Information on EC 1.14.19.5 - acyl-CoA 11-(Z)-desaturase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.19.5
-
RECOMMENDED NAME
GeneOntology No.
acyl-CoA 11-(Z)-desaturase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + reduced acceptor + O2 = Delta11-acyl-CoA + acceptor + 2 H2O
show the reaction diagram
an acyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = an (11Z)-enoyl-CoA + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
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-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bombykol biosynthesis
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Spodoptera littoralis pheromone biosynthesis
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-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (11,12 cis-dehydrogenating)
The enzyme introduces a cis double bond at position C-11 of saturated fatty acyl-CoAs. In moths the enzyme participates in the biosynthesis of their sex pheromones. The enzyme from the marine microalga Thalassiosira pseudonana is specific for palmitoyl-CoA (16:0) [4], that from the leafroller moth Choristoneura rosaceana desaturates myristoyl-CoA (14:0) [5], while that from the moth Spodoptera littoralis accepts both substrates [1]. The enzyme contains three histidine boxes that are conserved in all desaturases [2]. It is membrane-bound, and contains a cytochrome b5-like domain at the N-terminus that serves as the electron donor for the active site of the desaturase.
CAS REGISTRY NUMBER
COMMENTARY hide
199543-17-4
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77000-04-5
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the enzyme belongs to the fatty acid desaturase type 1 family
metabolism
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functional expression of Dpu-DELTA11-APSQ cDNA belonging to the D11-subfamily, shows that is catalyses the formation of unsaturated fatty acyls that can be chain-shortened by beta-oxidation and subsequently reduced to the alcohol components; functional expression of Dpu-DELTA11-LPAE cDNA belonging to the D11-subfamily, shows that is catalyses the formation of unsaturated fatty acyls that can be chain-shortened by beta-oxidation and subsequently reduced to the alcohol components
physiological function
additional information
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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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Z)-11-tetradecenoyl-CoA + reduced acceptor + O2
(E,E)-10,12-tetradecadienoyl-CoA + acceptor + H2O
show the reaction diagram
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(E,E)-10,12-tetradecadienoic acid is produced from (Z)-11-tetradecenoic acid by desaturation and concomitant migration of the precursor double bond
-
-
?
methyl myristate + reduced electron acceptor + O2
methyl (11E)-tetradec-11-enoate + methyl (11Z)-tetradec-11-enoate + acceptor + H2O
show the reaction diagram
myristic acid + 2 ferrocytochrome b5 + O2 + 2 H+
(Z)-11-tetradecenoate + (E)-11-tetradecenoate + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
-
-
-
-
?
myristic acid + NADH + ?
tetradec-11-enoic acid + NAD+ + ?
show the reaction diagram
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50% of the activity with palmitic acid
-
-
?
myristic acid + reduced acceptor + O2
(Z)-tetradec-11-enoic acid + (E)-tetradec-11-enoic acid + acceptor + H2O
show the reaction diagram
-
-
-
?
myristoyl-CoA + reduced acceptor + O2
(Z)-11-tetradecenoyl-CoA + acceptor + 2 H2O
show the reaction diagram
myristoyl-CoA + reduced acceptor + O2
(Z)-11-tetradecenoyl-CoA + acceptor + H2O
show the reaction diagram
myristoyl-CoA + reduced acceptor + O2
(Z)-tridec-11-enoyl-CoA + (E)-tridec-11-enoyl-CoA + acceptor + H2O
show the reaction diagram
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reaction involves a first slow, isotpe-sensitive C11-H bond cleavage, with probable formation of an unstable intermediate, followed by a second fast C12-H bond removal
-
-
?
palmitic acid + NADH + ?
(Z)-hexadec-11-enoic acid + NAD+ + ?
show the reaction diagram
-
-
-
-
?
palmitic acid + reduced acceptor + O2
(Z)-11-hexadecenoic acid + acceptor + H2O
show the reaction diagram
-
-
-
-
?
palmitic acid + reduced acceptor + O2
(Z)-hexadec-11-enoic acid + acceptor + H2O
show the reaction diagram
palmitic acid + reduced acceptor + O2
hexadec-11-enoic acid + acceptor + 2 H2O
show the reaction diagram
palmitoyl-CoA + NADH + ?
(Z)-hexadec-11-enoyl-CoA + NAD+ + ?
show the reaction diagram
-
-
-
-
?
stearic acid + NADH + ?
oleic acid + NAD+ + ?
show the reaction diagram
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18% of the activity with palmitic acid
-
-
?
stearoyl-CoA + reduced acceptor + O2
oleoyl-CoA + acceptor + 2 H2O
show the reaction diagram
-
-
-
?
tetradecanoic acid + O2 + AH2
(11E)-tetradec-11-enoic acid + A + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
myristic acid + 2 ferrocytochrome b5 + O2 + 2 H+
(Z)-11-tetradecenoate + (E)-11-tetradecenoate + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + reduced acceptor + O2
(Z)-11-tetradecenoyl-CoA + acceptor + 2 H2O
show the reaction diagram
palmitic acid + reduced acceptor + O2
hexadec-11-enoic acid + acceptor + 2 H2O
show the reaction diagram
Q6RT18
enzyme is not involved in production of polyunsaturated fatty acids
-
-
?
stearoyl-CoA + reduced acceptor + O2
oleoyl-CoA + acceptor + 2 H2O
show the reaction diagram
O44390
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b5
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-
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NADH
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NADPH is a less effective elctron donor. Highest activity with 1 mM of electron donors, reduced activity below
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11-fluorotetradecanoic acid
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50% inhibition at 1:1 substrate/inhibitor ratio
KCN
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83% inhibition by 1 mM, 95% inhibition by 5 mM
NaN3
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92% inhibition b
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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terminal abdominal segments with pheromone gland of female adults, RT-PCR
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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topological model of CroD11 desaturase spanning the endoplasmic reticulum membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37800
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calculated from cDNA
39000
A9ZSZ6
x * 39000, His-tagged enzyme, SDS-PAGE
40500
A9ZSZ6
x * 40500, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
A9ZSZ6
x * 39000, His-tagged enzyme, SDS-PAGE; x * 40500, calculated from amino acid sequence
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, stable for at least 1 h
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
C-terminal His-tagged fusion protein expressed using recombinant baculoviruses
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DNA and amino acid sequence determination and analysis, recombinant expression of the enzyme as fusion protein with beta-actin from Mamestra brassicae, UniProt ID B0LF73, quantitative real-time PCR enzyme expression analysis
expressed as polyhistidine-tagged protein in elongase 1 and DELTA9 desaturase-deficient yeast cells; expression in Saccharomyces cerevisiae DELTAelo1/DELTAole mutant strain, which is both elongase 1 and DELTA9 desaturase-deficient, using a Cu+2 inducible expression vector, the recombinant expression leads to producing large quantities of C11-monounsaturated fatty acids, mainly (Z)-11-hexadecenoic acid, (E,E)-10,12-tetradecadienoic acid, minor amounts of (E,Z)-10,12-hexadecadienoic acid, and very low amounts of (E,Z)-10,12-tetradecadienoic isomer
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expressed in Sf9 insect cells
A9ZSZ6
expressed in yeast
expression in yeast
gene d2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional expression of MsexAPTQ desaturase in Saccharomyces cerevisiae strain W303
genetic trans-formation of a desaturase-deficient strain of the yeast Sac-charomyces cerevisiae with an expression plasmid encoding PDesat-Tn DELTA11Z results in complementation of the strain's fatty acid auxotrophy and the production of DELTA11 Z-unsaturated fatty acids
heterologously expressed in Saccharomyces cerevisiae
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into a copper-inducible pYEX vector to assess its desaturase activity and then transformed into a desaturase- and elongase-deficient mutant ole1 elo1 yeast strain
partial cDNAs are amplified and cloned into the vector pCold I DNA, recombinant proteins are produced by Escherichia coli BL21 cells and used as antigens to raise antibodies in mice
recombinant enzyme expression in Saccharomyces cerevisiae double deficient ole1 elo1 strain
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16del_E
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site-directed mutagenesis, the product E/Z isomer ratio is 33:67
A161G/T163M
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site-directed mutagenesis, the product E/Z isomer ratio is 36:64
A88S
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site-directed mutagenesis, the product E/Z isomer ratio is 32:68
E258D
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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 (E)-11-tetradecenoate product, the product E/Z isomer ratio is 86:14
F252L
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site-directed mutagenesis, the product E/Z isomer ratio is 33:67
H116N/I118V
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site-directed mutagenesis, the product E/Z isomer ratio is 42:58
I103M
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site-directed mutagenesis, the product E/Z isomer ratio is 36:64
I174V
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site-directed mutagenesis, the product E/Z isomer ratio is 35:65
I65V
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site-directed mutagenesis, the product E/Z isomer ratio is 35:65
K286Q
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site-directed mutagenesis, the product E/Z isomer ratio is 35:65
K309N
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site-directed mutagenesis, the product E/Z isomer ratio is 34:66
L12M
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site-directed mutagenesis, the product E/Z isomer ratio is 31:69
L19W
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site-directed mutagenesis, the product E/Z isomer ratio is 34:66
L69I
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site-directed mutagenesis, the product E/Z isomer ratio is 30:70
M250I/T251A
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site-directed mutagenesis, the product E/Z isomer ratio is 35:65
N259S
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site-directed mutagenesis, the product E/Z isomer ratio is 31:69
Q33E
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site-directed mutagenesis, inactive mutant
S109A
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site-directed mutagenesis, inactive mutant
T95A
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site-directed mutagenesis, the product E/Z isomer ratio is 35:65
V321I
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site-directed mutagenesis, the product E/Z isomer ratio is 35:65
W45G
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site-directed mutagenesis, the product E/Z isomer ratio is 31:69
additional information
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a second non-functional ezi-inserted desaturase gene exists in Ostrinia nubilalis. The non-functionality of ezi-inserted desaturase genes may not be a direct consequence of the insertion of an ezi- or ezi-like element into the gene