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Your query returned 4 entries. 
Printable version
| EC | 1.14.19.12 | ||||||
| Accepted name: | acyl-lipid ω-(9-4) desaturase | ||||||
| Reaction: | (1) linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = pinolenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O (2) α-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = coniferonoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O |
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| Glossary: | taxoleate = (5Z,9Z)-octadeca-5,9-dienoate pinolenoate = (5Z,9Z,12Z)-octadeca-5,9,12-trienoate coniferonate = (5Z,9Z,12Z,15Z)-octadeca-5,9,12,15-tetraenoate |
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| Other name(s): | acyl-lipid ω-13 desaturase; acyl-lipid 7-desaturase (ambiguous) | ||||||
| Systematic name: | acyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase [ω(9-4),ω(9-5) cis-dehydrogenating] | ||||||
| Comments: | The enzyme, characterized from the green alga Chlamydomonas reinhardtii, is a front-end desaturase that introduces a cis double bond in ω9 unsaturated C18 or C20 fatty acids incorporated into lipids, at a position 4 carbon atoms from the existing ω9 bond, towards the carboxy end of the fatty acid (at the ω13 position). When acting on 20:2Δ(11,14) and 20:3Δ(11,14,17) substrates it introduces the new double bond between carbons 7 and 8. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor for the active site of the desaturase. | ||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||
| References: |
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| 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] |
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| 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: |
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| EC | 1.14.19.35 | ||||||
| Accepted name: | sn-2 acyl-lipid ω-3 desaturase (ferredoxin) | ||||||
| Reaction: | (1) a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O (2) a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = an α-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
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| Glossary: | (9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid] = linoleoyl-[glycerolipid] (9Z,12Z,15Z)-octadeca-9,12,15-trienoyl-[glycerolipid] = α-linolenoyl-[glycerolipid] |
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| Other name(s): | FAD7; FAD8 | ||||||
| Systematic name: | (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (13,14 cis-dehydrogenating) | ||||||
| Comments: | This plastidial enzyme desaturates 16:2 fatty acids attached to the sn-2 position of glycerolipids to 16:3 fatty acids, and converts18:2 to 18:3 in both the sn-1 and sn-2 positions. It acts on all 16:2- or 18:2-containing chloroplast membrane lipids, including phosphatidylglycerol, monogalactosyldiacylglycerol, digalactosyldiaclyglycerol, and sulfoquinovosyldiacylglycerol. The enzyme introduces a cis double bond at a location 3 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. cf. EC 1.14.19.25, acyl-lipid ω-3 desaturase (cytochrome b5) and EC 1.14.19.36, sn-1 acyl-lipid ω-3 desaturase (ferredoxin). | ||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||
| References: |
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| EC | 1.14.19.47 | ||||||
| Accepted name: | acyl-lipid (9-3)-desaturase | ||||||
| Reaction: | (1) an α-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a stearidonoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O (2) a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a γ-linolenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O |
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| Glossary: | stearidonic acid = (6Z,9Z,12Z,15Z)-octadeca-6,9,12,15-tetraenoic acid | ||||||
| Other name(s): | DES6 (gene name); acyl-lipid 6-desaturase; acyl-lipid Δ6-desaturase; Δ6-desaturase (ambiguous) | ||||||
| Systematic name: | Δ9 acyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase (6,7-cis-dehydrogenating) | ||||||
| Comments: | The enzyme, characterized from the moss Physcomitrella patens and the plant Borago officinalis (borage), introduces a cis double bond at carbon 6 of several acyl-lipids that contain an existing Δ9 cis double bond. The enzyme contains a cytochrome b5 domain that acts as the electron donor for the active site of the desaturase. | ||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||
| References: |
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