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Information on EC 1.14.19.33 - DELTA12 acyl-lipid conjugase (11E,13E-forming)
for references in articles please use BRENDA:EC1.14.19.33
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
1.14.19.33 DELTA12 acyl-lipid conjugase (11E,13E-forming)
IUBMB Comments
The enzyme, characterized from the plants Impatiens balsamina, Momordica charantia (bitter gourd) and Vernicia fordii (tung tree), converts a single cis double bond at carbon 12 to two conjugated trans bonds at positions 11 and 13. The enzyme from Vernicia fordii can also act as a 12(E) desaturase when acting on the monounsaturated fatty acids oleate and palmitoleate. cf. EC 1.14.19.16, linoleoyl-lipid Δ12 conjugase (11E,13Z-forming).
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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2
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2
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Synonyms
DELTA12 desaturase, DELTA12 oleate desaturase, FADX, FADX-1A, FADX-1B, FADX-2, fatty acid DELTA12-conjugase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FADX
fatty acid DELTA12-conjugase
FADX
-
-
-
-
fatty acid DELTA12-conjugase
-
-
ambiguous
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(2)
-
-
-
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(2)
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(1)
-
-
-
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(1)
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PATHWAY SOURCE
PATHWAYS
MetaCyc
alpha-eleostearate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
DELTA12 acyl-lipid,ferrocytochrome-b5:oxygen 11,14 allylic oxidase (11E,13E-forming)
The enzyme, characterized from the plants Impatiens balsamina, Momordica charantia (bitter gourd) and Vernicia fordii (tung tree), converts a single cis double bond at carbon 12 to two conjugated trans bonds at positions 11 and 13. The enzyme from Vernicia fordii can also act as a 12(E) desaturase when acting on the monounsaturated fatty acids oleate and palmitoleate. cf. EC 1.14.19.16, linoleoyl-lipid Delta12 conjugase (11E,13Z-forming).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(6Z,9Z,12Z)-octadeca-6,9,12-trienoate + 2 ferrocytochrome b5 + O2 + 2 H+
(6Z,9Z,11E,13E)-octadeca-6,9,11,13-tetraenoate + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
(9Z)-hexadecenoate + 2 ferrocytochrome b5 + O2 + 2 H+
(9Z,12E)-hexadeca-9,12-dienoate + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
(9Z)-octadecenoate + 2 ferrocytochrome b5 + O2 + 2 H+
(9Z,12E)-octadeca-9,12-dienoate + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
octadec-9-ynoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
(13Z)-octadecen-13-en-9-ynoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
?
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
?
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
?
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: the enzyme is involved in the biosynthetic pathway of eleostearic acid
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
?
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
?
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
?
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
?
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: the enzyme is involved in the biosynthetic pathway of eleostearic acid
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
?
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: the double bond introduced by FADX during fatty acid desaturation is in the trans, rather than cis, configuration
Products: -
Products: -
?
octadec-9-ynoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
(13Z)-octadecen-13-en-9-ynoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: 0.7% conversion
Products: -
Products: -
?
octadec-9-ynoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
(13Z)-octadecen-13-en-9-ynoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: 0.8% conversion
Products: -
Products: -
?
octadec-9-ynoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
(13Z)-octadecen-13-en-9-ynoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: 18.7% conversion
Products: -
Products: -
?
octadec-9-ynoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
(13Z)-octadecen-13-en-9-ynoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the FADX group enzymes have no detectable DELTA12 FAD activity but instead catalyze cis-DELTA13 desaturation of stearolic acid
Products: -
Products: -
?
additional information
?
-
Substrates: the FADX group enzymes have no detectable DELTA12 FAD activity but instead catalyze cis-DELTA13 desaturation of stearolic acid
Products: -
Products: -
?
additional information
?
-
Substrates: the FADX group enzymes have no detectable DELTA12 FAD activity but instead catalyze cis-DELTA13 desaturation of stearolic acid
Products: -
Products: -
?
additional information
?
-
Substrates: the wild-type enzyme produces predominantly conjugated alpha-eleostearic acid and little punicic acid from its substrate linoleic acid. The helix 2 and the first histidine box are a determinant of conjugase product partitioning into alpha-punicic acid ((9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate) or alpha-eleostearic acid ((9Z,11E,13E)-octadeca-9,11,13-trienoate), sequence comparisons, overview. Residues 111 and 115 of the enzyme exhibit an interactive effect in punicic acid formation
Products: -
Products: -
?
additional information
?
-
Substrates: linoleic acid serves as a precursor for punicic acid synthesis by the enzyme
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the conversion of the DELTA12-double bond of linoleic acid (18:2DELTA9cis,12cis) into conjugated DELTA11trans and DELTA13cis-double bonds
Products: -
Products: -
?
additional information
?
-
Substrates: the FADX group enzymes have no detectable DELTA12 FAD activity but instead catalyze cis-DELTA13 desaturation of stearolic acid
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is capable of generating a variety of alternative conjugated and 12-desaturated fatty acid products in yeast cells cultured in the presence of exogenously supplied fatty acid substrates
Products: -
Products: -
?
additional information
?
-
Substrates: a bifunctional enzyme also exhibiting the activity of EC 1.14.19.34
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
?
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
?
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: the enzyme is involved in the biosynthetic pathway of eleostearic acid
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
Products: alpha-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
?
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
?
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
?
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Substrates: the enzyme is involved in the biosynthetic pathway of eleostearic acid
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
Products: alpha-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
?
additional information
?
-
Substrates: the FADX group enzymes have no detectable DELTA12 FAD activity but instead catalyze cis-DELTA13 desaturation of stearolic acid
Products: -
Products: -
?
additional information
?
-
Substrates: the FADX group enzymes have no detectable DELTA12 FAD activity but instead catalyze cis-DELTA13 desaturation of stearolic acid
Products: -
Products: -
?
additional information
?
-
Substrates: the FADX group enzymes have no detectable DELTA12 FAD activity but instead catalyze cis-DELTA13 desaturation of stearolic acid
Products: -
Products: -
?
additional information
?
-
Substrates: linoleic acid serves as a precursor for punicic acid synthesis by the enzyme
Products: -
Products: -
?
additional information
?
-
Substrates: the FADX group enzymes have no detectable DELTA12 FAD activity but instead catalyze cis-DELTA13 desaturation of stearolic acid
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
tung FADX is grouped with DELTA12 fatty acid desaturases and hydroxylases rather than conjugases, which is consistent with its desaturase activity
physiological function
FADX converts linoleic acid into alpha-eleostearic acid. in the plant seed oil
additional information
incubation of yeast cells expressing FADX with exogenously supplied palmitoleicacid leads to substantial incorporation of thisfatty acid into yeast cells, accounting for approximately79% of total fatty acids. Oleic acid is reduced to only 3% under these growth conditions
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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). FADX_IMPBA
383
5
44743
Swiss-Prot
other Location (Reliability: 2)
FADX_MOMCH
399
6
45570
Swiss-Prot
other Location (Reliability: 2)
FADX_VERFO
386
5
44375
Swiss-Prot
other Location (Reliability: 5)
U5LN76_9MAGN
379
0
43085
TrEMBL
other Location (Reliability: 2)
U5LP51_9MAGN
379
0
43107
TrEMBL
other Location (Reliability: 4)
U5LP87_9MAGN
379
0
42994
TrEMBL
other Location (Reliability: 2)
U5LRN8_9MAGN
383
0
43894
TrEMBL
Secretory Pathway (Reliability: 1)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D115E
site-directed mutagenesis, the mutant shows reaction product like the wild-type enzyme, predominantly alpha-eleostearic acid and little punicic acid
G111V
site-directed mutagenesis, the mutant shows reaction product like the wild-type enzyme, predominantly alpha-eleostearic acid and little punicic acid
G111V/D115E
site-directed mutagenesis, the mutant shows reaction product unlike the wild-type enzyme, approximately equal amounts of alpha-eleostearic acidandits isomer, punicic acid
additional information
construction of a series of Momordica charantia FADX-Arabidopsis thaliana FAD2 chimeras: chimera 1 contains Momordica FADX amino acids 1-157 and Arabidopsis FAD2 amino acids 149-383, chimera 2 contains FADX aa 1210 with FAD2 aa 202-383, chimera 3 contains FADX aa 1-252 with FAD2 aa 244-383, chimera 4 contains FADX aa 1-326 with FAD2 aa 317-383, chimera 5 contains FAD2 aa 1-52 with FADX aa 61-399, chimera 6 contains FAD2 aa 1-83 with FADX aa 93-399, chimera 7 contains FAD2 aa 1-116 with FADX aa 126-399, and chimera 8 containsFAD2 aa 1-148 with FADX aa 158-399, mutant product formations, overview. Analysis of a FADX mutant containing six substitutions in which the sequence of helix 2 and first histidine box is converted to that of FAD2
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae and somatic embryos of Glycine max
gene FADX, combined transgenic expression of Punica granatum conjugase (FADX) under the control of a seed-specific napin promoter and Arabidopsis thaliana FAD2 desaturase, EC 1.14.19.34, in high linoleic acid Arabidopsis thaliana fad3/fae1 mutant, via Agrobacterium tumefaciens cell strain GV3101 transformation, leads to increased accumulation of punicic acid, quantitative RT-PCR enzyme expression analysis. Arabidopsis thaliana seeds overexpressing PgFADX show accumulation of punicic acid up to 9.2% average in tandem lines (6.43% in lines expressing FADX alone), highest content in line NCJ-11 is 11.26%, phenotypes, overview. Overexpression of PgFADX affects the activity of the native Arabidopsis thaliana FAD2 desaturase, the relative AtFAD2 expression level is significantly reduced up to 99%
gene FADX, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis, recombinant expression in Saccharomyces cerevisiae strains ole1 and INVSc1 in microsomes. Santalaceae FADX expressed in yeast has no detectable DELTA12 desaturase activity either acting on native fatty acids or when supplied with exogenous substrates but instead shows cis-DELTA13 desaturation activity on stearolic acid
gene FADX, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional expression of the enzyme in Saccharomyces cerevisiae strain MMYO11, transient expression of myc-tagged enzyme in Nicotiana tabacum cv. Bright-Yellow 2 suspension-cultured BY-2 cells
gene FADX, sequence comparisons, recombinant expression of enzyme mutant chimeras in the Arabidopsis thaliana fad3fae1 mutant strain, lacks the activity of both the endoplasmic reticulum omega-3 desaturase (FAD3) and the fatty acid elongation 1 (FAE1)-condensing enzyme, as well as elevated levels of linoleic acid
gene FADX-1A, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis, recombinant expression in Saccharomyces cerevisiae strains ole1 and INVSc1 in microsomes. Santalaceae FADX expressed in yeast has no detectable DELTA12 desaturase activity either acting on native fatty acids or when supplied with exogenous substrates but instead shows cis-DELTA13 desaturation activity on stearolic acid
gene FADX-1B, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis, recombinant expression in Saccharomyces cerevisiae strains ole1 and INVSc1 in microsomes. Santalaceae FADX expressed in yeast has no detectable DELTA12 desaturase activity either acting on native fatty acids or when supplied with exogenous substrates but instead shows cis-DELTA13 desaturation activity on stearolic acid
gene FADX-2, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis, recombinant expression in Saccharomyces cerevisiae strains ole1 and INVSc1 in microsomes. Santalaceae FADX expressed in yeast has no detectable DELTA12 desaturase activity either acting on native fatty acids or when supplied with exogenous substrates but instead shows cis-DELTA13 desaturation activity on stearolic acid
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dyer, J.M.; Chapital, D.C.; Kuan, J.C.; Mullen, R.T.; Turner, C.; McKeon, T.A.; Pepperman, A.B.
Molecular analysis of a bifunctional fatty acid conjugase/desaturase from tung. Implications for the evolution of plant fatty acid diversity
Plant Physiol.
130
2027-2038
2002
Vernicia fordii (Q8GZC2)
brenda
Cahoon, E.B.; Carlson, T.J.; Ripp, K.G.; Schweiger, B.J.; Cook, G.A.; Hall, S.E.; Kinney, A.J.
Biosynthetic origin of conjugated double bonds: production of fatty acid components of high-value drying oils in transgenic soybean embryos
Proc. Natl. Acad. Sci. USA
96
12935-12940
1999
Impatiens balsamina (Q9SP62), Momordica charantia (Q9SP61)
brenda
Rawat, R.; Yu, X.H.; Sweet, M.; Shanklin, J.
Conjugated fatty acid synthesis: residues 111 and 115 influence product partitioning of Momordica charantia conjugase
J. Biol. Chem.
287
16230-16237
2012
Momordica charantia (Q9SP61)
brenda
Okada, S.; Zhou, X.R.; Damcevski, K.; Gibb, N.; Wood, C.; Hamberg, M.; Haritos, V.S.
Diversity of DELTA12 fatty acid desaturases in santalaceae and their role in production of seed oil acetylenic fatty acids
J. Biol. Chem.
288
32405-32413
2013
Exocarpos cupressiformis (U5LN76), Exocarpos cupressiformis (U5LP51), Exocarpos cupressiformis (U5LP87), Santalum acuminatum (U5LRN8)
brenda
Mietkiewska, E.; Miles, R.; Wickramarathna, A.; Sahibollah, A.F.; Greer, M.S.; Chen, G.; Weselake, R.J.
Combined transgenic expression of Punica granatum conjugase (FADX) and FAD2 desaturase in high linoleic acid Arabidopsis thaliana mutant leads to increased accumulation of punicic acid
Planta
240
575-583
2014
Punica granatum (Q84UB8)
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.19.33)
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Release 2023.1 (January 2023)
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