Information on EC 1.14.19.33 - DELTA12 acyl-lipid conjugase (11E,13E-forming)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.19.33
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RECOMMENDED NAME
GeneOntology No.
DELTA12 acyl-lipid conjugase (11E,13E-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
PgFADX; gene FADX
SwissProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
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(9Z)-hexadecanoate + 2 ferrocytochrome b5 + O2 + 2 H+
(9Z,12E)-hexadeca-9,12-dienoate + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
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(9Z)-octadecanoate + 2 ferrocytochrome b5 + O2 + 2 H+
(9Z,12E)-octadeca-9,12-dienoate + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
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?
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
octadec-9-ynoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
(13Z)-octadecen-13-en-9-ynoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
additional information
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a gamma-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
an alpha-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b5
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae and somatic embryos of Glycine max
expression in Saccharomyces cerevisiae; 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
expression in 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, 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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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 1–210 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