Any feedback?
Information on EC 1.14.19.22 - acyl-lipid omega-6 desaturase (cytochrome b5)
for references in articles please use BRENDA:EC1.14.19.22Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.19.22 acyl-lipid omega-6 desaturase (cytochrome b5)IUBMB Comments
This microsomal enzyme introduces a cis double bond in fatty acids attached to lipid molecules at a location 6 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. The most common substrates are oleoyl groups attached to either the sn-1 or sn-2 position of the glycerol backbone in phosphatidylcholine. cf. EC 1.14.19.23, acyl-lipid omega-6 desaturase (ferredoxin).
Specify your search results
Word Map
- 1.14.19.22
-
linoleic
-
desaturases
-
polyunsaturated
-
desaturation
- hypogaea
-
seed-specific
- carthamus
- tinctorius
-
hexadecadienoic
- stearoyl-acp
-
high-oleate
- agriculture
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
fad2-1a, fad2-1b, fad2-3, delta12 desaturase, fad2a, omega-6 desaturase, omega-6 fatty acid desaturase, fad2-4, microsomal oleate desaturase, oleoyl-pc desaturase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine DELTA12-desaturase
delta-12 fatty acid desaturase 2
Delta-12 oleate desaturase
DELTA12-desaturase
DELTA12-fatty acid desaturase
desaturase, oleate
-
-
-
-
EC 1.3.1.35
-
-
formerly
-
FAD2
FAD2-1
FAD2-1B
FAD2-2
FAD2-3
linoleate synthase
-
-
-
-
microsomal omega-6 fatty acid desaturase
oleate desaturase
oleoyl phosphatidylcholine desaturase
oleoyl-CoA desaturase
oleoyl-PC desaturase
oleoyl-phosphatidylcholine desaturase
oleoylphosphatidylcholine desaturase
-
-
-
-
omega-6 desaturase
omega-6 fatty acid desaturase
seed-specific delta-12 fatty acid desaturase 2
TauDELTA12des
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine DELTA12-desaturase
-
-
-
oleate desaturase
-
-
-
-
oleoyl-CoA desaturase
-
-
-
-
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
an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a linoleoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a linoleoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
-
-
-
-
an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a linoleoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
also desaturates phosphatidylcholines containing the oleoyl group on O-2 of the glycerol residue
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
-
,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine,ferrocytochrome-b5:oxygen oxidoreductase (12,13 cis-dehydrogenating)
This microsomal enzyme introduces a cis double bond in fatty acids attached to lipid molecules at a location 6 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. The most common substrates are oleoyl groups attached to either the sn-1 or sn-2 position of the glycerol backbone in phosphatidylcholine. cf. EC 1.14.19.23, acyl-lipid omega-6 desaturase (ferredoxin).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
59929-36-1
-
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
1,2-di-oleoyl-sn-glycero-3-phosphorylcholine + 2 ferrocytochrome b5 + O2 + 2 H+
1,2-di-linoleoyl-sn-glycero-3-phosphorylcholine + 2 ferricytochrome b5 + 2 H2O
-
desaturation takes place at both position-1 and position-2. The distearoyl or dielaidoyl phosphatidylcholines are not desaturated
-
-
?
1,2-dioleoylphosphatidylcholine + 2 ferrocytochrome b5 + O2 + 2 H+
1,2-linoleoylphosphatidylcholine + 2 ferricytochrome b5 + 2 H2O
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
1-acyl-2-oleoyl-sn-glycero-3-phosphorylcholine + 2 ferrocytochrome b5 + O2 + 2 H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphorylcholine + 2 ferricytochrome b5 + 2 H2O
-
-
-
-
?
1-palmitoyl-2-oleoyl phosphatidylcholine + NAD+
1-palmitoyl-2-linoleoyl phosphatidylcholine + NADH
-
-
-
-
?
1-stearoyl-2-oleoyl phosphatidylcholine + NAD+
1-stearoyl-2-linoleoyl phosphatidylcholine + NADH
-
-
-
-
?
oleoyl-phosphatidylcholine + 2 ferrocytochrome b5 + O2 + 2 H+
linoleoyl-phosphatidylcholine + 2 ferricytochrome b5 + 2 H2O
-
-
-
-
?
oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
linoleoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
-
the IgG fraction from ascites fluid inhibits 62% of NADH-dependent cytochrome c reduction in safflower (Carthamus tinctorius L.) microsomes. These antibodies also block desaturation of oleic acid to linoleic acid in lipids of Carthamus tinctorius microsomes by 93%, suggesting that cytochrome b5 is the electron donor for the DELTA12 desaturase
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
oleoyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
linoleoyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
the enzyme inserts a double bond between the carbons 12 and 13 of monounsaturated oleic acid to generate polyunsaturated linoleic acid
-
-
?
palmitoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
hexadecadienoyl-[glycerolipid] + ferricytochrome b5 + H2O
1,2-dioleoylphosphatidylcholine + 2 ferrocytochrome b5 + O2 + 2 H+
1,2-linoleoylphosphatidylcholine + 2 ferricytochrome b5 + 2 H2O
-
the rate of desaturation of endogenous oleoyl phosphatidylcholine is much greater that of exogenous dioleoyl phosphatidylcholine
-
-
?
1,2-dioleoylphosphatidylcholine + 2 ferrocytochrome b5 + O2 + 2 H+
1,2-linoleoylphosphatidylcholine + 2 ferricytochrome b5 + 2 H2O
-
the rate of desaturation of endogenous oleoyl phosphatidylcholine is much greater that of exogenous dioleoyl phosphatidylcholine
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[CoA] + ferrocytochrome b5 + O2 + H+
linoleoyl-[CoA] + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[CoA] + ferrocytochrome b5 + O2 + H+
linoleoyl-[CoA] + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
best substrate
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
best substrate
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
-
?
palmitoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
hexadecadienoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
?
palmitoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
hexadecadienoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
-
?
additional information
?
-
-
wild-type enzyme has an inherent, low level of hydroxylation activity
-
-
?
additional information
?
-
-
a desaturase mutant that is unable to convert oleic acid to linoleic acid is impaired in polyunsaturated fatty acid biosynthesis, shows delayed spore germination, a twofold reduction in growth, a reduced level of conidiation and complete loss of eclerotial development, compared to the wild-type
-
-
?
additional information
?
-
-
CeFAT-2 displays characteristics of a bifunctional DELTA12/DELTA15-desaturase and has a great deal of elasticity with respect to fatty acid chain length in being able to desaturate fatty acids ranging from C14 to C18 at the DELTA12 and DELTA15 positions
-
-
?
additional information
?
-
-
yeast cells transformed with the plasmid construct pYES2/FAD2 produce a substantial amount of linoleic acid (18:2) after a period of galactose induction
-
-
?
additional information
?
-
-
yeast cells transformed with the plasmid construct pYES2/FAD2 produced a substantial amount of linoleic acid (18:2) after a period of galactose induction
-
-
?
additional information
?
-
-
esterification of oleate at position 1 and 2
-
-
?
additional information
?
-
-
yeast cells expressing CtFAD2-1 cDNA partially convert oleic fatty acid to linoleic fatty acid
-
-
?
additional information
?
-
-
esterification of oleate at position 1 and 2
-
-
?
additional information
?
-
LKFAD15 is a DELTA12/DELTA15 bifunctional fatty acid desaturase being able to produce linoleic acid and alpha-linolenic acid using oleic acid as substrate and also adjusting the omega-6/omega-3 fatty acids
-
-
?
additional information
?
-
-
recombinant yeast cells can convert oleic acid to linoleic acid
-
-
?
additional information
?
-
-
exogenously added oleic acid is converted to linoleic acid in the gene transformants but not mock transformants of Aurantiochytrium limacinum mh0186 and yeast cells
-
-
?
additional information
?
-
-
exogenously added oleic acid is converted to linoleic acid in the gene transformants but not mock transformants of Aurantiochytrium limacinum mh0186 and yeast cells
-
-
?
additional information
?
-
-
yeasts transformed with the tauDELTA12des converts endogenous oleic acid into linoleic acid
-
-
?
additional information
?
-
-
yeasts transformed with the tauDELTA12des converts endogenous oleic acid into linoleic acid
-
-
?
additional information
?
-
-
yeasts transformed with the tauDELTA12des converts endogenous oleic acid into linoleic acid
-
-
?
additional information
?
-
the enzyme may use a cytochrome b5-like domain in another desaturase as an electron donor
-
-
?
additional information
?
-
-
the enzyme may use a cytochrome b5-like domain in another desaturase as an electron donor
-
-
?
additional information
?
-
-
not: di-oleoyl phosphatidylcholine, dielaidoyl phosphatidylcholine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
oleoyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
linoleoyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
the enzyme inserts a double bond between the carbons 12 and 13 of monounsaturated oleic acid to generate polyunsaturated linoleic acid
-
-
?
palmitoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
hexadecadienoyl-[glycerolipid] + ferricytochrome b5 + H2O
additional information
?
-
-
a desaturase mutant that is unable to convert oleic acid to linoleic acid is impaired in polyunsaturated fatty acid biosynthesis, shows delayed spore germination, a twofold reduction in growth, a reduced level of conidiation and complete loss of eclerotial development, compared to the wild-type
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2 + H+
1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[CoA] + ferrocytochrome b5 + O2 + H+
linoleoyl-[CoA] + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[CoA] + ferrocytochrome b5 + O2 + H+
linoleoyl-[CoA] + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
best substrate
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
best substrate
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
-
?
oleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
linoleoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
-
?
palmitoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
hexadecadienoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
?
palmitoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
hexadecadienoyl-[glycerolipid] + ferricytochrome b5 + H2O
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyanide
-
the enzyme inhibited by cyanide but not by carbon monoxide, indicating that it required cytochrome b5
additional information
-
anti-(cytochrome b5) immunglobuline G is an efficient inhibitor
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O2
-
elevation of external O2 supply produces a dramatic increase of the FAD2 enzyme activity
Triton X-100
-
at an optimal concentration of 0.1% Triton X-100, the detergent increases the rate of desaturation about three fold
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
-
10°C: about 50% of maximal activity, 40°C: about 40% of maximal activity
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
isoform FAD2, intron-mediated regulatory mechanism controls both the seed-specific expression of enzyme gene and the expression of plant FAD2 gene
-
-
brenda
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
-
detached, fast and dramatic increase or decrease in the level of enzyme activity in response to a temperature change from 30°C to 10°C, or from 10°C to 30°C
brenda
-
accumulates in leaf mesophyll cells when exposed to 15°C for 4 days in dark conditions
brenda
additional information
altered levels of polyunsaturated fatty acids in leaves treated with cold stress have no direct correlation with the expression of enzyme isoforms FAD2-3 and FAD2-2
brenda
-
accumulates in root epidermis cells when exposed to 15°C for 4 days in dark conditions
brenda
-
peeled, a change of temperature from 10°C to 30°C brings about a significant decrease of enzyme activity. When the temperature shifts from 30°C to 10°C, the enzyme activity only increases slightly
brenda
additional information
constitutive expression in both vegetative tissues and developing seeds
brenda
additional information
-
constitutive expression in both vegetative tissues and developing seeds
brenda
additional information
not found in stem, leaf, cotyledon, root and embryo
brenda
additional information
-
not found in stem, leaf, cotyledon, root and embryo
brenda
additional information
enzyme expression in all tissues tested, higher levels of RNA accumulation in reproductive organs and cells that proliferate rapidly or store lipids
brenda
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
-
omega-6 fatty acid desaturase fad2
brenda
-
when a pBrFAD2-1:mRFP construct is introduced into tobacco epidermal cells, the fluorescent signal is noted in the endoplasmic reticulum
brenda
-
amino acid sequence possesses a C-terminal signal for endoplasmic reticulum retention
brenda
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
malfunction
metabolism
-
the enzyme is involved in providing polyunsaturated phosphatidylcholine to the chloroplast envelope
physiological function
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
evolution
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
malfunction
-
combinations of mutations in FAD2-1A and FAD2-1B produce high oleic acid levels in the seed oil
malfunction
-
the disruption of the tauDELTA12des in Thraustochytrium aureum by homologous recombination results in the accumulation of oleic acid and a decrease in the levels of linoleic acid and its downstream polyunsaturated fatty acids. The transformation of the tauDELTA 12des -disruption mutants with a tauDELTA 12des expression cassette restores the wild-type fatty acid profiles
malfunction
-
the PI 283327 FAD2-1B allele, carrying the mutant FAD2-1B P137R allele, is associated with an increase in seed oleic acid content. Although the FAD2-1B mutant alleles alone are not capable of producing a high oleic acid phenotype. When existing FAD2-1A mutations are combined with the novel mutant FAD2-1B alleles, a high oleic acid phenotype is recovered only for those lines which are homozygous for both of the mutant alleles
malfunction
-
transgenic Korean rapeseed Tammi containing high oleic acid contents (78 mol%) are developed via the expression of the BrFAD2-1 gene in an antisense orientation
malfunction
-
transgenic lines expressing an antisense CsFAD2 gene show a high increase in 18:1 content from 13-18% in wild type to 38-51% in transgenic seeds, and concomitantly significant decrease in 18:2 and 18:3 PUFAs. The levels of eicosenoic acid (20:1), another major monounsaturated fatty acid in camelina seed, are also slightly increased in transgenic seeds. These results clearly indicate that CsFAD2 genes encode microsomal oleate desaturases and contribute to PUFA synthesis in camelina seeds
malfunction
-
transgenic lines expressing an antisense CsFAD2 genes show a high increase in 18:1 content from 13-18% in wild type to 38-51% in transgenic seeds, and concomitantly significant decrease in 18:2 and 18:3 PUFAs. The levels of eicosenoic acid (20:1), another major monounsaturated fatty acid in camelina seed, are also slightly increased in transgenic seeds. These results clearly indicate that CsFAD2 genes encode microsomal oleate desaturases and contribute to PUFA synthesis in camelina seeds
malfunction
the increased oleate level in unexpanded leaves due to enzyme-silencing recedes significantly in fully expanded leaves
malfunction
the low protein density in fad2-deficient mitochondrial membranes is mainly responsible for the reduction in proton leak
malfunction
-
the disruption of the tauDELTA12des in Thraustochytrium aureum by homologous recombination results in the accumulation of oleic acid and a decrease in the levels of linoleic acid and its downstream polyunsaturated fatty acids. The transformation of the tauDELTA 12des -disruption mutants with a tauDELTA 12des expression cassette restores the wild-type fatty acid profiles
-
malfunction
-
the disruption of the tauDELTA12des in Thraustochytrium aureum by homologous recombination results in the accumulation of oleic acid and a decrease in the levels of linoleic acid and its downstream polyunsaturated fatty acids. The transformation of the tauDELTA 12des -disruption mutants with a tauDELTA 12des expression cassette restores the wild-type fatty acid profiles
-
physiological function
-
functional recombinant hybird desaturase-lichenase protein can enhance tolerance to cold stress in transgenic potato, overview
physiological function
-
sve1, a mutant allele of the endoplasmic reticulum-localized oleic acid desaturase FAD2 completely suppresses all vte2 low-temperature phenotype, sve1 expressing plant fatty acid composition, overview. The vte1 mutant is deficient in tocopherol cyclase activity and lacks also all tocopherols
physiological function
-
ectopic expression of BrFAD2-1:mRFP complement the Arabidopsis fad2-2 mutant
physiological function
-
heterologous expression of OsFAD2 enhances the yeast cells cold tolerance capacity compared to wild-type yeast. OsFAD2 enhances tolerance to low temperature when overexpressed in rice at the vegetative stage
physiological function
-
when expressed in yeast cells, CeFAT-2 displays characteristics of a bifunctional DELTA12/DELTA15-desaturase and has a great deal of elasticity with respect to fatty acid chain length in being able to desaturate fatty acids ranging from C14 to C18
physiological function
the enzyme is essential for the survival of Arabidopsis at low temperatures
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
physiological function
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FAD6E_ARATH
383
6
44048
Swiss-Prot
other Location (Reliability: 3)
A0A059XHI7_9BRAS
383
5
44141
TrEMBL
other Location (Reliability: 4)
A0A5B6Z1X6_DAVIN
372
4
43126
TrEMBL
other Location (Reliability: 4)
E1A446_ARAHY
379
4
43636
TrEMBL
other Location (Reliability: 4)
A0A059XI79_9BRAS
384
4
44338
TrEMBL
other Location (Reliability: 4)
Q8W2F0_HELAN
383
5
43992
TrEMBL
other Location (Reliability: 2)
A0A059XHI4_9BRAS
384
5
44305
TrEMBL
other Location (Reliability: 3)
A0A059XHH7_CRAAB
383
4
44035
TrEMBL
other Location (Reliability: 3)
A0A5B7ABV4_DAVIN
383
4
44357
TrEMBL
other Location (Reliability: 4)
G8GUL0_ARAHY
379
5
43682
TrEMBL
other Location (Reliability: 4)
A0A059XME6_9BRAS
383
5
44119
TrEMBL
other Location (Reliability: 3)
Q9SP28_VERGA
383
5
44330
TrEMBL
other Location (Reliability: 2)
E9M5E4_ARAHY
379
5
43653
TrEMBL
other Location (Reliability: 4)
A0A5B6YZ71_DAVIN
438
4
51025
TrEMBL
other Location (Reliability: 4)
A0A059XMF2_9BRAS
383
5
44113
TrEMBL
other Location (Reliability: 3)
A0A059XCG1_CRAAB
383
4
44118
TrEMBL
other Location (Reliability: 3)
J9WJ66_ARAHY
246
4
28265
TrEMBL
other Location (Reliability: 3)
A0A059XMB1_CRAAB
383
5
44116
TrEMBL
other Location (Reliability: 5)
A0A5B6Z0N4_DAVIN
134
0
14136
TrEMBL
other Location (Reliability: 3)
G8GUK7_ARAHY
379
4
43618
TrEMBL
other Location (Reliability: 4)
A0A059XI75_9BRAS
384
4
44295
TrEMBL
other Location (Reliability: 3)
A0A396JCP0_MEDTR
213
2
23974
TrEMBL
Chloroplast (Reliability: 5)
A0A059XME3_CRAAB
384
4
44116
TrEMBL
other Location (Reliability: 3)
D9ZGG5_9AGAM
462
1
51541
TrEMBL
other Location (Reliability: 5)
A0A5B7AE93_DAVIN
363
4
42072
TrEMBL
other Location (Reliability: 3)
J9WJV6_ARAHY
246
4
28307
TrEMBL
other Location (Reliability: 4)
A0A3Q9B2S0_IDEPO
380
6
43877
TrEMBL
other Location (Reliability: 2)
A0A059XCI5_9BRAS
383
5
44119
TrEMBL
other Location (Reliability: 3)
G8GUK9_ARAHY
379
4
43606
TrEMBL
other Location (Reliability: 4)
O24499_HELAN
378
5
43719
TrEMBL
other Location (Reliability: 2)
Q8W2E9_HELAN
382
5
44005
TrEMBL
other Location (Reliability: 2)
A0A059XI89_9BRAS
383
5
44101
TrEMBL
other Location (Reliability: 3)
A0A172W5U9_9CHLO
389
5
42589
TrEMBL
other Location (Reliability: 2)
Q9LKK6_ARAHY
379
4
43636
TrEMBL
other Location (Reliability: 4)
A0A059XCH8_9BRAS
383
5
44113
TrEMBL
other Location (Reliability: 3)
A0A5B7C8P1_DAVIN
306
0
33575
TrEMBL
Mitochondrion (Reliability: 3)
A0A059XMC0_9BRAS
384
4
44348
TrEMBL
other Location (Reliability: 4)
A0A5B7C2W1_DAVIN
266
0
29512
TrEMBL
other Location (Reliability: 3)
C8CK30_ARAHY
246
4
28276
TrEMBL
other Location (Reliability: 4)
A0A396J9R6_MEDTR
127
2
15227
TrEMBL
other Location (Reliability: 2)
E1A444_ARAHY
379
4
43652
TrEMBL
other Location (Reliability: 4)
A0A5B6Z1J0_DAVIN
287
0
30788
TrEMBL
other Location (Reliability: 2)
Q48DW3_PSE14
Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
327
4
37389
TrEMBL
-
A0A396JBV5_MEDTR
131
0
15576
TrEMBL
other Location (Reliability: 3)
A3LUV0_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
418
5
47999
TrEMBL
other Location (Reliability: 4)
A0A059XCH3_9BRAS
384
4
44221
TrEMBL
other Location (Reliability: 4)
W0SA01_FISSO
432
5
48828
TrEMBL
other Location (Reliability: 4)
A0A059XMG2_9BRAS
384
5
44332
TrEMBL
other Location (Reliability: 3)
A0A1U9XQV1_9MAGN
384
5
44164
TrEMBL
other Location (Reliability: 4)
A0A059XMD1_9BRAS
384
3
44258
TrEMBL
other Location (Reliability: 4)
A0A059XHJ3_9BRAS
378
4
43466
TrEMBL
other Location (Reliability: 3)
A0A059XMB5_9BRAS
384
4
44341
TrEMBL
other Location (Reliability: 3)
U5U2P9_EUCCA
389
4
44507
TrEMBL
other Location (Reliability: 5)
G8GUK8_ARAHY
379
4
43622
TrEMBL
other Location (Reliability: 4)
E9M5E3_ARAHY
379
4
43657
TrEMBL
other Location (Reliability: 4)
S5RJN0_CRAAB
383
5
44146
TrEMBL
other Location (Reliability: 3)
E1A443_ARAHY
379
4
43592
TrEMBL
other Location (Reliability: 4)
W0S9Y7_FISSO
433
5
48935
TrEMBL
other Location (Reliability: 2)
Q9SP29_VERGA
383
5
44268
TrEMBL
other Location (Reliability: 2)
A0A059XI69_CRAAB
384
4
44155
TrEMBL
other Location (Reliability: 3)
A0A059XCG8_9BRAS
384
5
44260
TrEMBL
other Location (Reliability: 4)
H9CP21_LIPKO
435
0
49767
TrEMBL
Mitochondrion (Reliability: 1)
Q4QWZ1_OLEEU
381
0
44144
TrEMBL
other Location (Reliability: 5)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme motifs and domain organization, overview
additional information
enzyme motifs and domain organization, overview
additional information
enzyme motifs and domain organization, overview
additional information
enzyme motifs and domain organization, overview
additional information
enzyme motifs and domain organization, overview
additional information
enzyme motifs and domain organization, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
sequence contains the typical three histidine boxes of membrane-bound desaturases and a C-terminal signal for ER-retention
additional information
-
sequence contains the typical three histidine boxes of membrane-bound desaturases and a C-terminal signal for ER-retention
additional information
sequence contains a C-terminal ER-retention signal
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A104G
-
2.1fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/M324V
-
2.6fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/S322A
-
3.1fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/S322A/M324V
-
4.3fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/T148I
-
29.5fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/T148I/M324V
-
36.1fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/T148I/S322A
-
44.3fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/T148I/S322A/M324V
-
90.2fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
A104G/T148N/S322A/M324I
-
24.6fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
M324I
-
54.1fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
M324V
-
49.2fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
S322A
-
1.3fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
S322A/M324V
-
2.1fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
T148I
-
14.8fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
T148I/M324V
-
26.2fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
T148I/S322A
-
26.2fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
T148I/S322A/M324V
-
34.4fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
T148N
-
3.3fold increase in the ratio of hydroxylation to desaturation compared to wild-type enzyme
D150N
-
the mutation of the ahFAD2 gene results in a dysfunctional desaturase
G374E
-
line 743, missense mutations in a less conserved region, seed phenotype does not differ from wild-type
P137R
-
the PI 283327 FAD2-1B allele, carrying the mutant FAD2-1B P137R allele, is associated with an increase in seed oleic acid content
S117N
S238F
-
line 615, missense mutations in a less conserved region, seed phenotype does not differ from wild-type
additional information
-
mutation Ol greatly increases oleic acid and is correlated with greatly reduced expression of enzyme isoform FAD2-1. FAD2-1 gene is duplicated in Ol mutants. Development of dominant INDEL markers diagnostic for presence or absence of the Ol mutation
S117N
-
line 17D, missense mutation in a highly conserved region of the protein sequence, oleic acid levels in seeds are significantly higher than in wild-type, hence the enzyme activity is lower than in wild-type
S117N
-
missense mutation in combination with mutant FAD2-1B P137R allele is associated with an increase in seed oleic acid content
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 30
-
temperature changes from 10°C to 30°C or vice versa bring about a fast and dramatic decrease or increase in the level of FAD2 activity, respectively
20 - 32
no difference in FAD2 expression is found in plants grown between 20°C and 32°C, isozymes FAD2-3 and FAD2-4 are induced under cold stress, FAD2-4 induction is significantly higher than FAD2-3, in contrast isozyme FAD2-2 is not affected by cold
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
removal of hulls followed by incubation in air does not change the activity level of the enzyme, whereas incubation under nitrogen causes strong decrease
-
when peeled seeds are incubated at 10°C for 14 h, the enzyme activity remains constant
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
low internal oxygen levels (0.001 mM) limit FAD2 activity, the internal oxygen level acts as a key regulator for the activity of the FAD2 enzyme
-
688081
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
CeFAT-2 is expressed under the control of an inducible Gal1 promoter in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae
expressed in Solanum tuberosum leaves as fusion protein with thermostable lichenase
-
flag-tagged enzyme is functionally expressed in yeast cells. To express the gene in thraustochytrids, a construct driven by the thraustochytrid-derived ubiquitin promoter is used
-
gene desA, expression profile analysis, construction of a hybrid of desA and reporter gene encoding thermostable lichenase, licBM3, and expression in Escherichia coli strain XL1blue and Solanum tuberosum cells, the latter via Agrobacterium tumefaciens strain AGLO transfection. The desaturase can enhance tolerance to cold stress in potato, and desaturase and lichenase retain their functionality in the structure of a recombinant hybrid protein where the enzymatic activity of target gene product is higher than in the case of reporter lichenase gene absence in the construction
-
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
recombinantly expressed in Saccharomyces cerevisiae and Pichia Pastoris
CeFAT-2 is expressed under the control of an inducible Gal1 promoter in Saccharomyces cerevisiae
-
CeFAT-2 is expressed under the control of an inducible Gal1 promoter in Saccharomyces cerevisiae
-
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression levels of OsFAD2 are markedly decreased in shoots treated with kinetin and gibberellins
-
expression levels of OsFAD2 are markedly increased in shoots treated with 6-benzyladenine
-
the expression level remains approximately constant for at least 3 days after transfer to the cold (22 to 6°C)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
mutation Ol greatly increases oleic acid and is correlated with greatly reduced expression of enzyme isoform FAD2-1. FAD2-1 gene is duplicated in Ol mutants. Development of dominant INDEL markers diagnostic for presence or absence of the Ol mutation
medicine
-
use of enzyme as a molecular target for the development of chemotherapeutic approaches against Chagas disease
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Slack, C.R.; Roughan, P.G.; Terpstra, J.
Some properties of a microsomal oleate desaturase from leaves
Biochem. J.
155
71-80
1976
Pisum sativum
brenda
Demandre, C.; Vigh, L.; Justin, A.M.; Jolliot, A.; Wolf, C.; Mazliak, P.
Effects of the catalytic hydrogenation of microsomal lipids upon four enzyme activities involved in oleic acid desaturation
Plant Sci.
44
13-21
1986
Solanum tuberosum
-
brenda
Stymne, S.; Appelqvist, L.A.
The biosynthesis of linoleate from oleoyl-CoA via oleoyl-phosphatidylcholine in microsomes of developing safflower seeds
Eur. J. Biochem.
90
223-229
1978
Carthamus tinctorius
brenda
Umeki, S.; Nozawa, Y.
Thermoadaptive regulation of microsomal desaturase and electron-transport enzyme activities in lipid-manipulated Tetrahymena cells. Extent of unsaturated fatty acid production is dependent on membrane fluidity before temperature down-shift
Biochim. Biophys. Acta
793
123-128
1984
Tetrahymena pyriformis, Tetrahymena pyriformis NT-1
brenda
Cheesbrough, T.M.
Changes in the enzymes for fatty acid synthesis and desaturation during acclimation of developing soybean seeds to altered growth temperature
Plant Physiol.
90
760-764
1989
Glycine max
brenda
Murphy, D.J.; Woodrow, I.E.; Latzko, E.; Mukherjee, K.D.
Solubilisation of oleoyl-CoA thioesteras, oleoyl-CoA:phosphatidylcholine acyltransferase and oleoyl phosphatidylcholine desaturase
FEBS Lett.
162
442-446
1983
Pisum sativum
-
brenda
Citharel, B.; Oursel, A.; Mazliak, P.
Desaturation of oleoyl and linoleoyl residues linked to phospholipids in growing roots of yellow lupin
FEBS Lett.
161
251-256
1983
Lupinus luteus
-
brenda
Murphy, D.J.; Woodrow, I.E.; Mukherjee, K.D.
Substrate specificities of the enzymes of the oleate desaturase system from photosynthetic tissue
Biochem. J.
225
267-270
1985
Pisum sativum
brenda
Browse, J.; Slack, C.R.
The effects of temperature and oxygen on the rates of fatty acid synthesis and oleate desaturation in seaflower (Carthamus tinctorius) seed
Biochim. Biophys. Acta
753
145-152
1983
Carthamus tinctorius
-
brenda
Wilson, A.C.; Adams, W.C.; Miller, R.W.
Lipid involvement in oleoyl CoA desaturase activity of Fusarium oxysporum microsomes
Can. J. Biochem.
58
97-102
1980
Fusarium oxysporum
brenda
Murphy, D.J.; Mukherjee, K.D.; Latzko, E.
Lipid metabolism in microsomal fraction from photosynthetic tissue. Effects of catalase and hydrogen peroxide on oleate desaturation
Biochem. J.
213
249-252
1983
Pisum sativum
brenda
Hawke, J.C.; Stumpf, P.K.
Desaturation of oleic and linoleic acids by leaves of dark- and light-grown maize seedlings
Plant Physiol.
65
1027-1030
1980
Zea mays
brenda
Slack, C.R.; Grattan Roughan, P.; Browse, J.
Evidence for an oleoyl phosphatidylcholine desaturase in microsomal preparations from cotyledons of safflower (Carthamus tinctorius) seed
Biochem. J.
179
649-656
1979
Carthamus tinctorius, Carthamus tinctorius cultivar 0-22
brenda
Pugh, E.L.; Kates, M.
Characterization of a membrane-bound phospholipid desaturase system of candida lipolytica
Biochim. Biophys. Acta
380
442-453
1975
Yarrowia lipolytica
brenda
Sarmiento, C.; Garces, R.; Mancha, M.
Oleate desaturation and acyl turnover in sunflower (Helianthus annuus L.) seed lipids during rapid temperature adaption
Planta
205
595-600
1998
Helianthus annuus
-
brenda
Gray, D.A.; Kekwick, R.G.O.
Intracellular location of oleate desaturase and associated constituents in developing sunflower (Helianthus annuus) seeds
Plant Sci.
119
11-21
1996
Helianthus annuus
-
brenda
Gray, D.A.; Kekwick, R.G.O.
Oleate desaturase activity in sunflower (Helianthus annuus) seeds and its relation to associated constituents during seed development
Plant Sci.
115
39-47
1996
Helianthus annuus
-
brenda
Garcia-Diaz, M.T.; Martinez-Rivas, J.M.; Mancha, M.
Temperature and oxygen regulation of oleate desaturation in developing sunflower (Helianthus annuus) seeds
Physiol. Plant.
114
13-20
2002
Helianthus annuus
brenda
Petrini, G.A.; Altabe, S.G.; Uttaro, A.D.
Trypanosoma brucei oleate desaturase may use a cytochrome b5-like domain in another desaturase as an electron donor
Eur. J. Biochem.
271
1079-1086
2004
Trypanosoma brucei (Q6UCJ6), Trypanosoma brucei
brenda
Esteban, A.B.; Sicardo, M.D.; Mancha, M.; Martinez-Rivas, J.M.
Growth temperature control of the linoleic acid content in safflower (Carthamus tinctorius) seed oil
J. Agric. Food Chem.
52
332-336
2004
Carthamus tinctorius
brenda
Broadwater, J.A.; Whittle, E.; Shanklin, J.
Desaturation and hydroxylation. Residues 148 and 324 of Arabidopsis FAD2, in addition to substrate chain length, exert a major influence in partitioning of catalytic specificity
J. Biol. Chem.
277
15613-15620
2002
Arabidopsis thaliana
brenda
Wilson, R.A.; Calvo, A.M.; Chang, P.K.; Keller, N.P.
Characterization of the Aspergillus parasiticus DELTA12-desaturase gene: A role for lipid metabolism in the Aspergillus-seed interaction
Microbiology
150
2881-2888
2004
Aspergillus parasiticus
brenda
Martinez-Rivas, J.M.; Sanchez-Garcia, A.; Sicardo, M.D.; Garcia-Diaz, M.T.; Mancha, M.
Oxygen-independent temperature regulation of the microsomal oleate desaturase (FAD2) activity in developing sunflower (Helianthus annuus) seeds
Physiol. Plant.
117
179-185
2003
Helianthus annuus
-
brenda
Maldonado, R.A.; Kuniyoshi, R.K.; Linss, J.G.; Almeida, I.C.
Trypanosoma cruzi oleate desaturase: molecular characterization and comparative analysis in other trypanosomatids
J. Parasitol.
92
1064-1074
2006
Trypanosoma cruzi
brenda
Li, L.; Wang, X.; Gai, J.; Yu, D.
Molecular cloning and characterization of a novel microsomal oleate desaturase gene from soybean
J. Plant Physiol.
164
1516-1526
2007
Glycine max (Q19AK7), Glycine max
brenda
Schuppert, G.F.; Tang, S.; Slabaugh, M.B.; Knapp, S.J.
The sunflower high-oleic mutant Ol carries variable tandem repeats of FAD2-1, a seed-specific oleoyl-phosphatidyl choline desaturase
Mol. Breed.
17
241-256
2006
Helianthus annuus
brenda
Kim, M.J.; Kim, H.; Shin, J.S.; Chung, C.H.; Ohlrogge, J.B.; Suh, M.C.
Seed-specific expression of sesame microsomal oleic acid desaturase is controlled by combinatorial properties between negative cis-regulatory elements in the SeFAD2 promoter and enhancers in the 5-UTR intron
Mol. Genet. Genomics
276
351-368
2006
Sesamum indicum
brenda
Banilas, G.; Moressis, A.; Nikoloudakis, N.; Hatzopoulos, P.
Spatial and temporal expressions of two distinct oleate desaturases from olive (Olea europaea L.)
Plant Sci.
168
547-555
2005
Olea europaea (Q8GVC9)
brenda
Reza, M.A.; Goldenkova-Pavlova, I.V.; Pchelkin, V.P.; Tsydendambaev, V.D.; Los, D.A.; Nosov, A.M.
Acyl-lipid DELTA12-desaturase of the cyanobacterium increases the unsaturation degree in transgenic potato (Solanum tuberosum L.)
Biologia
53
4-7
2007
Synechocystis sp.
-
brenda
Chu, Y.; Ramos, L.; Holbrook, C.C.; Ozias-Akins, P.
Frequency of a loss-of-function mutation in oleoyl-PC desaturase (ahFAD2A) in the mini-core of the U.S. peanut germplasm collection
Crop Sci.
47
2372-2378
2007
Arachis hypogaea
-
brenda
Li, L.; Wang, X.; Gai, J.; Yu, D.
Isolation and characterization of a seed-specific isoform of microsomal omega-6 fatty acid desaturase gene (FAD2-1B) from soybean
DNA Seq.
19
28-36
2008
Glycine max (Q19AK8), Glycine max
brenda
Rolletschek, H.; Borisjuk, L.; Sanchez-Garcia, A.; Gotor, C.; Romero, L.C.; Martinez-Rivas, J.M.; Mancha, M.
Temperature-dependent endogenous oxygen concentration regulates microsomal oleate desaturase in developing sunflower seeds
J. Exp. Bot.
58
3171-3181
2007
Helianthus annuus
brenda
Kargiotidou, A.; Deli, D.; Galanopoulou, D.; Tsaftaris, A.; Farmaki, T.
Low temperature and light regulate delta 12 fatty acid desaturases (FAD2) at a transcriptional level in cotton (Gossypium hirsutum)
J. Exp. Bot.
59
2043-2056
2008
Gossypium hirsutum (Q8W2B9), Gossypium hirsutum
brenda
Hernandez, M.L.; Padilla, M.N.; Mancha, M.; Martinez-Rivas, J.M.
Expression analysis identifies FAD2-2 as the olive oleate desaturase gene mainly responsible for the linoleic acid content in virgin olive oil
J. Agric. Food Chem.
57
6199-6206
2009
Olea europaea (A9UKE1), Olea europaea (Q4QWZ0), Olea europaea (Q4QWZ1)
brenda
Lacombe, S.; Souyris, I.; Berville, A.J.
An insertion of oleate desaturase homologous sequence silences via siRNA the functional gene leading to high oleic acid content in sunflower seed oil
Mol. Genet. Genomics
281
43-54
2009
Helianthus annuus (O24499)
brenda
Dierking, E.C.; Bilyeu, K.D.
New sources of soybean seed meal and oil composition traits identified through TILLING
BMC Plant Biol.
9
89
2009
Glycine max
brenda
Amiri, R.M.; Yureva, N.O.; Shimshilashvili, K.R.; Goldenkova-Pavlova, I.V.; Pchelkin, V.P.; Kuznitsova, E.I.; Tsydendambaev, V.D.; Trunova, T.I.; Los, D.A.; Jouzani, G.S.; Nosov, A.M.
Expression of acyl-lipid Delta12-desaturase gene in prokaryotic and eukaryotic cells and its effect on cold stress tolerance of potato
J. Integr. Plant Biol.
52
289-297
2010
Synechocystis sp.
brenda
Song, W.; Maeda, H.; DellaPenna, D.
Mutations of the ER to plastid lipid transporters TGD1, 2, 3 and 4 and the ER oleate desaturase FAD2 suppress the low temperature-induced phenotype of Arabidopsis tocopherol-deficient mutant vte2
Plant J.
62
1004-1018
2010
Arabidopsis thaliana
brenda
Lei, N.; Peng, S.; Niu, B.; Chen, J.; Zhou, J.; Tang, L.; Xu, Y.; Wang, S.; Chen, F.
Molecular cloning and characterization of a novel microsomal oleate desaturase gene DiFAD2 from Davidia involucrata Baill
Biol. Plant.
54
41-46
2010
Davidia involucrata
-
brenda
Pham, A.T.; Lee, J.D.; Shannon, J.G.; Bilyeu, K.D.
Mutant alleles of FAD2-1A and FAD2-1B combine to produce soybeans with the high oleic acid seed oil trait
BMC Plant Biol.
10
195
2010
Glycine max
brenda
Yan, Z.; Zhuo, L.; Mulan, J.; Xia, W.; Yangmin, G.; Yinbo, Z.; Fenghong, H.
Clone and identification of bifunctional DELTA12/DELTA15 fatty acid desaturase LKFAD15 from Lipomyces kononenkoae
Food Sci. Biotechnol.
22
573-576
2013
Lipomyces kononenkoae (H9CP21)
-
brenda
Matsuda, T.; Sakaguchi, K.; Kobayashi, T.; Abe, E.; Kurano, N.; Sato, A.; Okita, Y.; Sugimoto, S.; Hama, Y.; Hayashi, M.; Okino, N.; Ito, M.
Molecular cloning of a Pinguiochrysis pyriformis oleate-specific microsomal DELTA12-fatty acid desaturase and functional analysis in yeasts and thraustochytrids
J. Biochem.
150
375-383
2011
Pinguiochrysis pyriformis
brenda
Zhou, X.; Green, A.; Singh, S.
Caenorhabditis elegans ?12-desaturase FAT-2 is a bifunctional desaturase able to desaturate a diverse range of fatty acid substrates at the DELTA12 and DELTA15 positions
J. Biol. Chem.
286
43644-43650
2011
Caenorhabditis elegans
brenda
Matsuda, T.; Sakaguchi, K.; Hamaguchi, R.; Kobayashi, T.; Abe, E.; Hama, Y.; Hayashi, M.; Honda, D.; Okita, Y.; Sugimoto, S.; Okino, N.; Ito, M.
Analysis of DELTA12-fatty acid desaturase function revealed that two distinct pathways are active for the synthesis of PUFAs in T. aureum ATCC 34304
J. Lipid Res.
53
1210-1222
2012
Thraustochytrium aureum, Thraustochytrium aureum ATCC 3404
brenda
Shi, J.; Cao, Y.; Fan, X.; Li, M.; Wang, Y.; Ming, F.
A rice microsomal delta-12 fatty acid desaturase can enhance resistance to cold stress in yeast and Oryza sativa
Mol. Breed.
29
743-757
2012
Oryza sativa
-
brenda
Jung, J.H.; Kim, H.; Go, Y.S.; Lee, S.B.; Hur, C.G.; Kim, H.U.; Suh, M.C.
Identification of functional BrFAD2-1 gene encoding microsomal delta-12 fatty acid desaturase from Brassica rapa and development of Brassica napus containing high oleic acid contents
Plant Cell Rep.
30
1881-1892
2011
Brassica rapa
brenda
Guan, L.; Xu, Y.; Wang, Y.; Chen, L.; Shao, J.; Wu, W.
Isolation and characterization of a temperature-regulated microsomal oleate desaturase gene (CtFAD2-1) from Safflower (Carthamus tinctorius L.)
Plant Mol. Biol. Rep.
30
391-402
2012
Carthamus tinctorius
-
brenda
Kang, J.; Snapp, A.R.; Lu, C.
Identification of three genes encoding microsomal oleate desaturases (FAD2) from the oilseed crop Camelina sativa
Plant Physiol. Biochem.
49
223-229
2011
Camelina sativa
brenda
Kearns, E.V.; Hugly, S.; Somerville, C.R.
The role of cytochrome b5 in DELTA12 desaturation of oleic acid by microsomes of safflower (Carthamus tinctorius L.)
Arch. Biochem. Biophys.
284
431-436
1991
Carthamus tinctorius
brenda
Smith, M.A.; Cross, A.R.; Jones, O.T.; Griffiths, W.T.; Stymne, S.; Stobart, K.
Electron-transport components of the 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine DELTA 12-desaturase (DELTA12-desaturase) in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons
Biochem. J.
272
23-29
1990
Carthamus tinctorius, Carthamus tinctorius var High Linoleate
brenda
Smith, M.A.; Jonsson, L.; Stymne, S.; Stobart, K.
Evidence for cytochrome b5 as an electron donor in ricinoleic acid biosynthesis in microsomal preparations from developing castor bean (Ricinus communis L.)
Biochem. J.
287
141-144
1992
Ricinus communis
brenda
Sperling, P.; Schmidt, H.; Heinz, E.
A cytochrome-b5-containing fusion protein similar to plant acyl lipid desaturases
Eur. J. Biochem.
232
798-805
1995
Helianthus annuus
brenda
Miquel, M.; Browse, J.
Arabidopsis mutants deficient in polyunsaturated fatty acid synthesis. Biochemical and genetic characterization of a plant oleoyl-phosphatidylcholine desaturase
J. Biol. Chem.
267
1502-1509
1992
Arabidopsis thaliana
brenda
Caiveau, O.; Fortune, D.; Cantrel, C.; Zachowski, A.; Moreau, F.
Consequences of omega-6-oleate desaturase deficiency on lipid dynamics and functional properties of mitochondrial membranes of Arabidopsis thaliana
J. Biol. Chem.
276
5788-5794
2001
Arabidopsis thaliana (P46313), Arabidopsis thaliana
brenda
Yang, M.; Xu, Y.
Oleate accumulation, induced by silencing of microsomal omega-6 desaturase, declines with leaf expansion in transgenic tobacco
J. Plant Physiol.
164
23-30
2007
Nicotiana tabacum (Q6DMQ8), Nicotiana tabacum
brenda
Okuley, J.; Lightner, J.; Feldmann, K.; Yadav, N.; Lark, E.; Browse, J.
Arabidopsis FAD2 gene encodes the enzyme that is essential for polyunsaturated lipid synthesis
Plant Cell
6
147-158
1994
Arabidopsis thaliana (P46313)
brenda
Kumar, R.; Tran, L.S.; Neelakandan, A.K.; Nguyen, H.T.
Higher plant cytochrome b5 polypeptides modulate fatty acid desaturation
PLoS ONE
7
e31370
2012
Arabidopsis thaliana (P46313), Glycine max
brenda
Dehghan Nayeri, F.; Yarizade, K.
Bioinformatics study of delta-12 fatty acid desaturase 2 (FAD2) gene in oilseeds
Mol. Biol. Rep.
41
5077-5087
2014
Linum usitatissimum (B7ST72), Arachis hypogaea (E1A444), Linum grandiflorum (G4Y082), Helianthus annuus (Q8W2F0), Sesamum indicum (Q9LLL7), Vernonia galamensis (Q9SP28)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.14.19.22)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
