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| Product | Description | |
|---|---|---|
| acyl-lipid (11-3)-desaturase | The enzyme, characterized from the protist Euglena gracilis and the microalga Rebecca salina, introduces a cis double bond at the 8-position in 20-carbon fatty acids that are incorporated into a glycerolipid and have an existing Δ11 desaturation. The enzyme is a front-end desaturase, introducing the new double bond between the pre-existing double bond and the carboxyl-end of the fatty acid. It contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. Involved in alternative pathways for the biosynthesis of the polyunsaturated fatty acids arachidonate and icosapentaenoate. Group: Enzymes. Synonyms: acyl-lipid 8-desaturase; Δ8 fatty acid desaturase; Δ8-desaturase; Δ8-fatty-acid desaturase; efd1 (gene name); D8Des (gene name); phytosphinganine,hydrogen donor:oxygen Δ. Enzyme Commission Number: EC 1.14.19.4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1004; acyl-lipid (11-3)-desaturase; EC 1.14.19.4; acyl-lipid 8-desaturase; Δ8 fatty acid desaturase; Δ8-desaturase; Δ8-fatty-acid desaturase; efd1 (gene name); D8Des (gene name); phytosphinganine,hydrogen donor:oxygen Δ8-oxidoreductase (incorrect); SLD. Cat No: EXWM-1004. |  |
| acyl-lipid (7-3)-desaturase | The enzymes from several algae introduce a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Δ7 double bond. The enzyme from the fresh water alga Chlamydomonas reinhardtii acts on the 16 carbon fatty acid (7Z,10Z,13Z)-hexadeca-7,10,13-trienoate. The enzyme contains an N-terminal cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. Group: Enzymes. Synonyms: D4Des (gene name); des1 (gene name); CrΔ4FAD (gene name); acyl-lipid 4-desaturase. Enzyme Commission Number: EC 1.14.19.31. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0995; acyl-lipid (7-3)-desaturase; EC 1.14.19.31; D4Des (gene name); des1 (gene name); CrΔ4FAD (gene name); acyl-lipid 4-desaturase. Cat No: EXWM-0995. | |
| acyl-lipid (8-3)-desaturase | The enzyme, which has been characterized from multiple organisms including the moss Physcomitrella patens, the marine microalga Rebecca salina, and the filamentous fungus Mortierella alpina, introduces a cis double bond at the 5-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Δ8 double bond. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. Group: Enzymes. Synonyms: acyl-lipid 5-desaturase; Δ5-fatty-acid desaturase; DES5 (gene name); D5des (gene name); FADS1. Enzyme Commission Number: EC 1.14.19.30. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0994; acyl-lipid (8-3)-desaturase; EC 1.14.19.30; acyl-lipid 5-desaturase; Δ5-fatty-acid desaturase; DES5 (gene name); D5des (gene name); FADS1. Cat No: EXWM-0994. | |
| acyl-lipid (9-3)-desaturase | 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. Group: Enzymes. Synonyms: acyl-lipid 6-desaturase; Δ6-desaturase; DES6 (gene name). Enzyme Commission Number: EC 1.14.19.47. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1012; acyl-lipid (9-3)-desaturase; EC 1.14.19.47; acyl-lipid 6-desaturase; Δ6-desaturase; DES6 (gene name). Cat No: EXWM-1012. | |
| acyl-lipid (9+3)-(E)-desaturase | The enzymes from the plants Dimorphotheca sinuata (African daisy) and Vernicia fordii (tung oil tree) insert a trans double bond in position C-12 of oleate and palmitoleate incorporated into glycerolipids. The enzyme introduces the new double bond at a position three carbons away from an existing double bond at position 9, towards the methyl end of the fatty acid. The enzyme from tung oil tree also possesses the activity of EC 1.14.19.33, Δ12 acyl-lipid conjugase. Group: Enzymes. Synonyms: acyl-lipid 12-(E)-desaturase; DsFAD2-1; FADX. Enzyme Commission Number: EC 1.14.19.34. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0998; acyl-lipid (9+3)-(E)-desaturase; EC 1.14.19.34; acyl-lipid 12-(E)-desaturase; DsFAD2-1; FADX. Cat No: EXWM-0998. | |
| acyl-lipid (n+3)-(Z)-desaturase (ferredoxin) | 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. cf. EC 1.14.19.34, acyl-lipid (9+3)-(E)-desaturase. Group: Enzymes. Synonyms: acyl-. Enzyme Commission Number: EC 1.14.19.23. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0986; acyl-lipid (n+3)-(Z)-desaturase (ferredoxin); EC 1.14.19.23; acyl-lipid ω6-desaturase (ferredoxin); oleate desaturase (ambiguous); linoleate synthase (ambiguous); oleoyl-CoA desaturase (ambiguous); oleoylphosphatidylcholine desaturase (ambiguous); phosphatidylcholine desaturase (ambiguous); FAD6 (gene name). Cat No: EXWM-0986. | |
| acyl-lipid ω-3 desaturase (cytochrome b5) | 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. cf. EC 1.14.19.35, acyl-lipid ω-3 desaturase (ferredoxin). Group: Enzymes. Synonyms: FAD3. Enzyme Commission Number: EC 1.14.19.25. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0988; acyl-lipid ω-3 desaturase (cytochrome b5); EC 1.14.19.25; FAD3. Cat No: EXWM-0988. | |
| acyl-lipid ω-6 desaturase (cytochrome b5) | 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). Group: Enzymes. Synonyms: oleate desaturase (ambiguous); linoleate synthase (ambiguous); oleoyl-CoA desaturase (incorrect); oleoylphosphatidylcholine desaturase (ambiguous); phosphatidylcholine desaturase (ambiguous); n-6 desaturase (ambiguous); FAD2 (gene name). Enzyme Commission Number: EC 1.14.19.22. CAS No. 72536-70-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0985; acyl-lipid ω-6 desaturase (cytochrome b5); EC 1.14.19.22; 72536-70-0; oleate desaturase (ambiguous); linoleate synthase (ambiguous); oleoyl-CoA desaturase (incorrect); oleoylphosphatidylcholine desaturase (ambiguous); phosphatidylcholine desaturase (ambiguous); n-6 desaturase (ambiguous); FAD2 (gene name). Cat No: EXWM-0985. | |
| acyl-lipid ω-(9-4) desaturase | 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. Group: Enzymes. Synonyms: acyl-lipid ω-13 desaturase; acyl-lipid 7-desaturase (ambiguous). Enzyme Commission Number: EC 1.14.19.12. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0974; acyl-lipid ω-(9-4) desaturase; EC 1.14.19.12; acyl-lipid ω-13 desaturase; acyl-lipid 7-desaturase (ambiguous). Cat No: EXWM-0974. | |
| sn-1 acyl-lipid ω-3 desaturase (ferredoxin) | The enzyme, characterized from cyanobacteria, introduces a cis double bond at carbon 15 of linoleoyl and γ-linolenoyl groups attached to the sn-1 position of glycerolipids. The enzyme is an ω desaturase, and determines the location of the double bond by counting three carbons from the methyl end of the fatty acid. It is nonspecific with respect to the polar head group of the glycerolipid. cf. EC 1.14.19.35, sn-2 acyl-lipid ω-3 desaturase (ferredoxin). Group: Enzymes. Synonyms: desB (gene name). Enzyme Commission Number: EC 1.14.19.36. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1000; sn-1 acyl-lipid ω-3 desaturase (ferredoxin); EC 1.14.19.36; desB (gene name). Cat No: EXWM-1000. | |
| sn-2 acyl-lipid ω-3 desaturase (ferredoxin) | 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). Group: Enzymes. Synonyms: FAD7; FAD8. Enzyme Commission Number: EC 1.14.19.35. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0999; sn-2 acyl-lipid ω-3 desaturase (ferredoxin); EC 1.14.19.35; FAD7; FAD8. Cat No: EXWM-0999. | |
| acyl-lipid Δ6-acetylenase | The enzyme, characterized from the moss Ceratodon purpureus, converts the double bond at position 6 of γ-linolenate and stearidonate into a triple bond. The product of the latter, dicranin, is the main fatty acid found in C. purpureus. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the desaturase active site. The enzyme also has the activity of EC 1.14.19.47, acyl-lipid (9-3)-desaturase. Group: Enzymes. Enzyme Commission Number: EC 1.14.19.38. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1002; acyl-lipid Δ6-acetylenase; EC 1.14.19.38. Cat No: EXWM-1002. | |
| Δ12 acyl-lipid conjugase (11E,13E-forming) | The enzyme, characterized from the plants Impatiens balsamina, Momordica charantia (bitter gourd) and Vernicia fordii (tung tree), converts a single cis double bond at carbon 12 to two conjugated trans bonds at positions 11 and 13. The enzyme from Vernicia fordii can also act as a 12(E) desaturase when acting on the monounsaturated fatty acids oleate and palmitoleate. cf. EC 1.14.19.16, linoleoyl-lipid Δ12 conjugase (11E,13Z-forming). Group: Enzymes. Synonyms: fatty acid Δ12-conjugase (ambiguous); FADX (gene name). Enzyme Commission Number: EC 1.14.19.33. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0997; Δ12 acyl-lipid conjugase (11E,13E-forming); EC 1.14.19.33; fatty acid Δ12-conjugase (ambiguous); FADX (gene name). Cat No: EXWM-0997. | |
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