BRENDA - Enzyme Database

Non-redundant contribution of the plastidial FAD8 omega-3 desaturase to glycerolipid unsaturation at different temperatures in Arabidopsis

Roman, A.; Hernandez, M.L.; Soria-Garcia, A.; Lopez-Gomollon, S.; Lagunas, B.; Picorel, R.; Martinez-Rivas, J.M.; Alfonso, M.; Mol. Plant 8, 1599-1611 (2015)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.14.19.35
gene FAD7, DNA and amino acid sequence determination and analysis, genotyping of wild-type and mutants; gene FAD8, DNA and amino acid sequence determination and analysis, genotyping of wild-type and mutants. Recombinant expression of AtFAD8-YFP fusion protein in stable transgenic Arabidopsis thaliana lines and transiently in Nicotinana benthamiana leaves, overexpression of YFP-tagged fad8 in Arabidosis thaliana results in increased 18:3 trienoic fatty acid levels in phospholipids but not in galactolipids
Arabidopsis thaliana
Engineering
EC Number
Amino acid exchange
Commentary
Organism
1.14.19.35
C103Y
mutation occuring in the fad3 fad7 fad8 triple mutant
Arabidopsis thaliana
1.14.19.35
additional information
construction of a tandem T-DNA FAD7 insertion omega-3 desaturase mutant line SALK_147096C/fad7i. Construction of double fad7/fad8 and triple fad3/fad7/fad8 mutants. Fatty acid composition of total leaf lipids from wild-type and the different mutant lines grown at 22°C, overview. Mutant fad7i maintains 74% of 18:3 production with respect to Col-0 while only 23% of 16:3 synthesis is maintained in this mutant. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable; construction of a tandem T-DNA FAD8 insertion omega-3 desaturase mutant line SALK_093590 with no phenotype at 22°C. Construction of double fad7/fad8 and triple fad3/fad7/fad8 mutants. FAD8-YFP overexpressing lines show a specific increase in 18:3 fatty acids at 22°C. Fatty acid composition of total leaf lipids from wild-type and the different mutant lines grown at 22°C, overview. Disruption of the AtFAD8 gene in mutant fad8i results in trienoic fatty acid levels almost similar to those from wild-type Col-0. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable
Arabidopsis thaliana
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.14.19.35
chloroplast envelope
enzymes FAD8 and FAD7 might be located in close vicinity in the envelope membrane; enzymes FAD8 and FAD7 might be located in close vicinity in the envelope membrane
Arabidopsis thaliana
9941
-
1.14.19.35
membrane
;
Arabidopsis thaliana
16020
-
1.14.19.35
additional information
localization study of recombinantly expressed fluorescence-tagged enzymes, overview; localization study of recombinantly expressed fluorescence-tagged enzymes, overview
Arabidopsis thaliana
-
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.14.19.35
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
Arabidopsis thaliana
-
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
1.14.19.35
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
Arabidopsis thaliana Col-0
-
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
1.14.19.35
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
Arabidopsis thaliana
-
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
1.14.19.35
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
Arabidopsis thaliana Col-0
-
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
1.14.19.35
additional information
Arabidopsis thaliana
enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
?
-
-
-
1.14.19.35
additional information
Arabidopsis thaliana Col-0
enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.14.19.35
Arabidopsis thaliana
P46310
gene fad7
-
1.14.19.35
Arabidopsis thaliana
P48622
gene FAD8
-
1.14.19.35
Arabidopsis thaliana Col-0
P46310
gene fad7
-
1.14.19.35
Arabidopsis thaliana Col-0
P48622
gene FAD8
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
1.14.19.35
leaf
;
Arabidopsis thaliana
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.19.35
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
-
734740
Arabidopsis thaliana
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
1.14.19.35
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
-
734740
Arabidopsis thaliana Col-0
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
1.14.19.35
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
-
734740
Arabidopsis thaliana
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
1.14.19.35
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
-
734740
Arabidopsis thaliana Col-0
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
1.14.19.35
additional information
enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
734740
Arabidopsis thaliana
?
-
-
-
-
1.14.19.35
additional information
enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
734740
Arabidopsis thaliana Col-0
?
-
-
-
-
Temperature Range [°C]
EC Number
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
1.14.19.35
8
30
active at; active at
Arabidopsis thaliana
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.14.19.35
Ferredoxin
required; required
Arabidopsis thaliana
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.14.19.35
gene FAD7, DNA and amino acid sequence determination and analysis, genotyping of wild-type and mutants
Arabidopsis thaliana
1.14.19.35
gene FAD8, DNA and amino acid sequence determination and analysis, genotyping of wild-type and mutants. Recombinant expression of AtFAD8-YFP fusion protein in stable transgenic Arabidopsis thaliana lines and transiently in Nicotinana benthamiana leaves, overexpression of YFP-tagged fad8 in Arabidosis thaliana results in increased 18:3 trienoic fatty acid levels in phospholipids but not in galactolipids
Arabidopsis thaliana
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.14.19.35
Ferredoxin
required
Arabidopsis thaliana
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
1.14.19.35
C103Y
mutation occuring in the fad3 fad7 fad8 triple mutant
Arabidopsis thaliana
1.14.19.35
additional information
construction of a tandem T-DNA FAD7 insertion omega-3 desaturase mutant line SALK_147096C/fad7i. Construction of double fad7/fad8 and triple fad3/fad7/fad8 mutants. Fatty acid composition of total leaf lipids from wild-type and the different mutant lines grown at 22°C, overview. Mutant fad7i maintains 74% of 18:3 production with respect to Col-0 while only 23% of 16:3 synthesis is maintained in this mutant. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable
Arabidopsis thaliana
1.14.19.35
additional information
construction of a tandem T-DNA FAD8 insertion omega-3 desaturase mutant line SALK_093590 with no phenotype at 22°C. Construction of double fad7/fad8 and triple fad3/fad7/fad8 mutants. FAD8-YFP overexpressing lines show a specific increase in 18:3 fatty acids at 22°C. Fatty acid composition of total leaf lipids from wild-type and the different mutant lines grown at 22°C, overview. Disruption of the AtFAD8 gene in mutant fad8i results in trienoic fatty acid levels almost similar to those from wild-type Col-0. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable
Arabidopsis thaliana
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.14.19.35
chloroplast envelope
enzymes FAD8 and FAD7 might be located in close vicinity in the envelope membrane
Arabidopsis thaliana
9941
-
1.14.19.35
membrane
-
Arabidopsis thaliana
16020
-
1.14.19.35
additional information
localization study of recombinantly expressed fluorescence-tagged enzymes, overview
Arabidopsis thaliana
-
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.14.19.35
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
Arabidopsis thaliana
-
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
1.14.19.35
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
Arabidopsis thaliana Col-0
-
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
1.14.19.35
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
Arabidopsis thaliana
-
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
1.14.19.35
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
Arabidopsis thaliana Col-0
-
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
?
1.14.19.35
additional information
Arabidopsis thaliana
enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
?
-
-
-
1.14.19.35
additional information
Arabidopsis thaliana Col-0
enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
?
-
-
-
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
1.14.19.35
leaf
-
Arabidopsis thaliana
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.19.35
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
-
734740
Arabidopsis thaliana
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
1.14.19.35
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
-
734740
Arabidopsis thaliana Col-0
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
1.14.19.35
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
-
734740
Arabidopsis thaliana
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
1.14.19.35
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
-
734740
Arabidopsis thaliana Col-0
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
1.14.19.35
additional information
enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
734740
Arabidopsis thaliana
?
-
-
-
-
1.14.19.35
additional information
enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
734740
Arabidopsis thaliana Col-0
?
-
-
-
-
Temperature Range [°C] (protein specific)
EC Number
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
1.14.19.35
8
30
active at
Arabidopsis thaliana
General Information
EC Number
General Information
Commentary
Organism
1.14.19.35
malfunction
a fad8 mutant shows no significant changes in its fatty acid profile at a control (22°C) temperature, while at lower temperature (15°C) the mutant shows a phenotype, leaf lipid analysis, overview; mutant fad7i maintains 74% of 18:3 production with respect to Col-0 while only 23% of 16:3 synthesis is maintained in this mutant. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable. After disruption of the AtFAD7 gene, enzyme FAD8 enzymatic activity is able to maintain, at least partially (43.7%), the amount of 18:3 and to a much lesser extent that of 16:3 (23.2%) at 22°C
Arabidopsis thaliana
1.14.19.35
additional information
FAD8-YFP over-expressing lines show a specific increase in 18:3 fatty acids at 22°C. Residue 103 is part of the first His box essential for desaturase function
Arabidopsis thaliana
1.14.19.35
physiological function
plastidial omega-3 desaturases FAD7 and FAD8 are major contributors to trienoic fatty acid biosynthesis in the leaves of Arabidopsis thaliana plants. Enzyme FAD8 partially compensates the disruption of the AtFAD7 gene at 22°C; plastidial omega-3 desaturases FAD7 and FAD8 are major contributors to trienoic fatty acid biosynthesis in the leaves of Arabidopsis thaliana plants. Enzyme FAD8 partially compensates the disruption of the AtFAD7 gene at 22°C, indicating that enzyme FAD8 is active at this growth temperature, contrasting to previous observations that circumscribe the FAD8 activity at low temperatures
Arabidopsis thaliana
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.14.19.35
malfunction
mutant fad7i maintains 74% of 18:3 production with respect to Col-0 while only 23% of 16:3 synthesis is maintained in this mutant. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable. After disruption of the AtFAD7 gene, enzyme FAD8 enzymatic activity is able to maintain, at least partially (43.7%), the amount of 18:3 and to a much lesser extent that of 16:3 (23.2%) at 22°C
Arabidopsis thaliana
1.14.19.35
malfunction
a fad8 mutant shows no significant changes in its fatty acid profile at a control (22°C) temperature, while at lower temperature (15°C) the mutant shows a phenotype, leaf lipid analysis, overview
Arabidopsis thaliana
1.14.19.35
additional information
FAD8-YFP over-expressing lines show a specific increase in 18:3 fatty acids at 22°C. Residue 103 is part of the first His box essential for desaturase function
Arabidopsis thaliana
1.14.19.35
physiological function
plastidial omega-3 desaturases FAD7 and FAD8 are major contributors to trienoic fatty acid biosynthesis in the leaves of Arabidopsis thaliana plants. Enzyme FAD8 partially compensates the disruption of the AtFAD7 gene at 22°C
Arabidopsis thaliana
1.14.19.35
physiological function
plastidial omega-3 desaturases FAD7 and FAD8 are major contributors to trienoic fatty acid biosynthesis in the leaves of Arabidopsis thaliana plants. Enzyme FAD8 partially compensates the disruption of the AtFAD7 gene at 22°C, indicating that enzyme FAD8 is active at this growth temperature, contrasting to previous observations that circumscribe the FAD8 activity at low temperatures
Arabidopsis thaliana