HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.14.19.35 - sn-2 acyl-lipid omega-3 desaturase (ferredoxin)
Word Map on EC 1.14.19.35
- 1.14.19.35
- chloroplast
-
alpha-linolenic
-
trienoic
-
desaturation
-
linolenic
-
polyunsaturated
- plastidial
- jasmonate
-
18-carbon
-
delta12
-
pufas
-
wound-induced
-
glycerolipids
-
wound-responsive
- biotechnology
- agriculture
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.14.19.35
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
sn-2 acyl-lipid omega-3 desaturase (ferredoxin)
-
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)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+ = a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(1)
-
-
-
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+ = an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(2)
-
-
-
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+ = a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
(1)
-
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+ = a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
-
-
-
-
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+ = an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
(2)
-
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+ = an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (13,14 cis-dehydrogenating)
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 omega-3 desaturase (cytochrome b5) and EC 1.14.19.36, sn-1 acyl-lipid omega-3 desaturase (ferredoxin).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
cvs. Gerry (cold sensitive) and T47657 (moderately cold tolerant), gene fad7
Q7XX7I9
UniProt
gene fad7
SwissProt
gene fad7
SwissProt
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
A8DTI8, C67ZGG8
three histidine clusters characteristic of fatty acid desaturases, a putative chloroplast transit peptide in the N-terminal, and three putative transmembrane domains are identified in the enzyme sequence; three histidine clusters characteristic of fatty acid desaturases, a putative chloroplast transit peptide in the N-terminal, and three putative transmembrane domains are identified in the enzyme sequence
malfunction
metabolism
Q7XX7I9
glycine betaine protects tomato plants at low temperature by inducing fatty acid desaturase7 and lipoxygenase gene expression, providing protection against cold stress in tomato plants which might be related to the desaturation process of lipids leading to increased membrane stability and/or induction of other genes related to stress defense mechanisms via octadecanoid pathway or lipid peroxidation products
physiological function
additional information
malfunction
-
mutations at the fad7 locus of Arabidopsis thaliana cause decreased desaturation of dienoic fatty acids in chloroplast lipids in plants grown at elevated temperatures
malfunction
in a genetic background that is wild type at the FAD7 locus, the fad8 mutation has no detedable effed on overall leaf fatty acid composition irrespective of the temperature at which plants are grown. However, fatty acid analyses of individual leaf lipids reveales small decreases in the levels of 18:3 in two chloroplast lipids. In fad8 plants grown at 22°C, phosphatidylglycerol contains 22.5% 18:3 compared with 33.5% in wild type Arabidopsis; mutations at the fad7 locus of Arabidopsis thaliana cause decreased desaturation of dienoic fatty acids in chloroplast lipids in plants grown at elevated temperatures
malfunction
the omega-3 fatty acids hexadecatrienoic acid (C16:3n3), hexadecatetraenoic acid (C16:4),and alpha-linolenic acid (C18:3n3) are not detected in the CC-620 strain, phenotype and fatty acid composition of the omega-3 fatty acid deficiency in strain CC-620 due to the missense mutation detected in gene CrFAD7, complementation by the wild-type enzyme, overview
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
malfunction
-
in contrast to avirulent petiole exudates from wild-type plants, avirulent petiole exudates from fad7, sfd1 and sfd2 mutants are unable to activate systemic acquired resistance when applied to wild-type plants. The SAR-inducing activity is reconstituted by mixing avirulent petiole exudates collected from fad7 and sfd1 with avirulent petiole exudate from the SAR-deficient dir1 mutant
malfunction
-
comparison of trienoic fatty acid levels in wild-type and fad7 mutant leaves, an increase occurs in the wild-type at 15-26°C during maturation mainly due to galactolipids enriched in plastid membranes, while in mutant leaves at 26°C the levels decrease with leaf maturation, overview
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; comparison of trienoic fatty acid levels in wild-type and fad7 mutant leaves, an increase occurs in the wild-type at 15-26°C during maturation mainly due to galactolipids enriched in plastid membranes, while in mutant leaves at 26°C the levels decrease with leaf maturation, 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
-
physiological function
Thr residue located in the fourth transmembrane domain of fatty acid desaturase 7 (FAD7) that is essential for the biosynthesis of omega-3 fatty acids in Chlamydomonas reinhardtii, Thr286 is essential for the maintaining the catalytic structure of the enzyme
physiological function
Q7XX7I9
fatty acid desaturases catalyze the introduction of double bonds into the aliphatic tails of fatty acids which affects plant responses against a variety of stresses via the enhancement of membrane fluidity
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
physiological function
-
the plastidial omega-3 fatty acid desaturase FAD7 catalyzes the desaturation of dienoic fatty acids in membrane lipids
physiological function
-
FAD7-synthesized lipids provide fatty acids for synthesis of jasmonic acid. Petiole exudates collected from Arabidopsis leaves inoculated with an avirulent Pseudomonas syringae strain promote systemic acquired resistance, SAR, when applied to Arabidopsis thaliana. Arabidopsis fatty acid desaturase7, suppressor of fatty acid desaturase deficiency 1 (SFD1), and SFD2 genes are required for accumulation of the SAR-inducing activity. Jasmonic acid and methyljasmonic acid with avirulent petiole exudate from fad7 and sfd1 does not reconstitute the SAR-inducing activity. A plastid glycerolipid-dependent factor is required in avirulent petiole exudate along with the DIR1-encoded lipid transfer protein for long-distance signaling in systemic acquired resistance
physiological function
-
the role of fad8 is to provide increased omega3 desaturase activity in plants that are exposed to low growth temperature
physiological function
-
role of omega-3 fatty acid desaturases in the positive regulation of the level of trienoic fatty acids during leaf cell maturation
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; role of omega-3 fatty acid desaturases in the positive regulation of the level of trienoic fatty acids during leaf cell maturation; the plastidial omega-3 fatty acid desaturase FAD7 catalyzes the desaturation of dienoic fatty acids in membrane lipids; the role of fad8 is to provide increased omega3 desaturase activity in plants that are exposed to low growth temperature
-
additional information
-
elevated temperatures lead to decreases in leaf trienoic fatty acid level due to temperature sensitivity of enzyme FAD8 activity, the C-terminal region of FAD8 desaturase is essential for destabilization at high temperature (22°C). The C-terminal coding region of FAD8 is sufficient to suppress the accumulation of plastidial omega-3 desaturase protein at high temperature, overview
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
additional information
-
wounding changes the spatial expression pattern of the FAD7 gene
additional information
-
ectopic overexpression of FAD8 induces an increased ratio mainly in the plastidic lipids. Overexpression of FAD8 leads to increased tolerance to osmotic stress (imposed by two different agents, PEG 8000 and sorbitol) and decreased tolerance to heat stress (35°C), at both cellular and whole-plant levels. FAD8-overexpressing plants can regain growth after withholding water for a duration that severely impaires the ability of wild-type plants to recover from the stress. Fatty acid composition of leaf polar lipids of wild-type and transgenic plants, overview
additional information
-
increased levels of trienoic fatty acids in genetically engineered plants enhance cold tolerance
additional information
-
ectopic overexpression of FAD8 induces an increased ratio mainly in the plastidic lipids. Overexpression of FAD8 leads to increased tolerance to osmotic stress (imposed by two different agents, PEG 8000 and sorbitol) and decreased tolerance to heat stress (35°C), at both cellular and whole-plant levels. FAD8-overexpressing plants can regain growth after withholding water for a duration that severely impaires the ability of wild-type plants to recover from the stress. Fatty acid composition of leaf polar lipids of wild-type and transgenic plants, overview; elevated temperatures lead to decreases in leaf trienoic fatty acid level due to temperature sensitivity of enzyme FAD8 activity, the C-terminal region of FAD8 desaturase is essential for destabilization at high temperature (22°C). The C-terminal coding region of FAD8 is sufficient to suppress the accumulation of plastidial omega-3 desaturase protein at high temperature, overview; 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; increased levels of trienoic fatty acids in genetically engineered plants enhance cold tolerance; wounding changes the spatial expression pattern of the FAD7 gene
-
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
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
-
-
-
?
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
?
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
?
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Q7XX7I9
-
-
-
?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
-
-
-
?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
(9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid] i.e. linoleoyl-[glycerolipid]
(9Z,12Z,15Z)-octadeca-9,12,15-trienoyl-[glycerolipid] i.e. alpha-linolenoyl-[glycerolipid]
-
?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
A8DTI8, C67ZGG8
-
-
-
?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Q7XX7I9
-
-
-
?
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
-
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
?
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
?
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Q7XX7I9
-
-
-
?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
A8DTI8, C67ZGG8
-
-
-
?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Q7XX7I9
-
-
-
?
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
-
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
required for activity in the chloroplasts, ferredoxin is required for recombinantly expressed HaFAD7 activity but not for protein stability and accumulation in yeast
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
elevated temperatures lead to decreases in leaf trienoic fatty acid level due to temperature sensitivity of enzyme FAD8 activity
-
additional information
Q7XX7I9
effect of cold stress treatment on cold sensitive and cold tolerant plants presence or absence of glycine betaine, detailed overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
elevated temperatures lead to decreases in leaf trienoic fatty acid level due to temperature sensitivity of enzyme FAD8 activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.06
calculated from sequence. The proteolytic processing of the prepeptide would produce a 392 amino acid protein with a pI of 7.3
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
gene fad7 is expressed in leaves, but not in roots at normal temperature- and low temperature-growth conditions; gene fad8 is expressed in leaves, but not in roots at normal temperature- and low temperature-growth conditions
-
gene fad7 is expressed in leaves, but not in roots at normal temperature- and low temperature-growth conditions; gene fad8 is expressed in leaves, but not in roots at normal temperature- and low temperature-growth conditions
-
induction at high salt condition; induction at high salt condition
additional information
-
tissue-specific expression; tissue-specific expression
additional information
no or little expression is detected in mature seeds, roots and stems
additional information
OO24626
tissue-specific expression; tissue-specific expression
additional information
the overall level of ZmFAD7 transcript is increased after exposure to 5°C but not above 10°C. ZmFAD7 is dominantly expressed at 25°C, moderate expression at 15°C, no expression at 5°C; the overall level of ZmFAD8 transcript is increased after exposure to 5°C but not above 10°C. ZmFAD8 is dominantly expressed at 5°C, moderate expression at 15°C, no expression at 25°C
additional information
the overall level of ZmFAD7 transcript is increased after exposure to 5°C but not above 10°C. ZmFAD7 is dominantly expressed at 25°C, moderate expression at 15°C, no expression at 5°C; the overall level of ZmFAD8 transcript is increased after exposure to 5°C but not above 10°C. ZmFAD8 is dominantly expressed at 5°C, moderate expression at 15°C, no expression at 25°C
additional information
-
the overall level of ZmFAD7 transcript is increased after exposure to 5°C but not above 10°C. ZmFAD7 is dominantly expressed at 25°C, moderate expression at 15°C, no expression at 5°C; the overall level of ZmFAD8 transcript is increased after exposure to 5°C but not above 10°C. ZmFAD8 is dominantly expressed at 5°C, moderate expression at 15°C, no expression at 25°C
-
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
additional information
-
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
-
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
-
-
; membrane-associated; membrane-associated
-
additional information
-
localization study of recombinantly expressed fluorescence-tagged enzymes, overview; localization study of recombinantly expressed fluorescence-tagged enzymes, overview
-
additional information
-
localization study of recombinantly expressed fluorescence-tagged enzymes, overview; localization study of recombinantly expressed fluorescence-tagged enzymes, overview
-
-
additional information
immunohistochemic localization analysis, overview
-
additional information
ubiquitous expression, tissue-specific levels; ubiquitous expression, tissue-specific levels
-
additional information
C67ZGG8
ubiquitous expression, tissue-specific levels; ubiquitous expression, tissue-specific levels
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50800
x * 50800, calculated from sequence. The proteolytic processing of the prepeptide would produce a 392 amino acid protein with a molecular mass of around 452000 Da
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 50800, calculated from sequence. The proteolytic processing of the prepeptide would produce a 392 amino acid protein with a molecular mass of around 452000 Da
additional information
three histidine clusters characteristic of fatty acid desaturases, a putative chloroplast transit peptide in the N-terminal, and three putative transmembrane domains are identified in the enzyme sequence; three histidine clusters characteristic of fatty acid desaturases, a putative chloroplast transit peptide in the N-terminal, and three putative transmembrane domains are identified in the enzyme sequence
additional information
C67ZGG8
three histidine clusters characteristic of fatty acid desaturases, a putative chloroplast transit peptide in the N-terminal, and three putative transmembrane domains are identified in the enzyme sequence; three histidine clusters characteristic of fatty acid desaturases, a putative chloroplast transit peptide in the N-terminal, and three putative transmembrane domains are identified in the enzyme sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene fad7, construction of cDNA and genomic DNA libraries, and screening using Arabidopsis thaliana gene fad7 as template, the genomic clone has 8 exons, DNA and amino acid sequence determination and analysis, genomic organization, phylogenetic analysis; gene fad8, construction of cDNA and genomic DNA libraries, and screening using Arabidopsis thaliana gene fad7 as template, the genomic clone has 7 exons, DNA and amino acid sequence determination and analysis, genomic organization, phylogenetic analysis
gene fad7, DNA and amino acid sequence determination and analysis using gene fad3 as template. The fad7 and fad8 gene products are functionally equivalent, although the two genes share only about 75% nucleotide identity; gene fad8, DNA and amino acid sequence determination and analysis using gene fad3 as template, constitutive expression of the fad8 cDNA in transgenic plants of a fad7 mutant JBl01, via Agrobacterium turnefaciens C58 (pGV3101) containing plasmid pBI/fad8 or pBIl2l, results in genetic complementation of the mutation, indicating that the fad7 and fad8 gene products are functionally equivalent. Expression of the fad8 cDNA in transgenic plants often results in the co-suppression of both the endogenous fad7 and fad8 genes in spite of the fact that these two genes share only about 75% nucleotide identity
-
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
-
gene FAD7, DNA and amino acid sequence determination and analysis, genotyping, expression of T286 enzyme mutants
gene fad7, DNA and amino acid sequence determination and analysis; gene fad8, DNA and amino acid sequence determination and analysis
A8DTI8, C67ZGG8
gene fad7, enzyme expression analysis, recombinant expression of fad7 in wild-type Rschew ecotype WF11 cell line and enzyme-deficient mutant cell line SH10 derived from JB101/Col-0
-
gene FAD7, expression of the -825 Arabidopsis FAD7 promoter-P-glucuronidase fusion gene in Nicotiana tabacum cv. W38
-
gene fad7, expression of wild-type and chimeric mutant enzymes with or without a c-Myc epitope tag in transgenic Arabidopsis thaliana plants; gene fad8, expression of wild-type and chimeric mutant enzymes with or without a c-Myc epitope tag in transgenic Arabidopsis thaliana plants
-
gene fad7, gene expression profiles, overview. The FAD7 gene expression is differentially regulated in tomato varieties Gerry and T47657 under the effect of cold stress in the short and long term
Q7XX7I9
gene fad7, recombinant expression in Nicotiana tabacum cv. SR1 leaves, that contain increased levels of 16:3 and 18:3 fatty acids, and correspondingly decreased levels of their precursors, hexadecadienoic and linoleic acids, via using Agrobacterium tumefaciens C58ClRif (pGV2280) containing the plasmid pTiDES7 or p501-17. The expression of FAD7 leads to reduced suppression of leaf growth at 1°C compared to wild-type plants. The low-temperature-induced chlorosis is also much reduced in the plants transformed with the fad7 gene. Control growth at 25°C
-
gene fad7, sequence comparison with FAD3, recombinant expression in Saccharomyces cerevisiae strain W303-1A, plastidial omega3-fatty acid desaturase contains the signalling determinants required for targeting to, and retention in, the endoplasmic reticulum membrane in Saccharomyces cerevisiae but requires co-expressed ferredoxin for activity. Heterologous enzyme expression in yeast shows low activity in contrast to similar expression of microsomal FAD3 omega 3-desaturases. Expression of enzyme variants N-terminally tagged with HA, and/or anchor domains ELO or FAE, and containing a KKNL motif at the C-terminus. Deletion of the endogenous KEK C-terminal motif results in dramatically reduced accumulation of FAD7-HA. Coexpression of ferredoxin
gene fad7, the promoter sequence of gene fad7 contains several short sequence cis-elements and the -825 bp regulatory region, analysis, overview
-
gene fad8, recombinant expression in Nicotiana tabacum BY-2 cells and in transgenic tobacco plants via Agrobacterium-mediated transformation. Co-expression of Arabidopsis thaliana FAD8 and Brassica napus FAD3, EC 1.14.19.25, under the control of the 35S CaMV promoter leads to increase in 18:3, which is compensated mainly by the decrease in 18:2, but is also accompanied by a decrease in oleic acid (18:1). Additionally, there is a small but significant decrease in stearic acid (18:0) which seems to be compensated by an increase in palmitic acid (16:0). In the BY-2-FAD8 cells, the ratio of 18:3 to 18:2 is about twofold higher than that in the BY-2 cells. Fatty acid composition of leaf polar lipids of wild-type and transgenic plants, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activation of the FAD7 promoter by local wounding treatments. Wounding induces the expression of the FAD7 gene in rosette leaves (2fold), stems (29fold), and roots(10fold). Significant induction by wounding is observed in the overall tissues of stems and includes trichomes, the epidermis, cortex, vascular system, and the pith of the parenchyma. Strong promoter activity is found preferentially in the vascular tissues of wounded roots. Wound activation of the FAD7 promoter in roots occurs via the octadecanoid pathway, inhibitors salicylic acid and n-propyl gallate strongly suppress the wound activation of the FAD7 promoter in roots but not in leaves or stems. Light attenuates the wound-inducing activity of the FAD7 promoter in roots, although in unwounded roots, illumination does not affect the expression of the FAD7 gene. In unwounded plants, exogenously applied methyl jasmonate activates the FAD7 promoter in roots, whereas it represses FAD7 promoter activity in leaves
-
activation of the FAD7 promoter by local wounding treatments. Wounding induces the expression of the FAD7 gene in rosette leaves (2fold), stems (29fold), and roots(10fold). Significant induction by wounding is observed in the overall tissues of stems and includes trichomes, the epidermis, cortex, vascular system, and the pith of the parenchyma. Strong promoter activity is found preferentially in the vascular tissues of wounded roots. Wound activation of the FAD7 promoter in roots occurs via the octadecanoid pathway, inhibitors salicylic acid and n-propyl gallate strongly suppress the wound activation of the FAD7 promoter in roots but not in leaves or stems. Light attenuates the wound-inducing activity of the FAD7 promoter in roots, although in unwounded roots, illumination does not affect the expression of the FAD7 gene. In unwounded plants, exogenously applied methyl jasmonate activates the FAD7 promoter in roots, whereas it represses FAD7 promoter activity in leaves; the steady-state level of fad8 mRNA is strongly increased in plants grown at low temperature
-
-
FAD7 is up-regulated by wounding but not by low temperature. Total fatty acid and linolenic acid content are higher both, in wounded and intact leaves of plants exposed to low temperature; FAD8 is up-regulated by cold stress but not by wounding. Total fatty acid and linolenic acid content are higher both, in wounded and intact leaves of plants exposed to low temperature
A8DTI8, C67ZGG8
gene fad7 is rapidly induced in elicitor-treated cell culture leading to an accumulation of mRNA in leaves and as well in fungal infection sites in leaf buds, pathogen invasion induces the enzyme
-
glycine betaine induces the enzyme expression in tomato plants at low temperature
Q7XX7I9
high-salt treatment induces the accumulation of the ZmFAD7 transcript in roots but drought and abscisic acid have no effect on its expression. Cycloheximide induces the accumulation of the ZmFAD7 transcript in roots; high-salt treatment induces the accumulation of the ZmFAD8 transcript in roots but drought and abscisic acid have no effect on its expression
in unwounded plants, exogenously applied methyl jasmonate activates the FAD7 promoter in roots, whereas it represses FAD7 promoter activity in leaves
salt stress induces the enzyme FAD7 in roots; salt stress induces the enzyme FAD8 in roots, the enzyme is induced in leaves by low temperature below 20°C
OO24626
temperature-sensitive FAD8 expression
the enzyme is induced by wounding in leaves, stems and roots, jasmonic acid induces the enzyme in roots
-
the steady-state level of fad8 mRNA is strongly increased in plants grown at low temperature
-
wounding induces the enzyme expression in leaves and roots. The enzyme FAD8 is induced by cold temperatures below 20°C; wounding induces the FAD7 enzyme expression in leaves and roots. Light-responsive gene fad7 shows light-induced accumulation in rosette leaves
-
high-salt treatment induces the accumulation of the ZmFAD7 transcript in roots but drought and abscisic acid have no effect on its expression. Cycloheximide induces the accumulation of the ZmFAD7 transcript in roots; high-salt treatment induces the accumulation of the ZmFAD8 transcript in roots but drought and abscisic acid have no effect on its expression
high-salt treatment induces the accumulation of the ZmFAD7 transcript in roots but drought and abscisic acid have no effect on its expression. Cycloheximide induces the accumulation of the ZmFAD7 transcript in roots; high-salt treatment induces the accumulation of the ZmFAD8 transcript in roots but drought and abscisic acid have no effect on its expression
-
-
in unwounded plants, exogenously applied methyl jasmonate activates the FAD7 promoter in roots, whereas it represses FAD7 promoter activity in leaves
-
in unwounded plants, exogenously applied methyl jasmonate activates the FAD7 promoter in roots, whereas it represses FAD7 promoter activity in leaves
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W149stop
-
the fads-1 mutation creates a premature stop codon 149 amino acids from the N-terminal end of the fad8 open reading frame, the mutation results in a complete loss of fad8 activity
W149stop
-
the fads-1 mutation creates a premature stop codon 149 amino acids from the N-terminal end of the fad8 open reading frame, the mutation results in a complete loss of fad8 activity
-
T286C
site-directed mutagenesis, omega3-fatty acid deficiency mutant
T286G
site-directed mutagenesis, omega3-fatty acid deficiency mutant
T286H
site-directed mutagenesis, omega3-fatty acid deficiency mutant
T286N
naturally occuring mutation causing omega3-fatty acid deficiency in strain CC-620, that can be recovered by overexpression of the wild-type enzyme from strain CC-125
T286S
site-directed mutagenesis, the mutant shows partially reduced enzyme activity
T286Y
site-directed mutagenesis, omega3-fatty acid deficiency mutant
additional information
additional information
-
construction of a fad7/fad8 double mutant with reduced overall levels of trienoic fatty acids in leaf tissues. A series of FAD7-FAD8 chimeric genes, each encoding a functional plastidial omega-3 desaturase, are introduced into the Arabidopsis thaliana fad7/fad8 double mutant, structures, overview. All transformants show an unaltered temperature response, and none of the transformants exhibit an exceptional phenotype; construction of a fad7/fad8 double mutant with reduced overall levels of trienoic fatty acids in leaf tissues. A series of FAD7-FAD8 chimeric genes, each encoding a functional plastidial omega-3 desaturase, are introduced into the Arabidopsis thaliana fad7/fad8 double mutant, structures, overview. All transformants show an unaltered temperature response, and none of the transformants exhibit an exceptional phenotype
additional information
-
the fad7-1 mutant JB101 is deficient of plastid omega-3 desaturase FAD7 enzyme activity, the defect is due to mRNA destabilization, not deregulation
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
additional information
-
recombinant overexpression of FAD8 increases tolerance to drought in tobacco plants and to osmotic stress in cultured cells. Ectopic overexpression of FAD8 induces an increased ratio mainly in the plastidic lipids
additional information
-
constitutive expression of the fad8 cDNA in transgenic plants of a fad7 mutant JBl01, via Agrobacterium turnefaciens C58 (pGV3101) containing plasmid pBI/fad8 or pBIl2l, results in genetic complementation of the mutation, indicating that the fad7 and fad8 gene products are functionally equivalent. Expression of the fad8 cDNA in transgenic plants often results in the co-suppression of both the endogenous fad7 and fad8 genes in spite of the fact that these two genes share only about 75% nucleotide identity
additional information
-
generation of the fad7 knockout mutant line JB101
additional information
-
constitutive expression of the fad8 cDNA in transgenic plants of a fad7 mutant JBl01, via Agrobacterium turnefaciens C58 (pGV3101) containing plasmid pBI/fad8 or pBIl2l, results in genetic complementation of the mutation, indicating that the fad7 and fad8 gene products are functionally equivalent. Expression of the fad8 cDNA in transgenic plants often results in the co-suppression of both the endogenous fad7 and fad8 genes in spite of the fact that these two genes share only about 75% nucleotide identity; construction of a fad7/fad8 double mutant with reduced overall levels of trienoic fatty acids in leaf tissues. A series of FAD7-FAD8 chimeric genes, each encoding a functional plastidial omega-3 desaturase, are introduced into the Arabidopsis thaliana fad7/fad8 double mutant, structures, overview. All transformants show an unaltered temperature response, and none of the transformants exhibit an exceptional phenotype; construction of a fad7/fad8 double mutant with reduced overall levels of trienoic fatty acids in leaf tissues. A series of FAD7-FAD8 chimeric genes, each encoding a functional plastidial omega-3 desaturase, are introduced into the Arabidopsis thaliana fad7/fad8 double mutant, structures, overview. All transformants show an unaltered temperature response, and none of the transformants exhibit an exceptional phenotype; 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; generation of the fad7 knockout mutant line JB101; recombinant overexpression of FAD8 increases tolerance to drought in tobacco plants and to osmotic stress in cultured cells. Ectopic overexpression of FAD8 induces an increased ratio mainly in the plastidic lipids; the fad7-1 mutant JB101 is deficient of plastid omega-3 desaturase FAD7 enzyme activity, the defect is due to mRNA destabilization, not deregulation
-
additional information
mutation of Thr286 may directly affect the structure of the transmembrane domain of the enzyme
additional information
-
mutation of Thr286 may directly affect the structure of the transmembrane domain of the enzyme
additional information
-
the removal of the plastidial transit peptide and the incorporation of a KKNL motif to the C-terminus of HaFAD7 increases the activity by 10fold compared to the native protein. N-terminal fusion of transmembrane-domains from either the Saccharomyces cerevisiae microsomal ELO3, (a type III signal anchor domain), or FAE1, an endoplasmic reticulum membrane anchoring domain, results in moderate increases in enzyme activity. Fusing a hemagglutinin epitope tag upstream of an endogenous C-terminal KEK motif results in a significant loss of activity compared to the un-tagged construct, indicating that the endogenous KEK C-terminal di-lysine motif is capable of directing in yeast the ER-retention of this normally plastidial-located protein
additional information
the removal of the plastidial transit peptide and the incorporation of a KKNL motif to the C-terminus of HaFAD7 increases the activity by 10fold compared to the native protein. N-terminal fusion of transmembrane-domains from either the Saccharomyces cerevisiae microsomal ELO3, (a type III signal anchor domain), or FAE1, an endoplasmic reticulum membrane anchoring domain, results in moderate increases in enzyme activity. Fusing a hemagglutinin epitope tag upstream of an endogenous C-terminal KEK motif results in a significant loss of activity compared to the un-tagged construct, indicating that the endogenous KEK C-terminal di-lysine motif is capable of directing in yeast the ER-retention of this normally plastidial-located protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
agriculture
-
potential of exploiting FAD overexpression as a tool to ameliorate drought tolerance in plants
agriculture
-
potential of exploiting FAD overexpression as a tool to ameliorate drought tolerance in plants
-
biotechnology
-
potential of exploiting FAD overexpression as a tool to ameliorate drought tolerance in plants
biotechnology
-
potential of exploiting FAD overexpression as a tool to ameliorate drought tolerance in plants
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.14.19.35)
html completed
Information
