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Enzyme Nomenclature
Information on EC 1.14.19.23 - acyl-lipid (n+3)-(Z)-desaturase (ferredoxin)
Word Map on EC 1.14.19.23
- 1.14.19.23
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oleic
-
linoleic
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desaturation
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polyunsaturated
- cotton
- oleate
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cottonseed
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desaturase-2
- castellanii
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pufas
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docosahexaenoic
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omega-3
-
acanthamoeba
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eicosapentaenoic
- oleracea
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spinacia
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.19.23
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RECOMMENDED NAME
GeneOntology No.
acyl-lipid (n+3)-(Z)-desaturase (ferredoxin)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an oleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a linoleoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
oleoyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (12,13 cis-dehydrogenating)
This plastidial enzyme is able to insert a cis double bond in monounsaturated fatty acids incorporated into glycerolipids. The enzyme introduces the new bond at a position 3 carbons away from the existing double bond, towards the methyl end of the fatty acid. The native substrates are oleoyl (18:1 Delta9) and (Z)-hexadec-7-enoyl (16:1 Delta7) groups attached to either position of the glycerol backbone in glycerolipids, resulting in the introduction of the second double bond at positions 12 and 10, respectively This prompted the suggestion that this is an omega6 desaturase. However, when acting on palmitoleoyl groups(16:1 Delta9), the enzyme introduces the second double bond at position 12 (omega4), indicating it is an (n+3) desaturase [3]. cf. EC 1.14.19.34, acyl-lipid (9+3)-(E)-desaturase.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
compared with the wild type plants, the fad6 mutant shows reduced tolerance to salt stress, and accumulates more Na+ and less K+ under high NaCl stress condition. Furthermore, cellular oxidative damage is more severe in the fad6 mutant when treated with high concentrations of NaCl
physiological function
fatty acid desaturase-6 is required for salt tolerance during the early seedling development of Arabidopsis thaliana
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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
1,2-di-(9'-cis-octadecenyl)-3-beta-D-galactopyranosyl-sn-glycerol + 2 reduced ferredoxin [iron-sulfur] cluster O2 + 2 H+
?
-
-
-
?
1,2-dioleoyl-3-beta-D-galactopyranosyl-sn-glycerol + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
?
-
-
-
?
1-oleoyl-2-(7'-cis-hexadecenoyl)-3-beta-D-galactopyranosyl-sn-glycerol + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
1-linoleoyl-2-(7'-cis-hexadecenoyl)-3-beta-D-galactopyranosyl-sn-glycerol + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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-
-
?
1-oleoyl-sn-glycerol 3-phosphate + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
1-linoleoyl-sn-glycerol 3-phosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
an oleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a linoleoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
an oleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster+ O2 + 2 H+
a linoleoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
?
an oleoyl-[monogalactosyldiacylglycerol] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a linoleoyl-[monogalactosyldiacylglycerol] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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-
-
-
?
an palmitoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (9Z,12E)-hexadeca-9,12-dienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
the main product arising from desaturation of 16:1(9c) appears to be the 16:2(9,12) isomer and is thus an omega-4 desaturation product rather than an omega-6 desaturation product
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-
?
erucic acid + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
?
-
-
-
?
oleate + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
linoleate + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
oleoyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
linoleoyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
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-
-
-
?
an oleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a linoleoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
18:1 carbon fatty acid is the preferred substrate
-
-
?
an oleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a linoleoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
?
oleate + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
linoleate + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
oleate + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
linoleate + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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-
-
-
?
additional information
?
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the production of the omega-4 product when 16:1(9c) is the available substrate suggests that the enzyme introduces the second double bond in a methylene-interrupted configuration measuring from the first double bond rather than from the methyl end of the fatty acid
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-
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additional information
?
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the enzyme measures the insertion of the new double bond from the methyl end and the existing (n-9)-cis double bond of an appropriate acyl or alkyl chain. The distal part of the substrate group, normally the carboxy end of a fatty acyl residue, is of less importance and, in particular, its activation in thioester form is not required
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-
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additional information
?
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-
the enzyme measures the insertion of the new double bond from the methyl end and the existing (n-9)-cis double bond of an appropriate acyl or alkyl chain. The distal part of the substrate group, normally the carboxy end of a fatty acyl residue, is of less importance and, in particular, its activation in thioester form is not required
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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
an oleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a linoleoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
?
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
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pH 6.0: about 65% of maximal activity, pH 9.0: about 65% of maximal activity
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complementation of the fad6 mutant line of Arabidopsis. The fatty acid composition of the rosette leaves of these plants shows a partially or fully restored accumulation of 16:3 fatty acids, indicating complementation of the primary biochemical deficiency
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functional expression in cyanobacterium Synechococcus sp. strain PCC7942
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
progressive decline in the amount of fad6 mRNA during the later stages of growth
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stress signals including salt and mannitol significantly induce the expression of the enzyme. Upon treatment with 300 mM NaCl or 300 mM mannitol, the transcriptional level of the enzyme increases after 24 h
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.19.23)
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