BRENDA - Enzyme Database
show all sequences of 1.14.19.34

Dimorphecolic acid is synthesized by the coordinate activities of two divergent DELTA12-oleic acid desaturases

Cahoon, E.B.; Kinney, A.J.; J. Biol. Chem. 279, 12495-12502 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene DsFAD2-1, DNA and amino acid sequence determination and analysis, recombinant expression of DsFAD2-1 in Saccharomyces cerevisiae strain YPH499 and Glycine max somatic embryos resulting in the accumulation of the trans-DELTA12 isomer of linoleic acid (18:29cis,12trans) rather than the more typical cis-DELTA12 isomer. When co-expressed with DsFAD2-1 in soybean embryos or yeast, DsFAD2-2 converts 18:29cis,12trans into dimorphecolic acid; gene DsFAD2-2, DNA and amino acid sequence determination and analysis, recombinant expression of DsFAD2-2 in Saccharomyces cerevisiae strain YPH499 and Glycine max somatic embryos. When co-expressed with DsFAD2-1 in soybean embryos or yeast, DsFAD2-2 converts 18:29cis,12trans into dimorphecolic acid. When DsFAD2-2 is expressed alone in soybean embryos or together with a typical cis-DELTA12-oleic acid desaturase in yeast, trace amounts of the cis-DELTA12 isomer of dimorphecolic acid (9-OH-18:2DELTA9cis,12cis) are formed from DsFAD2-2 activity with cis-DELTA12-linoleic acid
Dimorphotheca sinuata
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
diiron-oxo center
Dimorphotheca sinuata
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
Dimorphotheca sinuata
-
a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
-
-
?
additional information
Dimorphotheca sinuata
seeds of Dimorphotheca species fatty acids contains structural features that are not typically found in plant fatty acids, including a C-9 hydroxyl group, DELTA10,DELTA12-conjugated double bonds, and trans-DELTA12 unsaturation
?
-
-
-
additional information
Dimorphotheca sinuata
seeds of Dimorphotheca species fatty acids contains structural features that are not typically found in plant fatty acids, including a C-9 hydroxyl group, DELTA10,DelTA12-conjugated double bonds, and trans-DELTA12 unsaturation.
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Dimorphotheca sinuata
Q6RS95
gene DsFAD2-1
-
Dimorphotheca sinuata
Q6RS96
gene DsFAD2-2
-
Reaction
Reaction
Commentary
Organism
an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
proposed mechanism of DsFAD2-2: removal of a C-11 hydrogen atom from trans-DELTA12-linoleic acid by the diiron-oxo center of DsFAD2-2 results in the shift of the cis-DELTA9 double bond to the trans-DELTA10 position. The radical remaining at the C-9 position is then able to remove an oxygen atom from the diiron-oxo center because of close proximity to the catalytic core of DsFAD2-2 as dictated by the substrate binding properties of this enzyme
Dimorphotheca sinuata
Source Tissue
Source Tissue
Commentary
Organism
Textmining
seed
;
Dimorphotheca sinuata
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
-
734145
Dimorphotheca sinuata
a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
additional information
seeds of Dimorphotheca species fatty acids contains structural features that are not typically found in plant fatty acids, including a C-9 hydroxyl group, DELTA10,DELTA12-conjugated double bonds, and trans-DELTA12 unsaturation
734145
Dimorphotheca sinuata
?
-
-
-
-
additional information
seeds of Dimorphotheca species fatty acids contains structural features that are not typically found in plant fatty acids, including a C-9 hydroxyl group, DELTA10,DelTA12-conjugated double bonds, and trans-DELTA12 unsaturation.
734145
Dimorphotheca sinuata
?
-
-
-
-
additional information
isozyme DsFAD2-2 catalyzes the conversion of the DELTA9 double bond of linoleic acid into a C-9 hydroxyl group and DELTA10trans double bond and displays a substrate preference for the trans-DELTA12, rather than the cis-DELTA12, isomer of linoleic acid
734145
Dimorphotheca sinuata
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome b5
-
Dimorphotheca sinuata
Cloned(Commentary) (protein specific)
Commentary
Organism
gene DsFAD2-1, DNA and amino acid sequence determination and analysis, recombinant expression of DsFAD2-1 in Saccharomyces cerevisiae strain YPH499 and Glycine max somatic embryos resulting in the accumulation of the trans-DELTA12 isomer of linoleic acid (18:29cis,12trans) rather than the more typical cis-DELTA12 isomer. When co-expressed with DsFAD2-1 in soybean embryos or yeast, DsFAD2-2 converts 18:29cis,12trans into dimorphecolic acid
Dimorphotheca sinuata
gene DsFAD2-2, DNA and amino acid sequence determination and analysis, recombinant expression of DsFAD2-2 in Saccharomyces cerevisiae strain YPH499 and Glycine max somatic embryos. When co-expressed with DsFAD2-1 in soybean embryos or yeast, DsFAD2-2 converts 18:29cis,12trans into dimorphecolic acid. When DsFAD2-2 is expressed alone in soybean embryos or together with a typical cis-DELTA12-oleic acid desaturase in yeast, trace amounts of the cis-DELTA12 isomer of dimorphecolic acid (9-OH-18:2DELTA9cis,12cis) are formed from DsFAD2-2 activity with cis-DELTA12-linoleic acid
Dimorphotheca sinuata
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome b5
-
Dimorphotheca sinuata
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
diiron-oxo center
Dimorphotheca sinuata
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
Dimorphotheca sinuata
-
a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
-
-
?
additional information
Dimorphotheca sinuata
seeds of Dimorphotheca species fatty acids contains structural features that are not typically found in plant fatty acids, including a C-9 hydroxyl group, DELTA10,DELTA12-conjugated double bonds, and trans-DELTA12 unsaturation
?
-
-
-
additional information
Dimorphotheca sinuata
seeds of Dimorphotheca species fatty acids contains structural features that are not typically found in plant fatty acids, including a C-9 hydroxyl group, DELTA10,DelTA12-conjugated double bonds, and trans-DELTA12 unsaturation.
?
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
seed
-
Dimorphotheca sinuata
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+
-
734145
Dimorphotheca sinuata
a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
additional information
seeds of Dimorphotheca species fatty acids contains structural features that are not typically found in plant fatty acids, including a C-9 hydroxyl group, DELTA10,DELTA12-conjugated double bonds, and trans-DELTA12 unsaturation
734145
Dimorphotheca sinuata
?
-
-
-
-
additional information
seeds of Dimorphotheca species fatty acids contains structural features that are not typically found in plant fatty acids, including a C-9 hydroxyl group, DELTA10,DelTA12-conjugated double bonds, and trans-DELTA12 unsaturation.
734145
Dimorphotheca sinuata
?
-
-
-
-
additional information
isozyme DsFAD2-2 catalyzes the conversion of the DELTA9 double bond of linoleic acid into a C-9 hydroxyl group and DELTA10trans double bond and displays a substrate preference for the trans-DELTA12, rather than the cis-DELTA12, isomer of linoleic acid
734145
Dimorphotheca sinuata
?
-
-
-
-
General Information
General Information
Commentary
Organism
evolution
the evolution of two divergent DELTA12-oleic acid desaturases for the biosynthesis of an unusual fatty acid; the evolution of two divergent DELTA12-oleic acid desaturases for the biosynthesis of an unusual fatty acid
Dimorphotheca sinuata
metabolism
biosynthetic pathway of dimorphecolic acid involving the concerted activities of DsFAD2-1 and DsFAD2-2; biosynthetic pathway of dimorphecolic acid involving the concerted activities of DsFAD2-1 and DsFAD2-2
Dimorphotheca sinuata
physiological function
involvement of DsFAD2-1 in dimorphecolic acid synthesis; involvement of DsFAD2-2 in dimorphecolic acid synthesis
Dimorphotheca sinuata
General Information (protein specific)
General Information
Commentary
Organism
evolution
the evolution of two divergent DELTA12-oleic acid desaturases for the biosynthesis of an unusual fatty acid
Dimorphotheca sinuata
metabolism
biosynthetic pathway of dimorphecolic acid involving the concerted activities of DsFAD2-1 and DsFAD2-2
Dimorphotheca sinuata
physiological function
involvement of DsFAD2-1 in dimorphecolic acid synthesis
Dimorphotheca sinuata
physiological function
involvement of DsFAD2-2 in dimorphecolic acid synthesis
Dimorphotheca sinuata
Other publictions for EC 1.14.19.34
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
734991
Mietkiewska
Combined transgenic expression ...
Punica granatum
Planta
240
575-583
2014
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734145
Cahoon
Dimorphecolic acid is synthesi ...
Dimorphotheca sinuata
J. Biol. Chem.
279
12495-12502
2004
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6
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732650
Dyer
Molecular analysis of a bifunc ...
Vernicia fordii
Plant Physiol.
130
2027-2038
2002
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