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Literature summary for 1.14.19.24 extracted from

  • Ding, B.J.; Carraher, C.; Loefstedt, C.
    Sequence variation determining stereochemistry of a DELTA11 desaturase active in moth sex pheromone biosynthesis (2016), Insect Biochem. Mol. Biol., 74, 68-75 .
    View publication on PubMed
Search for more literature for 1.14.19.24

Cloned(Commentary)

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

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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Choristoneura parallela Q6A4M5
-
-
Choristoneura rosaceana Q8ISS3
-
-

Substrates and Products (Substrate)

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

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

Cofactor Comment Organism Structure
cytochrome b5
-
 Choristoneura rosaceana
cytochrome b5
-
 Choristoneura parallela

General Information

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