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Information on EC 1.14.19.35 - sn-2 acyl-lipid omega-3 desaturase (ferredoxin)
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EC Tree
1.14.19.35 sn-2 acyl-lipid omega-3 desaturase (ferredoxin)IUBMB Comments
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).
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Word Map
- 1.14.19.35
-
trienoic
- jasmonate
-
desaturases
-
linolenic
-
alpha-linolenic
-
wound-responsive
-
18-carbon
-
delta12
- nutrition
- biotechnology
- agriculture
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
2
+
+
2
=
+
2
+
2
+
2
+
+
2
=
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2
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2
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=
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2
=
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2
+
2
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2
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2
=
+
2
+
2
+
2
reduced ferredoxin [iron-sulfur] cluster
+
+
2
=
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
2
+
2
+
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2
=
+
2
+
2
+
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reduced ferredoxin [iron-sulfur] cluster
+
+
2
=
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
2
Synonyms
fad7-2, osfad8, omega-3 fatty acid desaturase gene, gmfad7, omega3 fatty acid desaturase, hafad7, fad7-1, fatty acid desaturase7, fatty acid desaturase 7, pfrfad7-2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FAD7
FAD8
fatty acid desaturase 7
fatty acid desaturase-7
fatty acid desaturase7
omega-3 desaturase
omega-3 fatty acid desaturase
omega-3 fatty acid desaturase gene
plastid omega-3 desaturase
plastidial FAD7 omega-3 desaturase
plastidial omega-3 desaturase
plastidial omega-3 fatty acid desaturase
Sefad7
sn-2 acyl-lipid omega-3 desaturase (ferredoxin)
FAD7
-
-
-
-
FAD7
-
FAD8
-
-
-
-
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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
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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, , ,
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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).
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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
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Sesamum indicum Var-9
-
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
FAD7 utilizes ferredoxin as the intermediate electron donor to act upon fatty acids esterified to galactolipids, sulfolipid, and phosphatidylglycerol
-
-
?
additional information
?
-
-
FAD7 utilizes ferredoxin as the intermediate electron donor to act upon fatty acids esterified to galactolipids, sulfolipid, and phosphatidylglycerol
-
-
?
additional information
?
-
Sesamum indicum Var-9
FAD7 utilizes ferredoxin as the intermediate electron donor to act upon fatty acids esterified to galactolipids, sulfolipid, and phosphatidylglycerol
-
-
?
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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
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
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Sesamum indicum Var-9
-
-
-
?
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
-
-
?
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
-
-
?
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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
-
Ferredoxin
FAD7 utilizes ferredoxin as the intermediate electron donor to act upon fatty acids esterified to galactolipids, sulfolipid, and phosphatidylglycerol
-
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INHIBITOR
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
elevated temperatures lead to decreases in leaf trienoic fatty acid level due to temperature sensitivity of enzyme FAD8 activity
-
additional information
effect of cold stress treatment on cold sensitive and cold tolerant plants presence or absence of glycine betaine, detailed overview
-
additional information
-
effect of cold stress treatment on cold sensitive and cold tolerant plants presence or absence of glycine betaine, detailed overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Mycoses
Rapid, transient, and highly localized induction of plastidial omega-3 fatty acid desaturase mRNA at fungal infection sites in Petroselinum crispum.
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
elevated temperatures lead to decreases in leaf trienoic fatty acid level due to temperature sensitivity of enzyme FAD8 activity
additional information
elevated temperatures lead to decreases in leaf trienoic fatty acid level due to temperature sensitivity of enzyme FAD8 activity
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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
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cvs. Gerry (cold sensitive) and T47657 (moderately cold tolerant), gene fad7
UniProt
brenda
gene fad7
SwissProt
brenda
gene fad7
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
enzyme levels increase during growth and maturation at 15-26°C
brenda
-
enzyme levels increase during growth and maturation at 15-26°C
-
brenda
gene fad7 is expressed in leaves, but not in roots at normal temperature- and low temperature-growth conditions
brenda
gene fad8 is expressed in leaves, but not in roots at normal temperature- and low temperature-growth conditions
brenda
-
gene fad7 is expressed in leaves, but not in roots at normal temperature- and low temperature-growth conditions
-
brenda
-
gene fad8 is expressed in leaves, but not in roots at normal temperature- and low temperature-growth conditions
-
brenda
additional information
tissue-specific analysis of fatty acid patterns, overview. Enzyme FAD7 is detected in all vegetative tissues, and more abundant in the shoots and mature leaves, which are rich in chlorophyll, expression patterns
brenda
additional information
tissue-specific analysis of fatty acid patterns, overview. Enzyme FAD7 is detected in all vegetative tissues, and more abundant in the shoots and mature leaves, which are rich in chlorophyll, expression patterns
brenda
additional information
tissue-specific analysis of fatty acid patterns, overview. Enzyme FAD8 is detected in all vegetative tissues, and more abundant in the shoots and mature leaves, which are rich in chlorophyll, expression patterns
brenda
additional information
tissue-specific analysis of fatty acid patterns, overview. Enzyme FAD8 is detected in all vegetative tissues, and more abundant in the shoots and mature leaves, which are rich in chlorophyll, expression patterns
brenda
additional information
no or little expression is detected in mature seeds, roots and stems
brenda
additional information
-
FAD7-1 is normally expressed in tissues apart from roots and developing seeds. PfrFAD7-1 and PfrFAD7-2 genes are expressed at low levels during all stages of developing seeds as compared with expression levels in leaves
brenda
additional information
FAD7-1 is normally expressed in tissues apart from roots and developing seeds. PfrFAD7-1 and PfrFAD7-2 genes are expressed at low levels during all stages of developing seeds as compared with expression levels in leaves
brenda
additional information
-
FAD7-2 is highly expressed in leaves and roots. PfrFAD7-1 and PfrFAD7-2 genes are expressed at low levels during all stages of developing seeds as compared with expression levels in leaves
brenda
additional information
FAD7-2 is highly expressed in leaves and roots. PfrFAD7-1 and PfrFAD7-2 genes are expressed at low levels during all stages of developing seeds as compared with expression levels in leaves
brenda