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a (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(2)
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a (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
a (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(1)
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a (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
a (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
(1)
a (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
(1)
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-
a (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
-
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-
-
a (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
(1)
a (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
(1)
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-
a (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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22:4 DELTA7,10,13,16-docosatetraenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
22:5 DELTA4,7,10,13,16-docosapentaenoic acid + 2 ferricytochrome b5 + 2 H2O
22:5 DELTA7,10,13,16,19-docosapentaenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
22:6 DELTA4,7,10,13,16,19-docosahexaenoic acid + 2 ferricytochrome b5 + 2 H2O
a (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
a (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
docosa-7,10,13,16,19-pentaenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
docosa-4,7,10,13,16,19-hexaenoic acid + 2 ferricytochrome b5 + 2 H2O
docosa-7,10,13,16-tetraenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
docosa-4,7,10,13,16-pentaenoic acid + 2 ferricytochrome b5 + 2 H2O
additional information
?
-
22:4 DELTA7,10,13,16-docosatetraenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
22:5 DELTA4,7,10,13,16-docosapentaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
22:4 DELTA7,10,13,16-docosatetraenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
22:5 DELTA4,7,10,13,16-docosapentaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
22:5 DELTA7,10,13,16,19-docosapentaenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
22:6 DELTA4,7,10,13,16,19-docosahexaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
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?
22:5 DELTA7,10,13,16,19-docosapentaenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
22:6 DELTA4,7,10,13,16,19-docosahexaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
a (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
-
-
-
?
a (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
-
-
-
?
a (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
-
-
-
?
a (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
-
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-
?
a (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
-
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-
?
a (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
-
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-
?
a (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
-
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-
?
a (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
-
-
-
?
a (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
-
-
-
?
a (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
-
-
-
?
docosa-7,10,13,16,19-pentaenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
docosa-4,7,10,13,16,19-hexaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
docosa-7,10,13,16,19-pentaenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
docosa-4,7,10,13,16,19-hexaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
docosa-7,10,13,16,19-pentaenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
docosa-4,7,10,13,16,19-hexaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
-
-
-
?
docosa-7,10,13,16,19-pentaenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
docosa-4,7,10,13,16,19-hexaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
docosa-7,10,13,16,19-pentaenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
docosa-4,7,10,13,16,19-hexaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
docosa-7,10,13,16-tetraenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
docosa-4,7,10,13,16-pentaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
docosa-7,10,13,16-tetraenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
docosa-4,7,10,13,16-pentaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
docosa-7,10,13,16-tetraenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
docosa-4,7,10,13,16-pentaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
docosa-7,10,13,16-tetraenoic acid + 2 ferrocytochrome b5 + O2 + 2 H+
docosa-4,7,10,13,16-pentaenoic acid + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
additional information
?
-
the recombinant His-tagged cytochrome b5 domain of the enzyme is active in vitro
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?
additional information
?
-
substrate specificity, overview. The recombinant enzyme from Euglena gracilis expressed in Saccharomyces cerevisiae strain INVSc1 shows strongest activity of 15% toward 16:3(n-3) and desaturated 22:5(n-3) and 22:4(n-6) with efficiencies of 12 and 4%, respectively. The enzyme has no clear preference for desaturation of (n-3)- or (n-6)-substrates
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?
additional information
?
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the enzyme catalyzes the conversion of 2-docosapentaenoic acid (DPA, 22:5 DELTA7,10,13,16,19) to docosahexaenoic acid (DHA) by direct DELTA4-desaturation, not substrate breakdown and resynthesis. The enzyme shows strict DELTA4-regioselectivity and requires the presence of a DELTA7-double bond in the substrate. Positional analysis of phosphatidylcholine revealed that the proportion of the DELTA4-desaturated products is up to 20times higher in the sn-2 position than in the sn-1 position
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?
additional information
?
-
substrate specificity, overview. The recombinant enzyme from Euglena gracilis expressed in Saccharomyces cerevisiae strain INVSc1 shows strongest activity of 15% toward 16:3(n-3) and desaturated 22:5(n-3) and 22:4(n-6) with efficiencies of 12 and 4%, respectively. The enzyme has no clear preference for desaturation of (n-3)- or (n-6)-substrates
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?
additional information
?
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the enzyme catalyzes the production of docosahexaenoic acid
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?
additional information
?
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substrate specificity, the enzyme prefers very long chain polyunsaturated fatty acids, overview. The preferred substrate of the recombinant enzyme from Ostreococcus lucimarinus expressed in Saccharomyces cerevisiae strain INVSc1 with a desaturation activity of about 10% is 22:5(n-3) followed by 22:4(n-6) with an efficiency of about 4%. 16:3(n-3) is desaturated very poorly with an efficiency of about 1%. The enzyme has no clear preference for desaturation of (n-3)- or (n-6)-substrates
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?
additional information
?
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the enzyme catalyzes the production of docosahexaenoic acid
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?
additional information
?
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substrate specificity, the enzyme prefers very long chain polyunsaturated fatty acids, overview. The preferred substrate of the recombinant enzyme from Ostreococcus lucimarinus expressed in Saccharomyces cerevisiae strain INVSc1 with a desaturation activity of about 10% is 22:5(n-3) followed by 22:4(n-6) with an efficiency of about 4%. 16:3(n-3) is desaturated very poorly with an efficiency of about 1%. The enzyme has no clear preference for desaturation of (n-3)- or (n-6)-substrates
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?
additional information
?
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the FADS2 classical transcript mediates direct DELTA4-desaturation of 22:5n-3 to 22:6n-3 (docosahexaenoic acid) and of 22:4n-6 to 22:5n-6. The evidence supports trifunctionality of FADS2. The classical transcript shows DELTA6, DELTA8, and DELTA4 activities in mammals
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?
additional information
?
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the enzyme catalyzes the conversion of [2-(14)C]-docosapentaenoic acid (DPA, 22:5 DELTA7,10,13,16,19) to docosahexaenoic acid (DHA) by direct DELTA4-desaturation, not substrate breakdown and resynthesis. The enzyme shows strict DELTA4-regioselectivity and requires the presence of a DELTA7-double bond in the substrate. Positional analysis of phosphatidylcholine revealed that the proportion of the DELTA4-desaturated products is up to 20times higher in the sn-2 position than in the sn-1 position
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?
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malfunction
enzyme knockdown lines show decreases in the 16:4 and 18:3-9,12,15 acyl groups in lipids, fatty acid profile, overview
physiological function
the enzyme is involved in synthesis of the plastid lipid monogalactosyldiacylglycerol (MGDG) in the green alga Chlamydomonas reinhardtii occuring preferentially as a molecular species containing alpha-linolenic acid 18:3-9,12,15 in the sn-1 position and (4Z,7Z,10Z,13Z)-hexadeca-4,7,10,13-tetraenoic acid (16:4) in the sn-2 position of the glycerol backbone, fatty acid profile, overview
evolution
the enzyme belongs to the front-end desaturases
evolution
-
the enzyme belongs to the front-end desaturases, phylogenetic analysis and tree, overview. Introns appear to have evolved independently among Tpdes genes
evolution
the enzyme belongs to the front-end desaturases, phylogenetic analysis, overview. The HX3HH motif can be used to a priori characterize the enzyme as front-end DELTA4 desaturase
evolution
the enzyme belongs to the front-end desaturases, phylogenetic analysis, overview. The HX3HH motif can be used to a priori characterize the enzyme as front-end DELTA4 desaturase
evolution
the enzyme belongs to the front-end desaturases, phylogenetic analysis, overview. The HX3HH motif can be used to a priori characterize the enzyme as front-end DELTA4 desaturase
evolution
-
the enzyme belongs to the front-end desaturases, phylogenetic analysis, overview. The HX3HH motif can be used to a priori characterize the enzyme as front-end DELTA4 desaturase
-
evolution
-
the enzyme belongs to the front-end desaturases, phylogenetic analysis, overview. The HX3HH motif can be used to a priori characterize the enzyme as front-end DELTA4 desaturase
-
evolution
-
the enzyme belongs to the front-end desaturases, phylogenetic analysis, overview. The HX3HH motif can be used to a priori characterize the enzyme as front-end DELTA4 desaturase
-
evolution
-
the enzyme belongs to the front-end desaturases
-
metabolism
the enzyme is involved in the biosynthesis of docosahexanoic acid
metabolism
-
the enzyme is involved in production of the health beneficial polyunsaturated fatty acid docosahexaenoic acid
metabolism
the enzyme is involved in the pathway for very-long-chain polyunsaturated fatty acid biosynthesis existing in the protozoan. The enzymes involved in polyunsaturated fatty acid biosynthesis (i.e. DELTA6, DELTA8, DELTA5 and DELTA4 desaturases) are named front-end desaturases, because they introduce a double bond between a pre-existent olefinic bond and the carboxyl end of the fatty acid molecule. A complete pathway for very-long-chain polyunsaturated fatty acid biosynthesis is functional in Leishmania major using DELTA6, DELTA5 and DELTA4 desaturases
metabolism
the enzymes involved in polyunsaturated fatty acid biosynthesis (i.e. DELTA6, DELTA8, DELTA5 and DELTA4 desaturases) are named front-end desaturases, because they introduce a double bond between a pre-existent olefinic bond and the carboxyl end of the fatty acid molecule. In trypanosomes, only DELTA4-desaturases are present from a complete pathway for very-long-chain polyunsaturated fatty acid biosynthesis
metabolism
the enzymes involved in polyunsaturated fatty acid biosynthesis (i.e. DELTA6, DELTA8, DELTA5 and DELTA4 desaturases) are named front-end desaturases, because they introduce a double bond between a pre-existent olefinic bond and the carboxyl end of the fatty acid molecule. In trypanosomes, only DELTA4-desaturases are present from a complete pathway for very-long-chain polyunsaturated fatty acid biosynthesis, the enzyme is also able to use n-3 and n-6 fatty acid isomers
metabolism
the enzyme is involved in docosahexaenoic acid synthesis pathway in the teleost Solea senegalensis
metabolism
-
the enzymes involved in polyunsaturated fatty acid biosynthesis (i.e. DELTA6, DELTA8, DELTA5 and DELTA4 desaturases) are named front-end desaturases, because they introduce a double bond between a pre-existent olefinic bond and the carboxyl end of the fatty acid molecule. In trypanosomes, only DELTA4-desaturases are present from a complete pathway for very-long-chain polyunsaturated fatty acid biosynthesis
-
metabolism
-
the enzyme is involved in the biosynthesis of docosahexanoic acid
-
metabolism
-
the enzymes involved in polyunsaturated fatty acid biosynthesis (i.e. DELTA6, DELTA8, DELTA5 and DELTA4 desaturases) are named front-end desaturases, because they introduce a double bond between a pre-existent olefinic bond and the carboxyl end of the fatty acid molecule. In trypanosomes, only DELTA4-desaturases are present from a complete pathway for very-long-chain polyunsaturated fatty acid biosynthesis, the enzyme is also able to use n-3 and n-6 fatty acid isomers
-
metabolism
-
the enzyme is involved in the pathway for very-long-chain polyunsaturated fatty acid biosynthesis existing in the protozoan. The enzymes involved in polyunsaturated fatty acid biosynthesis (i.e. DELTA6, DELTA8, DELTA5 and DELTA4 desaturases) are named front-end desaturases, because they introduce a double bond between a pre-existent olefinic bond and the carboxyl end of the fatty acid molecule. A complete pathway for very-long-chain polyunsaturated fatty acid biosynthesis is functional in Leishmania major using DELTA6, DELTA5 and DELTA4 desaturases
-
additional information
distribution of Egd4p desaturation products into different yeast lipid classes may indicate lipid-dependency
additional information
distribution of Old4p desaturation products into different yeast lipid classes may indicate lipid-dependency
additional information
overproduction of the enzyme in Chlamydomonas not only increases levels of 16:4 acyl groups in cell extracts but specifically increases the total amount of monogalactosyldiacylglycerol, fatty acid profile, overview
additional information
-
distribution of Egd4p desaturation products into different yeast lipid classes may indicate lipid-dependency
-
additional information
-
distribution of Old4p desaturation products into different yeast lipid classes may indicate lipid-dependency
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Tonon, T.; Sayanova, O.; Michaelson, L.V.; Qing, R.; Harvey, D.; Larson, T.R.; Li, Y.; Napier, J.A.; Graham, I.A.
Fatty acid desaturases from the microalga Thalassiosira pseudonana
FEBS J.
272
3401-3412
2005
Thalassiosira pseudonana
brenda
Tripodi, K.E.; Buttigliero, L.V.; Altabe, S.G.; Uttaro, A.D.
Functional characterization of front-end desaturases from trypanosomatids depicts the first polyunsaturated fatty acid biosynthetic pathway from a parasitic protozoan
FEBS J.
273
271-280
2006
Trypanosoma brucei (Q38AQ3), Trypanosoma cruzi (Q4DDJ1), Leishmania major (Q4QFK0), Trypanosoma cruzi CL Brener (Q4DDJ1), Trypanosoma brucei 427 (Q38AQ3), Leishmania major Friedlin (Q4QFK0)
brenda
Tonon, T.; Harvey, D.; Larson, T.R.; Graham, I.A.
Identification of a very long chain polyunsaturated fatty acid DELTA4-desaturase from the microalga Pavlova lutheri
FEBS Lett.
553
440-444
2003
Diacronema lutheri (Q6VPV2), Diacronema lutheri, Diacronema lutheri CCAP 931/1 (Q6VPV2)
brenda
Qiu, X.; Hong, H.; MacKenzie, S.L.
Identification of a DELTA4 fatty acid desaturase from Thraustochytrium sp. involved in the biosynthesis of docosahexanoic acid by heterologous expression in Saccharomyces cerevisiae and Brassica juncea
J. Biol. Chem.
276
31561-31566
2001
Thraustochytrium sp. (Q8S3C0), Thraustochytrium sp. ATCC 21685 (Q8S3C0)
brenda
Zhou, X.R.; Robert, S.S.; Petrie, J.R.; Frampton, D.M., Mansour, M.P.; Blackburn, S.I.; Nichols, P.D.; Green, A.G.; Singh, S.P.
Isolation and characterization of genes from the marine microalga Pavlova salina encoding three front-end desaturases involved in docosahexaenoic acid biosynthesis
Phytochemistry
68
785-796
2007
Rebecca salina (A0PJ29), Rebecca salina
brenda
Meyer, A.; Cirpus, P.; Ott, C.; Schlecker, R.; Zhringer, U.; Heinz, E.
Biosynthesis of docosahexaenoic acid in Euglena gracilis: Biochemical and molecular evidence for the involvement of a DELTA4-fatty acyl group desaturase
Biochemistry
42
9779-9788
2003
Euglena gracilis, Thraustochytrium sp., no activity in Schizochytrium sp., no activity in Crypthecodinium cohnii
brenda
Zuner, S.; Jochum, W.; Bigorowski, T.; Benning, C.
A Cytochrome b5-containing plastid-located fatty acid desaturase from Chlamydomonas reinhardtii
Eukaryot. Cell
11
856-863
2012
Chlamydomonas reinhardtii (I2CYZ4)
brenda
Ahmann, K.; Heilmann, M.; Feussner, I.
Identification of a DELTA4-desaturase from the microalga Ostreococcus lucimarinus
Eur. J. Lipid Sci. Technol.
113
832-840
2011
Ostreococcus sp. 'lucimarinus' (A4RQJ7), Euglena gracilis (Q6WNG7), Euglena gracilis 1224-5/3 (Q6WNG7), Ostreococcus sp. 'lucimarinus' CCE9901 (A4RQJ7)
-
brenda
Morais, S.; Mourente, G.; Martinez, A.; Gras, N.; Tocher, D.R.
Docosahexaenoic acid biosynthesis via fatty acyl elongase and DELTA4-desaturase and its modulation by dietary lipid level and fatty acid composition in a marine vertebrate
Biochim. Biophys. Acta
1851
588-597
2015
Solea senegalensis (G8HYS6)
brenda
Park, H.G.; Park, W.J.; Kothapalli, K.S.; Brenna, J.T.
The fatty acid desaturase 2 (FADS2) gene product catalyzes DELTA4 desaturation to yield n-3 docosahexaenoic acid and n-6 docosapentaenoic acid in human cells
FASEB J.
29
3911-3919
2015
Papio anubis (B8R1K0)
brenda