1.14.19.31: acyl-lipid (7-3)-desaturase
This is an abbreviated version!
For detailed information about acyl-lipid (7-3)-desaturase, go to the full flat file.
Word Map on EC 1.14.19.31
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1.14.19.31
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desaturation
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docosahexaenoic
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polyunsaturated
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pavlova
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microalgae
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eicosapentaenoic
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delta5
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front-end
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desaturases
- 1.14.19.31
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desaturation
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docosahexaenoic
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polyunsaturated
- pavlova
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microalgae
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eicosapentaenoic
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delta5
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front-end
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desaturases
Reaction
+ 2 ferrocytochrome b5 + + 2 H+ = + 2 ferricytochrome b5 + 2 H2O
Synonyms
CrDELTA4FAD, DELTA4 desaturase, DELTA4 fatty acid desaturase, DELTA4-desaturase, DELTA4-fatty acid desaturase, DELTA4Fad, Egd4p, FADS2, MGDG-specific DELTA4-desaturase, monogalactosyldiacylglycerol-specific DELTA4-desaturase, Old4p, PlDES1, PsD4Des
ECTree
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Substrates Products
Substrates Products on EC 1.14.19.31 - acyl-lipid (7-3)-desaturase
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REACTION DIAGRAM
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
22:5 DELTA4,7,10,13,16-docosapentaenoic acid + 2 ferricytochrome b5 + 2 H2O
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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
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?
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
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?
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
Diacronema lutheri CCAP 931/1
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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)-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
Diacronema lutheri CCAP 931/1
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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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?
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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?
docosa-4,7,10,13,16,19-hexaenoic acid + 2 ferricytochrome b5 + 2 H2O
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?
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
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?
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
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?
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
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?
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
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?
docosa-4,7,10,13,16-pentaenoic acid + 2 ferricytochrome b5 + 2 H2O
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?
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
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?
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
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?
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
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the recombinant His-tagged cytochrome b5 domain of the enzyme is active in vitro
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additional information
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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
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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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Ostreococcus sp. ''lucimarinus'' CCE9901
the enzyme catalyzes the production of docosahexaenoic acid
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additional information
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Ostreococcus sp. ''lucimarinus'' CCE9901
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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