Cloned (Comment) | Organism |
---|---|
recombinant enzyme expression in Saccharomyces cerevisiae double deficient ole1 elo1 strain | Choristoneura rosaceana |
recombinant enzyme expression in Saccharomyces cerevisiae double deficient ole1 elo1 strain | Choristoneura parallela |
Protein Variants | Comment | Organism |
---|---|---|
16del_E | site-directed mutagenesis, the product E/Z isomer ratio is 33:67 | Choristoneura rosaceana |
A161G_T163M | site-directed mutagenesis, the product E/Z isomer ratio is 36:64 | Choristoneura rosaceana |
A88S | site-directed mutagenesis, the product E/Z isomer ratio is 32:68 | Choristoneura rosaceana |
D258E | site-directed mutagenesis, mutating the aspartic acid into glutamic acid transforms the Choristoneura parallela enzyme into a desaturase with Choristoneura rosaceana-like activity that produces a mixture of (11Z)-tetradecenoate and (11E)-tetradecenoate in a 64:36 E/Z product ratio | Choristoneura parallela |
E258D | site-directed mutagenesis, mutating the glutamic acid into aspartic acid transforms the Choristoneura rosaceana enzyme into a desaturase with Choristoneura parallela-like activity that produces an almost pure (11E)-tetradecenoate product | Choristoneura rosaceana |
E258D | site-directed mutagenesis, mutating the glutamic acid into aspartic acid transforms the Choristoneura rosaceana enzyme into a desaturase with Choristoneura parallela-like activity that produces an almost pure (11E)-tetradecenoate product, the product E/Z isomer ratio is 86:14 | Choristoneura rosaceana |
F252L | site-directed mutagenesis, the product E/Z isomer ratio is 33:67 | Choristoneura rosaceana |
H116N_I118V | site-directed mutagenesis, the product E/Z isomer ratio is 42:58 | Choristoneura rosaceana |
I103M | site-directed mutagenesis, the product E/Z isomer ratio is 36:64 | Choristoneura rosaceana |
I174V | site-directed mutagenesis, the product E/Z isomer ratio is 35:65 | Choristoneura rosaceana |
I65V | site-directed mutagenesis, the product E/Z isomer ratio is 35:65 | Choristoneura rosaceana |
K286Q | site-directed mutagenesis, the product E/Z isomer ratio is 35:65 | Choristoneura rosaceana |
K309N | site-directed mutagenesis, the product E/Z isomer ratio is 34:66 | Choristoneura rosaceana |
L12M | site-directed mutagenesis, the product E/Z isomer ratio is 31:69 | Choristoneura rosaceana |
L19W | site-directed mutagenesis, the product E/Z isomer ratio is 34:66 | Choristoneura rosaceana |
L69I | site-directed mutagenesis, the product E/Z isomer ratio is 30:70 | Choristoneura rosaceana |
M250I_T251A | site-directed mutagenesis, the product E/Z isomer ratio is 35:65 | Choristoneura rosaceana |
N259S | site-directed mutagenesis, the product E/Z isomer ratio is 31:69 | Choristoneura rosaceana |
Q33E | site-directed mutagenesis, inactive mutant | Choristoneura rosaceana |
S109A | site-directed mutagenesis, inactive mutant | Choristoneura rosaceana |
T95A | site-directed mutagenesis, the product E/Z isomer ratio is 35:65 | Choristoneura rosaceana |
V321I | site-directed mutagenesis, the product E/Z isomer ratio is 35:65 | Choristoneura rosaceana |
W45G | site-directed mutagenesis, the product E/Z isomer ratio is 31:69 | Choristoneura rosaceana |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
endoplasmic reticulum membrane | topological model of CroD11 desaturase spanning the endoplasmic reticulum membrane | Choristoneura rosaceana | 5789 | - |
endoplasmic reticulum membrane | topological model of CroD11 desaturase spanning the endoplasmic reticulum membrane | Choristoneura parallela | 5789 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
myristate + 2 ferrocytochrome b5 + O2 + 2 H+ | Choristoneura parallela | - |
(11E)-11-tetradecenoate + 2 ferricytochrome b5 + 2 H2O | - |
? | |
myristate + 2 ferrocytochrome b5 + O2 + 2 H+ | Choristoneura rosaceana | - |
(Z)-11-tetradecenoate + (E)-11-tetradecenoate + 2 ferricytochrome b5 + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Choristoneura parallela | Q6A4M5 | - |
- |
Choristoneura rosaceana | Q8ISS3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | structure-function analysis determing the stereochemistry of the product formation | Choristoneura parallela | ? | - |
? | |
additional information | structure-function analysis determing the stereochemistry of the product formation. Residue E258 in the cytosolic carboxyl terminus of the protein is critical for the Z specific activity of the Choristoneura rosaceana desaturase | Choristoneura rosaceana | ? | - |
? | |
myristate + 2 ferrocytochrome b5 + O2 + 2 H+ | - |
Choristoneura parallela | (11E)-11-tetradecenoate + 2 ferricytochrome b5 + 2 H2O | - |
? | |
myristate + 2 ferrocytochrome b5 + O2 + 2 H+ | - |
Choristoneura rosaceana | (Z)-11-tetradecenoate + (E)-11-tetradecenoate + 2 ferricytochrome b5 + 2 H2O | - |
? | |
myristate + 2 ferrocytochrome b5 + O2 + 2 H+ | - |
Choristoneura rosaceana | (11Z)-tetradecenoate + (11E)-tetradecenoate + 2 ferricytochrome b5 + 2 H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
acyl-CoA Z/E11 desaturase | UniProt | Choristoneura rosaceana |
CroDELTA11 desaturase | - |
Choristoneura rosaceana |
CroDELTA11 desaturase | - |
Choristoneura parallela |
DELTA11 desaturase | - |
Choristoneura rosaceana |
DELTA11 desaturase | - |
Choristoneura parallela |
More | cf. EC 1.14.19.5 | Choristoneura rosaceana |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome b5 | - |
Choristoneura rosaceana | |
cytochrome b5 | - |
Choristoneura parallela |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the fatty acid desaturase type 1 family | Choristoneura rosaceana |
evolution | the enzyme belongs to the fatty acid desaturase type 1 family | Choristoneura parallela |
additional information | the 258E/D residue contributes to the formation of the secondary coordination sphere of the dimetal unit, along with 129D, 133D and 228N, molecular docking study, overview. This residue might be influencing the shape of the reactive cavity and may play an important role in the catalytic property of this desaturase. Residue D258 in the cytosolic carboxyl terminus of the protein is critical for the steroechmistry of activity | Choristoneura parallela |
additional information | the 258E/D residue contributes to the formation of the secondary coordination sphere of the dimetal unit, along with 129D, 133D and 228N, molecular docking study, overview. This residue might be influencing the shape of the reactive cavity and may play an important role in the catalytic property of this desaturase. Residue E258 in the cytosolic carboxyl terminus of the protein is critical for the steroechmistry of activity | Choristoneura rosaceana |