Information on EC 1.14.19.35 - sn-2 acyl-lipid omega-3 desaturase (ferredoxin)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.19.35
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RECOMMENDED NAME
GeneOntology No.
sn-2 acyl-lipid omega-3 desaturase (ferredoxin)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
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
show the reaction diagram
(1)
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a linoleoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+ = an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
show the reaction diagram
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
show the reaction diagram
(2)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(7Z,10Z,13Z)-hexadecatrienoate biosynthesis
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alpha-linolenate biosynthesis I (plants and red algae)
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glycolipid desaturation
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phospholipid desaturation
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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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene fad7
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
gene fad7
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Manually annotated by BRENDA team
gene fad7
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Manually annotated by BRENDA team
cvs. Gerry (cold sensitive) and T47657 (moderately cold tolerant), gene fad7
Q7XX7I9
UniProt
Manually annotated by BRENDA team
gene fad7
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
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?
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
show the reaction diagram
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
show the reaction diagram
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 30
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active at; active at
additional information
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elevated temperatures lead to decreases in leaf trienoic fatty acid level due to temperature sensitivity of enzyme FAD8 activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
x * 39000, SDS-PAGE
50134
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x * 50134, sequence calculation
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
51172
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x * 51172, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
the phosphorylation target site is Thr286
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preparation of chloroplasts
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
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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
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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
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gene FAD7, expression of the -825 Arabidopsis FAD7 promoter-P-glucuronidase fusion gene in Nicotiana tabacum cv. W38
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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
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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
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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
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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
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heterologous expression in Synechocystis sp. PCC 6803
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
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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
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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
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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
induced by low temperature; induced by low temperature
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
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the enzyme is significantly induced by wounding in tubers
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the steady-state level of fad8 mRNA is strongly increased in plants grown at low temperature
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C103Y
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mutation occuring in the fad3 fad7 fad8 triple mutant
W149stop
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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
C103Y
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mutation occuring in the fad3 fad7 fad8 triple mutant
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W149stop
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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
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
biotechnology