Any feedback?
Information on EC 1.14.19.31 - acyl-lipid (7-3)-desaturase
for references in articles please use BRENDA:EC1.14.19.31Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.19.31 acyl-lipid (7-3)-desaturaseIUBMB Comments
The enzymes from several algae introduce a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Delta7 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.
Specify your search results
Word Map
- 1.14.19.31
-
desaturation
-
docosahexaenoic
-
polyunsaturated
- pavlova
-
microalgae
-
eicosapentaenoic
-
delta5
-
front-end
-
desaturases
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
2
+
+
2
=
+
+
2
+
2
+
+
2
=
+
+
2
+
2
+
+
2
=
+
+
2
+
2
+
+
2
=
+
+
2
+
2
+
+
2
=
+
2
+
2
+
2
+
+
2
=
+
2
+
2
Synonyms
delta4-desaturase, pldes1, delta4-fatty acid desaturase, psd4des, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DELTA4 desaturase
DELTA4 fatty acid desaturase
DELTA4-desaturase
DELTA4-fatty acid desaturase
Egd4p
Old4p
PlDES1
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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)
-
-
-
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)
-
-
-
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)
-
-
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
(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)
-
-
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
DELTA7 acyl-lipid,ferrocytochrome b5:oxygen oxidoreductase (4,5 cis-dehydrogenating)
The enzymes from several algae introduce a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Delta7 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 [5]. 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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
22:4 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
-
-
-
?
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
Diacronema lutheri CCAP 931/1
-
-
-
?
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
-
-
-
?
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,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
Diacronema lutheri CCAP 931/1
-
-
-
?
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
-
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
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
-
-
?
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
-
-
?
additional information
?
-
the enzyme catalyzes the production of docosahexaenoic acid
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
Ostreococcus sp. ''lucimarinus'' CCE9901
the enzyme catalyzes the production of docosahexaenoic acid
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
additional information
?
-
the enzyme catalyzes the production of docosahexaenoic acid
-
-
?
additional information
?
-
Ostreococcus sp. ''lucimarinus'' CCE9901
the enzyme catalyzes the production of docosahexaenoic acid
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome b5
cytochrome b5 is the primary electron donor for endoplasmic reticulum desaturases. The soluble cytochrome b5 domain corresponds to amino acids 48 to 147
-
cytochrome b5
the enzyme exhibits a cytochrome b5 domain fused to its amino terminus and three histidine boxes that are typically found in front-end desaturases
-
cytochrome b5
the enzyme exhibits a cytochrome b5 domain fused to its amino terminus and three histidine boxes that are typically found in front-end desaturases
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
can be classified as DELTA4 desaturase due to its HX3HH motif; gene Tb10.6k15.3610
UniProt
brenda
can be classified as DELTA4 desaturase due to its HX3HH motif; gene Tb10.6k15.3610
UniProt
brenda
can be classified as DELTA4 desaturase due to its HX3HH motif; gene Tc00.1047053510181.20
UniProt
brenda
can be classified as DELTA4 desaturase due to its HX3HH motif; gene Tc00.1047053510181.20
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
the enzyme is expressed during the exponential phase of growth
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
membrane-bound enzyme, showing all characteristic features of a membrane-bound desaturase, including three histidine boxes and a transit peptide for chloroplast targeting
brenda
the localization of FADS2 in mitochondria, supports the involvement of this organelle in long-chain polyunsaturated fatty acid synthesis
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
enzyme knockdown lines show decreases in the 16:4 and 18:3-9,12,15 acyl groups in lipids, fatty acid profile, overview
metabolism
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
additional information
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
Ostreococcus sp. ''lucimarinus'' CCE9901
-
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
Ostreococcus sp. ''lucimarinus'' CCE9901
-
distribution of Old4p desaturation products into different yeast lipid classes may indicate lipid-dependency
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). D4FAD_CHLRE
516
0
56877
Swiss-Prot
Chloroplast (Reliability: 5)
D4FAD_DIALT
445
3
49062
Swiss-Prot
other Location (Reliability: 2)
D4FAD_EUGGR
541
1
60183
Swiss-Prot
other Location (Reliability: 2)
D4FAD_REBSA
447
3
49307
Swiss-Prot
other Location (Reliability: 5)
D4FAD_THRSP
Thraustochytrium sp
519
4
59119
Swiss-Prot
other Location (Reliability: 1)
A0A1Z5JZZ2_FISSO
617
9
70621
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1Z5JR29_FISSO
617
9
70832
TrEMBL
Secretory Pathway (Reliability: 1)
A4RQJ7_OSTLU
Ostreococcus lucimarinus (strain CCE9901)
459
0
50985
TrEMBL
-
Q38AQ3_TRYB2
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
421
0
47986
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged cytochrome b5 domain (residues 48-147) from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, recombinant functional expression in Saccharomyces cerevisiae strain HH3
expression in MCF-7 human breast cancer cells. MCF-7 cells stably expressing FADS1 and FADS2
gene CrDELTA4FAD, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of GFP-tagged enzyme in Chlamydomonas reinhardtii chloroplasts, recombinant expression of the His-tagged cytochrome b5 domain (resdues 48-147) in Escherichia coli strain BL21(DE3)
gene Egd4, DNA and amino acid sequence determination and analysis, phylogenetic tree, partly codon-optimized version of the cDNA, sequence comparison, recombinant expression in Saccharomyces cerevisiae strain INVSc1 in endoplasmic reticulum membrane,fatty acid analysis, overview. Expression of GFP-tagged enzyme
gene Old4, DNA and amino acid sequence determination and analysis, phylogenetic tree, partly codon-optimized version of the cDNA, sequence comparison, recombinant expression in Saccharomyces cerevisiae strain INVSc1 in endoplasmic reticulum membrane,fatty acid analysis, overview. Expression of GFP-tagged enzyme, GFP-Old4p does not form aggregates in yeast cells and localizes to the endoplasmic reticulum
gene TpdesK, encoded on chromosome 5, the gene has a single intron, phylogenetic analysis and tree, recombinant expression in Saccharomyces cerevisiae strain W303A1
-
heterologous expression in Saccharomyces cerevisiae and Brassica juncea respectively. Introduction of the full-length enzyme into Brassica juncea under the control of the 35S promoter results in the production of (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaeno in leaves when exogenously supplied with (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoic acid
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, recombinant functional expression in Saccharomyces cerevisiae strain HH3
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, recombinant functional expression in Saccharomyces cerevisiae strain HH3
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, recombinant functional expression in Saccharomyces cerevisiae strain HH3
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
dietary vegetable oil induced a significant up-regulation of DELTA4fad transcripts in the liver 6 h after feeding
higher growth temperature increases the expression of front-end desaturase genes
in fasting conditions the effect of lipid level possibly prevails over or interacted with fatty acid composition in regulating the expression of DELTA4fad, which is down-regulated in the liver of fish fed the high lipid diets
Pldes1 expression is 4fold higher during the mid-exponential phase of growth compared to late exponential and stationary phases
the expression is reduced when Pavlova salina is grown at 15°C. The ratio of expression of desaturases in samples grown at 25°C and 20°C, is 5times greater for the DELTA4-desaturase than for the DELTA5-desaturase gene
Pldes1 expression is 4fold higher during the mid-exponential phase of growth compared to late exponential and stationary phases
Pldes1 expression is 4fold higher during the mid-exponential phase of growth compared to late exponential and stationary phases
Diacronema lutheri CCAP 931/1
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.14.19.31)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
