1.14.19.3: acyl-CoA 6-desaturase
This is an abbreviated version!
For detailed information about acyl-CoA 6-desaturase, go to the full flat file.
Word Map on EC 1.14.19.3
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1.14.19.3
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polyunsaturated
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arachidonic
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desaturation
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pufas
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phospholipid
-
docosahexaenoic
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eicosapentaenoic
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gamma-linolenic
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unsaturated
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cholesterol
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alpha-linolenic
-
elongase
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triglyceride
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la
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lc-pufas
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palmitic
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elovl5
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adipose
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delta-5
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monounsaturated
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triacylglycerols
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stearoyl-coa
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linolenic
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prostaglandin
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phosphatidylcholine
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dihomo-gamma-linolenic
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eicosanoids
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omega-6
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delta5-desaturase
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5-desaturase
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linseed
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borage
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evening
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stearic
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primrose
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teleost
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palmitoleic
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stearidonic
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eczema
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mortierella
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seabream
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alpina
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srebf1
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eicosatrienoic
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synthesis
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nutrition
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safflower
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desaturase-1
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gilthead
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aurata
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flaxseed
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stearoyl
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diagnostics
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drug development
- 1.14.19.3
-
polyunsaturated
-
arachidonic
-
desaturation
-
pufas
- phospholipid
-
docosahexaenoic
-
eicosapentaenoic
-
gamma-linolenic
- unsaturated
- cholesterol
-
alpha-linolenic
- elongase
- triglyceride
- la
-
lc-pufas
-
palmitic
- elovl5
- adipose
-
delta-5
-
monounsaturated
- triacylglycerols
- stearoyl-coa
-
linolenic
- prostaglandin
- phosphatidylcholine
-
dihomo-gamma-linolenic
-
eicosanoids
-
omega-6
- delta5-desaturase
-
5-desaturase
-
linseed
-
borage
-
evening
-
stearic
- primrose
-
teleost
-
palmitoleic
-
stearidonic
- eczema
- mortierella
- seabream
- alpina
-
srebf1
-
eicosatrienoic
- synthesis
- nutrition
- safflower
-
desaturase-1
-
gilthead
- aurata
-
flaxseed
-
stearoyl
- diagnostics
- drug development
Reaction
Synonyms
acyl-CoA DELTA6-desaturase, acyl-CoA desaturase, acyl-CoA-dependent DELTA6-desaturase, AsD6DES, D6 desaturase, d6-des, D6D, D6Des, DEALTA6I, delta 6 desaturase, DELTA 6-desaturase, delta 6-fatty acid desaturase, DELTA-6 desaturase, delta-6 fatty acid desaturase, DELTA-6-desaturase, DELTA6 desaturase, DELTA6 fatty acid desaturase, DELTA6 fatty acyl desaturase, DELTA6-acyl CoA desaturase, DELTA6-acyl-group desaturase, DELTA6-desaturase, DELTA6-desaturase II, DELTA6-fatty acid desaturase, DELTA6-fatty acyl-CoA desaturase, delta61, DELTA6fad_b, DES6, desaturase, fatty acid DA6-, desaturase, linoleate, DesI, EaD6DES, EC 1.14.99.25, FA desaturase 2, FADS2, FADS6, fadsd6, FAT-3, fatty acid 6-desaturase, fatty acid DA6-desaturase, fatty acid DELTA 6-desaturase, fatty acid delta-6 desaturase, fatty acid DELTA6-desaturase, fatty acid desaturase 2, fatty acid desaturase-2, GcFADS2, linoleate desaturase, linoleic acid desaturase, linoleic desaturase, linoleoyl CoA desaturase, linoleoyl-coenzyme A desaturase, long-chain fatty acid DELTA6-desaturase, MaFADS6, MaFADS6-I, Md6, MpFADS6, PiDesD6, TpFADS2
ECTree
1.14.19.3 acyl-CoA 6-desaturaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.14.19.3 - acyl-CoA 6-desaturase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H129G
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity, can be rescued by 150 mM exogenous imidazole
H129R
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity using linoleic acid as substrate
H305G
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity, can be rescued by 150 mM exogenous imidazole
H305R
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity using linoleic acid as substrate
H89G
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, very low enzyme activity, can be rescued by 150 mM exogenous imidazole
H89R
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, very low enzyme activity using linoleic acid as substrate
H129G
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity, can be rescued by 150 mM exogenous imidazole
-
H129R
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity using linoleic acid as substrate
-
H305G
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity, can be rescued by 150 mM exogenous imidazole
-
H89G
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, very low enzyme activity, can be rescued by 150 mM exogenous imidazole
-
H89R
-
expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, very low enzyme activity using linoleic acid as substrate
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D313I
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
D367H
site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme
F310L
site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme
I390L
site-directed mutagenesis, mutant shows similar activity with linoleoyl-CoA and reduced activity with alpha-linolenoyl-CoA compared to the wild-type enzyme
M384S/M385L
site-directed mutagenesis, mutant shows significantly increased activity compared to the wild-type enzyme
N388H
site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme
S306T
site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme
S322A
site-directed mutagenesis, mutant shows highly increased activity compared to the wild-type enzyme
T302V
Y375F
site-directed mutagenesis, mutant shows significantly increased activity compared to the wild-type enzyme
E222S
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is reduced by almost 50% compared to the wild-type enzyme
G194L
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is significantly reduced to 6.50% compared to the wild-type enzyme
M227K
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is reduced by almost 50% compared to the wild-type enzyme
Q209G
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
S197Q
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
V189L/Q190A
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
V399I/I400E
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is reduced by almost 50% compared to the wild-type enzyme
G194L
-
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is significantly reduced to 6.50% compared to the wild-type enzyme
-
M227K
-
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is reduced by almost 50% compared to the wild-type enzyme
-
S197Q
-
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
-
V189L/Q190A
-
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
-
G390D
-
amino acid replacement in isoenzyme DELTA6I of DELTA6 desaturase-defective mutant strain YB214
T375K
-
amino acid replacement in isoenzyme DELTA6I of DELTA6 desaturase-defective mutant strain HR95
W314Stop
-
amino acid replacement in isoenzyme DELTA6I of DELTA6 desaturase-defective mutant strain ST66
DELTA238P/DELTA239L
F166V/V167L
activity is significantly lower than that of wild-type enzyme
F356V/S358T
activity is significantly lower than that of wild-type enzyme
H410Y/E413K
activity is significantly lower than that of wild-type enzyme
K234N/S235M/L236DELTA/K444Q
activity is significantly lower than that of wild-type enzyme
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/I195L/W245V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/V344P
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/I326V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N/I326V/Y188F/K190T
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N/I326V/Y188F/K190T/H410Y
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N/I326V/Y188F/K190T/H410Y/E413K
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/Y352N/I326V/H410Y
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/W245V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
P246S/L247V/Y249L
activity is significantly lower than that of wild-type enzyme
Q415E/E416S
R216M
S209P/N211S
Y352N/R353V
activity is significantly lower than that of wild-type enzyme
H360D
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
H381N
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
I306L
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
L303F
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
L383I
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
M384S/M385
site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme
S322A
site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme
T299S
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
T302V
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y375F
site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme
A181T/A188G/Y189F/S205N/L206T/G207A
-
compared to wild-type: reduced DELTA6 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate, strong DELTA9 desaturase activity with stearoyl-[acyl-carrier protein] as substrate, exhibits DELTA9 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate
A181T/A200F
-
increase in DELTA6 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate, strong DELTA9 desaturase activity with stearoyl-[acyl-carrier protein] as substrate
A181T/A200F/S205N/L206T/G207A
-
reduced DELTA6 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate, very low DELTA9 desaturase activity, no DELTA6 desaturase activity with stearoyl-[acyl-carrier protein] as substrate
A188G/Y189F
-
reduced DELTA6 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate
additional information
T302V
site-directed mutagenesis, mutant shows highly increased activity compared to the wild-type enzyme
T302V
site-directed mutagenesis, mutant shows potently increased activity compared to the wild-type enzyme
DELTA238P/DELTA239L
activity is significantly lower than that of wild-type enzyme
Q415E/E416S
activity is significantly lower than that of wild-type enzyme
S209P/N211S
activity is significantly lower than that of wild-type enzyme
additional information
construction of chimeric enzymes of delta6 desaturases from Glossomastix chrysoplasta and Thalassiosira pseudonana, chimera 7 with GcFADS2 residues 285-315 replaced by TpFADS2 residues 291-324 shows about 5fold increased activity with both substrates compared to the wild-type enzyme, the catalytic efficiency of chimera 9 with GcFADS2 residues 359-458 replaced by TpFADS2 residues 370-484 is also increased. The other chimeras exhibit a catalytic efficiency not significantly different both substrates compared with that exhibited by wild-type GcFADS2/TpFADS2. Fatty acid contents of wild-type and mutant strains, overview
additional information
-
genetic polymorphism of DELTA6 desaturase are naturally occuring in humans, a delivery of the gene for D6 desaturase to endothelial cells at atherosclerosis prone areas is expected to prevent/arrest the development of atherosclerosis despite the presence of hyperlipidemia, hypertension, diabetes mellitus, and at sites of shear stress of blood flow
additional information
construction of chimeric mutant genes from MaFADS6 and MpFADS6 genes, the former from Mortierella alpina strain ATCC 32222, overview. The relative conversion rate for linoleoyl-CoA remains low in all mutants compared to the wild-type enzyme
additional information
-
construction of chimeric mutant genes from MaFADS6 and MpFADS6 genes, the former from Mortierella alpina strain ATCC 32222, overview. The relative conversion rate for linoleoyl-CoA remains low in all mutants compared to the wild-type enzyme
additional information
-
construction of chimeric mutant genes from MaFADS6 and MpFADS6 genes, the former from Mortierella alpina strain ATCC 32222, overview. The relative conversion rate for linoleoyl-CoA remains low in all mutants compared to the wild-type enzyme
-
additional information
construction of chimeric mutant genes from MaFADS6 and MpFADS6 genes, the latter from Micromonas pusilla strain CCMP1545, overview. The relative conversion rate for linoleoyl-CoA remains low in all mutants compared to the wild-type enzyme
additional information
-
construction of chimeric mutant genes from MaFADS6 and MpFADS6 genes, the latter from Micromonas pusilla strain CCMP1545, overview. The relative conversion rate for linoleoyl-CoA remains low in all mutants compared to the wild-type enzyme
additional information
recombinant overexpression of Micromonas pusilla strain CCMP 1545 enzyme MpFADS6 in a uracil-auxotrophic Mortierella alpina strain to enhance eicosapentaenoic acid production in Mortierella alpina by favoring the omega3 pathway, using the Agrobacterium tumefaciens-mediated transformation method. The expression of MpFADS6 results in a 26.2fold increase in EPA production compared to wild-type Mortierella alpina, fatty acid profile with addition of exogenous alpha-linolenoic acid. Further enhancement of EPA production with peony seed meal, overview
additional information
-
recombinant overexpression of Micromonas pusilla strain CCMP 1545 enzyme MpFADS6 in a uracil-auxotrophic Mortierella alpina strain to enhance eicosapentaenoic acid production in Mortierella alpina by favoring the omega3 pathway, using the Agrobacterium tumefaciens-mediated transformation method. The expression of MpFADS6 results in a 26.2fold increase in EPA production compared to wild-type Mortierella alpina, fatty acid profile with addition of exogenous alpha-linolenoic acid. Further enhancement of EPA production with peony seed meal, overview
additional information
-
construction of chimeric mutant genes from MaFADS6 and MpFADS6 genes, the latter from Micromonas pusilla strain CCMP1545, overview. The relative conversion rate for linoleoyl-CoA remains low in all mutants compared to the wild-type enzyme
-
additional information
-
recombinant overexpression of Micromonas pusilla strain CCMP 1545 enzyme MpFADS6 in a uracil-auxotrophic Mortierella alpina strain to enhance eicosapentaenoic acid production in Mortierella alpina by favoring the omega3 pathway, using the Agrobacterium tumefaciens-mediated transformation method. The expression of MpFADS6 results in a 26.2fold increase in EPA production compared to wild-type Mortierella alpina, fatty acid profile with addition of exogenous alpha-linolenoic acid. Further enhancement of EPA production with peony seed meal, overview
-
additional information
generation of a series deletion analysis of the promoter suggesting that the sequence between -919 to -784 bp (relative to start site), termed eMd6, is the key factor for high activity of DELTA6-desaturase. Deletion of sequence between -919 and -784 bp (pYD6784-Md6), that contains three TATA boxes, a CREB1 site, and a potential promoter region, significantly reduces DELTA6-desaturase activity to 77% that of pYD6919-Md6. Further deletion of sequence from -644 to -434 bp (pYD6434-Md6), -434 to -121 (pYD6121-Md6) significantly reduces Md6 promoter activity to less than 40 and 13% that of the predecessor
additional information
-
generation of a series deletion analysis of the promoter suggesting that the sequence between -919 to -784 bp (relative to start site), termed eMd6, is the key factor for high activity of DELTA6-desaturase. Deletion of sequence between -919 and -784 bp (pYD6784-Md6), that contains three TATA boxes, a CREB1 site, and a potential promoter region, significantly reduces DELTA6-desaturase activity to 77% that of pYD6919-Md6. Further deletion of sequence from -644 to -434 bp (pYD6434-Md6), -434 to -121 (pYD6121-Md6) significantly reduces Md6 promoter activity to less than 40 and 13% that of the predecessor
-
additional information
construction of chimeric enzymes of delta6 desaturases from Glossomastix chrysoplasta and Thalassiosira pseudonana, e.g. chimera 16 with TpFADS2 residues 291-324 replaced by GcFADS2 residues 285-315 shows decreased activity with both substrates compared to the wild-type enzyme. The replacement of the aa359-458 region of GcFADS2 results in a significant reduction in catalytic activity against both substrates, such that chimera 18 exhibits a decreased catalytic efficiency which represents the lowest rate observed among the TpFADS2 chimeras. The other chimeras exhibit a catalytic efficiency not significantly different both substrates compared with that exhibited by wild-type GcFADS2/TpFADS2. Fatty acid contents of wild-type an dmutant strains, overview
