O-palmitoyltransferase |
Comments: |
Other acyl-CoAs can also act, but more slowly. α-Saturated dolichols are acylated more rapidly than the α-unsaturated analogues. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 111839-04-4 |
References: |
1. |
Tollbom, Ö., Valtersson, C., Chojnacki, T. and Dallner, G. Esterification of dolichol in rat liver. J. Biol. Chem. 263 (1988) 1347–1352. [PMID: 3121628] |
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[EC 2.3.1.123 created 1990] |
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EC |
2.3.1.137 |
Accepted name: |
carnitine O-octanoyltransferase |
Reaction: |
octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine |
Other name(s): |
medium-chain/long-chain carnitine acyltransferase; carnitine medium-chain acyltransferase; easily solubilized mitochondrial carnitine palmitoyltransferase; overt mitochondrial carnitine palmitoyltransferase |
Systematic name: |
octanoyl-CoA:L-carnitine O-octanoyltransferase |
Comments: |
Acts on a range of acyl-CoAs, with optimal activity with C6 or C8 acyl groups. cf. EC 2.3.1.7 (carnitine O-acetyltransferase) and EC 2.3.1.21 (carnitine O-palmitoyltransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39369-19-2 |
References: |
1. |
Farrell, S.O., Fiol, C.J., Reddy, J.K. and Bieber, L.L. Properties of purified carnitine acyltransferases of mouse liver peroxisomes. J. Biol. Chem. 259 (1984) 13089–13095. [PMID: 6436243] |
2. |
Healy, M.J., Kerner, J. and Bieber, L.L. Enzymes of carnitine acylation. Is overt carnitine palmitoyltransferase of liver peroxisomal carnitine octanoyltransferase? Biochem. J. 249 (1988) 231–237. [PMID: 3342008] |
3. |
Miyazawa, S., Ozasa, H., Osumi, T. and Hashimoto, T. Purification and properties of carnitine octanoyltransferase and carnitine palmitoyltransferase from rat liver. J. Biochem. (Tokyo) 94 (1983) 529–542. [PMID: 6630173] |
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[EC 2.3.1.137 created 1992] |
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EC |
2.3.1.139 |
Accepted name: |
ecdysone O-acyltransferase |
Reaction: |
palmitoyl-CoA + ecdysone = CoA + ecdysone palmitate |
Other name(s): |
acyl-CoA:ecdysone acyltransferase; fatty acyl-CoA:ecdysone acyltransferase |
Systematic name: |
palmitoyl-CoA:ecdysone palmitoyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 120038-26-8 |
References: |
1. |
Slinger, A.J. and Isaac, R.E. Acyl-CoA-ecdysone acyltransferase activity from the ovary of P. americana. Insect Biochem. 18 (1988) 779–784. |
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[EC 2.3.1.139 created 1992] |
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EC |
2.3.1.142 |
Accepted name: |
glycoprotein O-fatty-acyltransferase |
Reaction: |
palmitoyl-CoA + mucus glycoprotein = CoA + O-palmitoylglycoprotein |
Other name(s): |
protein acyltransferase |
Systematic name: |
fatty-acyl-CoA:mucus-glycoprotein fatty-acyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122191-29-1 |
References: |
1. |
Kasinathan, C., Grzelinska, E., Okazaki, F., Slomiany, B.L. and Slomiany, A. Purification of protein fatty acyltransferase and determination of its distribution and topology. J. Biol. Chem. 265 (1990) 5139–5144. [PMID: 2318887] |
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[EC 2.3.1.142 created 1992] |
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EC
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2.3.1.154
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Transferred entry: | Propionyl-CoA C2-trimethyltridecanoyltransferase. Now EC 2.3.1.176, propanoyl-CoA C-acyltransferase.
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[EC 2.3.1.154 created 2000, deleted 2015] |
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EC |
2.3.1.155 |
Accepted name: |
acetyl-CoA C-myristoyltransferase |
Reaction: |
myristoyl-CoA + acetyl-CoA = CoA + 3-oxopalmitoyl-CoA |
Systematic name: |
myristoyl-CoA:acetyl-CoA C-myristoyltransferase |
Comments: |
A peroxisomal enzyme involved in branched chain fatty acid β-oxidation in peroxisomes. It differs from EC 2.3.1.154 (propionyl-CoA C2-trimethyldecanoyltransferase) in not being active towards 3-oxopristanoyl-CoA. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Miyazawa, S., Furuta, S., Osumi, T., Hashimoto, T. and Ui, N. Properties of peroxisomal 3-ketoacyl-coA thiolase from rat liver. J. Biochem. (Tokyo) 90 (1981) 511–519. [PMID: 6117552] |
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[EC 2.3.1.155 created 2000] |
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EC |
2.3.1.199 |
Accepted name: |
very-long-chain 3-oxoacyl-CoA synthase |
Reaction: |
a very-long-chain acyl-CoA + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA |
Glossary: |
a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms. |
Other name(s): |
very-long-chain 3-ketoacyl-CoA synthase; very-long-chain β-ketoacyl-CoA synthase; condensing enzyme (ambiguous); CUT1 (gene name); CER6 (gene name); FAE1 (gene name); KCS (gene name); ELO (gene name) |
Systematic name: |
malonyl-CoA:very-long-chain acyl-CoA malonyltransferase (decarboxylating and thioester-hydrolysing) |
Comments: |
This is the first component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. Multiple forms exist with differing preferences for the substrate, and thus the specific form expressed determines the local composition of very-long-chain fatty acids [6,7]. For example, the FAE1 form from the plant Arabidopsis thaliana accepts only 16 and 18 carbon substrates, with oleoyl-CoA (18:1) being the preferred substrate [5], while CER6 from the same plant prefers substrates with chain length of C22 to C32 [4,8]. cf. EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Toke, D.A. and Martin, C.E. Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae. J. Biol. Chem. 271 (1996) 18413–18422. [DOI] [PMID: 8702485] |
2. |
Oh, C.S., Toke, D.A., Mandala, S. and Martin, C.E. ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J. Biol. Chem. 272 (1997) 17376–17384. [DOI] [PMID: 9211877] |
3. |
Dittrich, F., Zajonc, D., Huhne, K., Hoja, U., Ekici, A., Greiner, E., Klein, H., Hofmann, J., Bessoule, J.J., Sperling, P. and Schweizer, E. Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of elongation-defective mutants. Eur. J. Biochem. 252 (1998) 477–485. [DOI] [PMID: 9546663] |
4. |
Millar, A.A., Clemens, S., Zachgo, S., Giblin, E.M., Taylor, D.C. and Kunst, L. CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme. Plant Cell 11 (1999) 825–838. [PMID: 10330468] |
5. |
Ghanevati, M. and Jaworski, J.G. Engineering and mechanistic studies of the Arabidopsis FAE1 β-ketoacyl-CoA synthase, FAE1 KCS. Eur. J. Biochem. 269 (2002) 3531–3539. [DOI] [PMID: 12135493] |
6. |
Blacklock, B.J. and Jaworski, J.G. Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases. Biochem. Biophys. Res. Commun. 346 (2006) 583–590. [DOI] [PMID: 16765910] |
7. |
Denic, V. and Weissman, J.S. A molecular caliper mechanism for determining very long-chain fatty acid length. Cell 130 (2007) 663–677. [DOI] [PMID: 17719544] |
8. |
Tresch, S., Heilmann, M., Christiansen, N., Looser, R. and Grossmann, K. Inhibition of saturated very-long-chain fatty acid biosynthesis by mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA synthases. Phytochemistry 76 (2012) 162–171. [DOI] [PMID: 22284369] |
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[EC 2.3.1.199 created 2012] |
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EC |
2.3.1.225 |
Accepted name: |
protein S-acyltransferase |
Reaction: |
palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA |
Other name(s): |
DHHC palmitoyl transferase; S-protein acyltransferase; G-protein palmitoyltransferase |
Systematic name: |
palmitoyl-CoA:[protein]-L-cysteine S-palmitoyltransferase |
Comments: |
The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Dunphy, J.T., Greentree, W.K., Manahan, C.L. and Linder, M.E. G-protein palmitoyltransferase activity is enriched in plasma membranes. J. Biol. Chem. 271 (1996) 7154–7159. [DOI] [PMID: 8636152] |
2. |
Veit, M., Dietrich, L.E. and Ungermann, C. Biochemical characterization of the vacuolar palmitoyl acyltransferase. FEBS Lett. 540 (2003) 101–105. [DOI] [PMID: 12681491] |
3. |
Batistic, O. Genomics and localization of the Arabidopsis DHHC-cysteine-rich domain S-acyltransferase protein family. Plant Physiol. 160 (2012) 1597–1612. [DOI] [PMID: 22968831] |
4. |
Jennings, B.C. and Linder, M.E. DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities. J. Biol. Chem. 287 (2012) 7236–7245. [DOI] [PMID: 22247542] |
5. |
Zhou, L.Z., Li, S., Feng, Q.N., Zhang, Y.L., Zhao, X., Zeng, Y.L., Wang, H., Jiang, L. and Zhang, Y. Protein S-acyl transferase10 is critical for development and salt tolerance in Arabidopsis. Plant Cell 25 (2013) 1093–1107. [DOI] [PMID: 23482856] |
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[EC 2.3.1.225 created 2013] |
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EC |
2.3.1.250 |
Accepted name: |
[Wnt protein] O-palmitoleoyl transferase |
Reaction: |
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine = CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine |
Glossary: |
(9Z)-hexadec-9-enoate = palmitoleoate |
Other name(s): |
porcupine; PORCN (gene name) |
Systematic name: |
(9Z)-hexadec-9-enoyl-CoA:[Wnt]-L-serine O-hexadecenoyltransferase |
Comments: |
The enzyme, found in animals, modifies a specific serine residue in Wnt proteins, e.g. Ser209 in human Wnt3a and Ser224 in chicken WNT1 [2,3]. The enzyme can accept C13 to C16 fatty acids in vitro, but only (9Z)-hexadecenoate modification is observed in vivo [1]. cf. EC 3.1.1.98, [Wnt protein]-O-palmitoleoyl-L-serine hydrolase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Takada, R., Satomi, Y., Kurata, T., Ueno, N., Norioka, S., Kondoh, H., Takao, T. and Takada, S. Monounsaturated fatty acid modification of Wnt protein: its role in Wnt secretion. Dev Cell 11 (2006) 791–801. [DOI] [PMID: 17141155] |
2. |
Gao, X. and Hannoush, R.N. Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine. Nat. Chem. Biol. 10 (2014) 61–68. [DOI] [PMID: 24292069] |
3. |
Miranda, M., Galli, L.M., Enriquez, M., Szabo, L.A., Gao, X., Hannoush, R.N. and Burrus, L.W. Identification of the WNT1 residues required for palmitoylation by Porcupine. FEBS Lett. 588 (2014) 4815–4824. [DOI] [PMID: 25451226] |
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[EC 2.3.1.250 created 2015] |
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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
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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] |
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[EC 2.3.1.251 created 2015] |
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EC |
2.3.1.278 |
Accepted name: |
mycolipenoyl-CoA—2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase |
Reaction: |
a mycolipenoyl-CoA + a 2-(long-chain-fatty acyl)-trehalose = a 2-(long-chain-fatty acyl)-3-mycolipenoyl-trehalose + CoA |
Glossary: |
a mycolipenoyl-CoA = a (2E,2S,4S,6S)-2,4,6-trimethyl-2-enoyl-CoA
polyacyltrehalose = PAT = a 2-(long-chain-fatty acyl)-2′,3,4′,6-tetramycolipenoyl-trehalose |
Other name(s): |
papA3 (gene name) |
Systematic name: |
mycolipenoyl-CoA:2-(long-chain-fatty acyl)-trehalose 3-mycolipenoyltransferase |
Comments: |
The enzyme, characterized from the bacterium Mycobacterium tuberculosis, participates in the biosynthesis of polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains. The enzyme catalyses two successive activities - it first transfers an acyl (often palmitoyl) group to position 2 (see EC 2.3.1.279, long-chain-acyl-CoA—trehalose acyltransferase), followed by the transfer of a mycolipenyl group to position 3. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Hatzios, S.K., Schelle, M.W., Holsclaw, C.M., Behrens, C.R., Botyanszki, Z., Lin, F.L., Carlson, B.L., Kumar, P., Leary, J.A. and Bertozzi, C.R. PapA3 is an acyltransferase required for polyacyltrehalose biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 284 (2009) 12745–12751. [PMID: 19276083] |
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[EC 2.3.1.278 created 2018] |
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EC |
2.3.1.279 |
Accepted name: |
long-chain-acyl-CoA—trehalose acyltransferase |
Reaction: |
a long-chain-fatty acyl-CoA + α,α-trehalose = a 2-(long-chain-fatty acyl)-trehalose + CoA |
Glossary: |
polyacyltrehalose = PAT = a 2-(long-chain-fatty acyl)-2′,3,4′,6-tetramycolipenoyl-trehalose
a mycolipenoyl-CoA = a (2E,2S,4S,6S)-2,4,6-trimethyl-2-enoyl-CoA |
Other name(s): |
papA3 (gene name) |
Systematic name: |
long-chain-fatty acyl-CoA:α,α-trehalose 2-acyltransferase |
Comments: |
The enzyme, characterized from the bacterium Mycobacterium tuberculosis, participates in the biosynthesis of polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid found in the cell wall of pathogenic strains. The enzyme catalyses two successive activities - it first transfers an acyl (often palmitoyl) group to position 2, followed by the transfer of a mycolipenyl group to position 3 (see EC 2.3.1.278, mycolipenoyl-CoA—2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Hatzios, S.K., Schelle, M.W., Holsclaw, C.M., Behrens, C.R., Botyanszki, Z., Lin, F.L., Carlson, B.L., Kumar, P., Leary, J.A. and Bertozzi, C.R. PapA3 is an acyltransferase required for polyacyltrehalose biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 284 (2009) 12745–12751. [PMID: 19276083] |
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[EC 2.3.1.279 created 2018] |
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EC |
2.3.1.283 |
Accepted name: |
2′-acyl-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase |
Reaction: |
a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 2′-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose = a 3′-(hydroxy)phthioceranyl-2′-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose + holo-[(hydroxy)phthioceranic acid synthase] |
Other name(s): |
papA1 (gene name) |
Systematic name: |
(hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid synthase]:2′-acyl-2-O-sulfo-α,α-trehalose 3′-(hydroxy)phthioceranyltransferase |
Comments: |
This mycobacterial enzyme catalyses the acylation of 2′-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose at the 3′ position by a (hydroxy)phthioceranoyl group during the biosynthesis of mycobacterial sulfolipids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Bhatt, K., Gurcha, S.S., Bhatt, A., Besra, G.S. and Jacobs, W.R., Jr. Two polyketide-synthase-associated acyltransferases are required for sulfolipid biosynthesis in Mycobacterium tuberculosis. Microbiology 153 (2007) 513–520. [PMID: 17259623] |
2. |
Kumar, P., Schelle, M.W., Jain, M., Lin, F.L., Petzold, C.J., Leavell, M.D., Leary, J.A., Cox, J.S. and Bertozzi, C.R. PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Proc. Natl. Acad. Sci. USA 104 (2007) 11221–11226. [PMID: 17592143] |
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[EC 2.3.1.283 created 2019] |
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EC |
2.3.1.284 |
Accepted name: |
3′-(hydroxy)phthioceranyl-2′-palmitoyl(stearoyl)-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase |
Reaction: |
3 3′-(hydroxy)phthioceranyl-2′-palmitoyl(stearoyl)-2-O-sulfo-α,α-trehalose = 3,6,6′-tris-(hydroxy)phthioceranyl-2-palmitoyl(stearoyl)-2′-sulfo-α-alpha-trehalose + 2 2′-palmitoyl/stearoyl-2-O-sulfo-α,α-trehalose |
Glossary: |
3,6,6′-tris-(hydroxy)phthioceranyl-2-palmitoyl(stearoyl)-2′-sulfo-α-alpha-trehalose = a mycobacterial sulfolipid |
Other name(s): |
chp1 (gene name) |
Systematic name: |
3′-(hydroxy)phthioceranyl-2′-palmitoyl(stearoyl)-2-O-sulfo-α,α-trehalose:3′-(hydroxy)phthioceranyl-2′-palmitoyl(stearoyl)-2-O-sulfo-α,α-trehalose 6,6′-di(hydroxy)phthioceranyltransferase |
Comments: |
The enzyme, present in mycobacteria, catalyses the ultimate step in the biosynthesis of mycobacterial sulfolipids. It catalyses two successive transfers of a (hydroxy)phthioceranyl group from two diacylated intermediates to third diacylated intermediate, generating the tetraacylated sulfolipid. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Seeliger, J.C., Holsclaw, C.M., Schelle, M.W., Botyanszki, Z., Gilmore, S.A., Tully, S.E., Niederweis, M., Cravatt, B.F., Leary, J.A. and Bertozzi, C.R. Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 287 (2012) 7990–8000. [PMID: 22194604] |
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[EC 2.3.1.284 created 2019] |
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EC |
2.3.1.287 |
Accepted name: |
phthioceranic/hydroxyphthioceranic acid synthase |
Reaction: |
(1) 8 (S)-methylmalonyl-CoA + palmitoyl-[(hydroxy)phthioceranic acid synthase] + 16 NADPH + 16 H+ = 8 CoA + C40-phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 16 NADP+ + 8 CO2 + 8 H2O (2) 7 (S)-methylmalonyl-CoA + palmitoyl-[(hydroxy)phthioceranic acid synthase] + 14 NADPH + 14 H+ = 7 CO2 + C37-phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 14 NADP+ + 7 CoA + 7 H2O |
Other name(s): |
msl2 (gene name); PKS2 |
Systematic name: |
(S)-methylmalonyl-CoA:palmitoyl-[(hydroxy)phthioceranic acid synthase] methylmalonyltransferase (phthioceranyl-[(hydroxy)phthioceranic acid synthase]-forming) |
Comments: |
This mycobacterial polyketide enzyme produces the hepta- and octa-methylated fatty acids known as phthioceranic acids, and presumably their hydroxylated versions. Formation of hepta- and octamethylated products depends on whether the enzyme incorporates seven or eight methylmalonyl-CoA extender units, respectively. Formation of hydroxylated products may result from the enzyme skipping the dehydratase (DH) and enoylreductase (ER) domains during the first cycle of condensation [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Sirakova, T.D., Thirumala, A.K., Dubey, V.S., Sprecher, H. and Kolattukudy, P.E. The Mycobacterium tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis. J. Biol. Chem. 276 (2001) 16833–16839. [DOI] [PMID: 11278910] |
2. |
Gokhale, R.S., Saxena, P., Chopra, T. and Mohanty, D. Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids. Nat. Prod. Rep. 24 (2007) 267–277. [PMID: 17389997] |
3. |
Passemar, C., Arbues, A., Malaga, W., Mercier, I., Moreau, F., Lepourry, L., Neyrolles, O., Guilhot, C. and Astarie-Dequeker, C. Multiple deletions in the polyketide synthase gene repertoire of Mycobacterium tuberculosis reveal functional overlap of cell envelope lipids in host-pathogen interactions. Cell Microbiol 16 (2014) 195–213. [PMID: 24028583] |
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[EC 2.3.1.287 created 2019] |
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EC |
2.3.1.288 |
Accepted name: |
2-O-sulfo trehalose long-chain-acyltransferase |
Reaction: |
(1) stearoyl-CoA + 2-O-sulfo-α,α-trehalose = 2-O-sulfo-2′-stearoyl-α,α-trehalose + CoA (2) palmitoyl-CoA + 2-O-sulfo-α,α-trehalose = 2-O-sulfo-2′-palmitoyl-α,α-trehalose + CoA
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Other name(s): |
papA2 (gene name) |
Systematic name: |
acyl-CoA:2-O-sulfo-α,α-trehalose 2′-long-chain-acyltransferase |
Comments: |
This mycobacterial enzyme catalyses the acylation of 2-O-sulfo-α,α-trehalose at the 2′ position by a C16 or C18 fatty acyl group during the biosynthesis of mycobacterial sulfolipids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kumar, P., Schelle, M.W., Jain, M., Lin, F.L., Petzold, C.J., Leavell, M.D., Leary, J.A., Cox, J.S. and Bertozzi, C.R. PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Proc. Natl. Acad. Sci. USA 104 (2007) 11221–11226. [PMID: 17592143] |
2. |
Seeliger, J.C., Holsclaw, C.M., Schelle, M.W., Botyanszki, Z., Gilmore, S.A., Tully, S.E., Niederweis, M., Cravatt, B.F., Leary, J.A. and Bertozzi, C.R. Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 287 (2012) 7990–8000. [PMID: 22194604] |
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[EC 2.3.1.288 created 2019] |
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EC |
2.3.1.291 |
Accepted name: |
sphingoid base N-palmitoyltransferase |
Reaction: |
palmitoyl-CoA + a sphingoid base = an N-(palmitoyl)-sphingoid base + CoA |
Other name(s): |
mammalian ceramide synthase 5; CERS5 (gene name); LASS5 (gene name) |
Systematic name: |
palmitoyl-CoA:sphingoid base N-palmitoyltransferase |
Comments: |
Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 5 (CERS5) is specific for palmitoyl-CoA as the acyl donor. It can use multiple sphingoid bases including sphinganine, sphingosine, and phytosphingosine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Lahiri, S. and Futerman, A.H. LASS5 is a bona fide dihydroceramide synthase that selectively utilizes palmitoyl-CoA as acyl donor. J. Biol. Chem. 280 (2005) 33735–33738. [PMID: 16100120] |
2. |
Xu, Z., Zhou, J., McCoy, D.M. and Mallampalli, R.K. LASS5 is the predominant ceramide synthase isoform involved in de novo sphingolipid synthesis in lung epithelia. J. Lipid Res. 46 (2005) 1229–1238. [PMID: 15772421] |
3. |
Mizutani, Y., Kihara, A. and Igarashi, Y. Mammalian Lass6 and its related family members regulate synthesis of specific ceramides. Biochem. J. 390 (2005) 263–271. [PMID: 15823095] |
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[EC 2.3.1.291 created 2019, modified 2019] |
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EC |
3.1.1.1 |
Accepted name: |
carboxylesterase |
Reaction: |
a carboxylic ester + H2O = an alcohol + a carboxylate |
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For diagram of retinal and derivatives biosynthesis, click here |
Other name(s): |
ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase |
Systematic name: |
carboxylic-ester hydrolase |
Comments: |
Wide specificity. The enzymes from microsomes also catalyse the reactions of EC 3.1.1.2 (arylesterase), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.6 (acetylesterase), EC 3.1.1.23 (acylglycerol lipase), EC 3.1.1.28 (acylcarnitine hydrolase), EC 3.1.2.2 (palmitoyl-CoA hydrolase), EC 3.5.1.4 (amidase) and EC 3.5.1.13 (aryl-acylamidase). Also hydrolyses vitamin A esters. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9016-18-6 |
References: |
1. |
Augusteyn, R.C., de Jersey, J., Webb, E.C. and Zerner, B. On the homology of the active-site peptides of liver carboxylesterases. Biochim. Biophys. Acta 171 (1969) 128–137. [DOI] [PMID: 4884138] |
2. |
Barker, D.L. and Jencks, W.P. Pig liver esterase. Physical properties. Biochemistry 8 (1969) 3879–3889. [PMID: 4981346] |
3. |
Bertram, J. and Krisch, K. Hydrolysis of vitamin A acetate by unspecific carboxylesterases from liver and kidney. Eur. J. Biochem. 11 (1969) 122–126. [DOI] [PMID: 5353595] |
4. |
Burch, J. The purification and properties of horse liver esterase. Biochem. J. 58 (1954) 415–426. [PMID: 13208632] |
5. |
Horgan, D.J., Stoops, J.K., Webb, E.C. and Zerner, B. Carboxylesterases (EC 3.1.1). A large-scale purification of pig liver carboxylesterase. Biochemistry 8 (1969) 2000–2006. [PMID: 5785220] |
6. |
Malhotra, O.P. and Philip, G. Specificity of goat intestinal esterase. Biochem. Z. 346 (1966) 386–402. |
7. |
Mentlein, R., Schumann, M. and Heymann, E. Comparative chemical and immunological characterization of five lipolytic enzymes (carboxylesterases) from rat liver microsomes. Arch. Biochem. Biophys. 234 (1984) 612–621. [DOI] [PMID: 6208846] |
8. |
Runnegar, M.T.C., Scott, K., Webb, E.C. and Zerner, B. Carboxylesterases (EC 3.1.1). Purification and titration of ox liver carboxylesterase. Biochemistry 8 (1969) 2013–2018. [PMID: 5785222] |
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[EC 3.1.1.1 created 1961] |
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EC |
3.1.1.28 |
Accepted name: |
acylcarnitine hydrolase |
Reaction: |
O-acylcarnitine + H2O = a fatty acid + L-carnitine |
Other name(s): |
high activity acylcarnitine hydrolase; HACH; carnitine ester hydrolase; palmitoylcarnitine hydrolase; palmitoyl-L-carnitine hydrolase; long-chain acyl-L-carnitine hydrolase; palmitoyl carnitine hydrolase |
Systematic name: |
O-acylcarnitine acylhydrolase |
Comments: |
Acts on higher fatty acid (C6 to C18) esters of L-carnitine; highest activity is with O-decanoyl-L-carnitine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-42-5 |
References: |
1. |
Mahadevan, S. and Sauer, F. Carnitine ester hydrolase of rat liver. J. Biol. Chem. 244 (1969) 4448–4453. [PMID: 5806585] |
2. |
Mentlein, R., Reuter, G. and Heymann, E. Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other carboxylesterases, and their possible function. Arch. Biochem. Biophys. 240 (1985) 801–810. [DOI] [PMID: 4026306] |
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[EC 3.1.1.28 created 1972] |
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EC |
3.1.2.2 |
Accepted name: |
palmitoyl-CoA hydrolase |
Reaction: |
palmitoyl-CoA + H2O = CoA + palmitate |
Other name(s): |
long-chain fatty-acyl-CoA hydrolase; palmitoyl coenzyme A hydrolase; palmitoyl thioesterase; palmitoyl coenzyme A hydrolase; palmitoyl-CoA deacylase; palmityl thioesterase; palmityl-CoA deacylase; fatty acyl thioesterase I; palmityl thioesterase I |
Systematic name: |
palmitoyl-CoA hydrolase |
Comments: |
Also hydrolyses CoA thioesters of other long-chain fatty acids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-87-0 |
References: |
1. |
Barnes, E.M., Jr. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XIX. Preparation and general properties of palmityl thioesterase. J. Biol. Chem. 243 (1968) 2955–2962. [PMID: 4871199] |
2. |
Berge, R.K. and Farstad, M. Long-chain fatty acyl-CoA hydrolase from rat liver mitochondria. Methods Enzymol. 71 (1981) 234–242. [PMID: 6116156] |
3. |
Miyazawa, S., Furuta, S. and Hashimoto, T. Induction of a novel long-chain acyl-CoA hydrolase in rat liver by administration of peroxisome proliferators. Eur. J. Biochem. 117 (1981) 425–430. [DOI] [PMID: 6115749] |
4. |
Srere, P.A., Seubert, W. and Lynen, F. Palmityl coenzyme A deacylase. Biochim. Biophys. Acta 33 (1959) 313–319. [DOI] [PMID: 13670899] |
5. |
Yabusaki, K.K. and Ballou, C.E. Long-chain fatty acyl-CoA thioesterases from Mycobacterium smegmatis. Methods Enzymol. 71 (1981) 242–246. |
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[EC 3.1.2.2 created 1961] |
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