Information on EC 1.14.19.47 - acyl-lipid (9-3)-desaturase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.14.19.47
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RECOMMENDED NAME
GeneOntology No.
acyl-lipid (9-3)-desaturase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a gamma-linolenoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
show the reaction diagram
(2)
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an alpha-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a stearidonoyl-[glycerolipid] + ferricytochrome b5 + 2 H2O
show the reaction diagram
(1)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
arachidonate biosynthesis I (6-desaturase, lower eukaryotes)
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dicranin biosynthesis
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icosapentaenoate biosynthesis I (lower eukaryotes)
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SYSTEMATIC NAME
IUBMB Comments
DELTA9 acyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase (6,7-cis-dehydrogenating)
The enzyme, characterized from the moss Physcomitrella patens and the plant Borago officinalis (borage), introduces a cis double bond at carbon 6 of several acyl-lipids that contain an existing Delta9 cis double bond. The enzyme contains a cytochrome b5 domain that acts as the electron donor for the active site of the desaturase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-linolenoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
stearidonoyl-[glycerolipid] + ferricytochrome b5 + H2O
show the reaction diagram
linoleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-[glycerolipid] + ferricytochrome b5 + H2O
show the reaction diagram
additional information
?
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DELTA6-desaturation appears to occur both in glycerolipids and the acyl-CoA pool
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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
alpha-linolenoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
stearidonoyl-[glycerolipid] + ferricytochrome b5 + H2O
show the reaction diagram
linoleoyl-[glycerolipid] + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-[glycerolipid] + ferricytochrome b5 + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b5
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
trans-9,12-linoleic acid
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potent inhibitor
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Anabaena sp.
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expressed in Arabidopsis thaliana
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expressed in Aspergillus oryzae
expressed in HEK-293 cells
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expressed in Nicotiana tabacum leaf and Arabidopsis thaliana seed
expressed in Pichia pastoris
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expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae DBY746 cells
expressed in Saccharomyces cerevisiae strain W303-1A and Arabidopsis thaliana
expressed in Solanum lycopersicum
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after adriamycin treatment, enzyme activity increases in polyenylphosphatidylcholine-fed and trilinolein-fed rats
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neuronal differentiation of Y-79 cells causes a great increase in enzyme activity
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D169V/T275A
the mutant has little effect on the D6-desaturation activity of the enzyme
L14P
the mutant shows dramatically reduced activity compared to the wild type enzyme
L224S
the mutant shows dramatically reduced activity compared to the wild type enzyme
L371F
the mutant shows dramatically reduced activity compared to the wild type enzyme
S205N
the mutant has little effect on the D6-desaturation activity of the enzyme
S301P
the mutant shows dramatically reduced activity compared to the wild type enzyme
S391P
the mutant shows dramatically reduced activity compared to the wild type enzyme
V137A
the mutant shows dramatically reduced activity compared to the wild type enzyme