Information on EC 1.14.19.46 - sn-1 linoleoyl-lipid 6-desaturase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.19.46
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RECOMMENDED NAME
GeneOntology No.
sn-1 linoleoyl-lipid 6-desaturase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 1-linoleoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a 1-gamma-linolenoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
gamma-linolenate biosynthesis I (plants)
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gamma-linolenate biosynthesis III (cyanobacteria)
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SYSTEMATIC NAME
IUBMB Comments
1-linoleoyl-2-acyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (6,7-cis-dehydrogenating)
The enzyme, characterized from cyanobacteria, introduces a cis double bond at carbon 6 of linoleoyl groups (18:2) attached to the sn-1 position of glycerolipids. The enzyme is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid. It is nonspecific with respect to the polar head group of the glycerolipid.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-linoleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-gamma-linolenoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
linoleic acid + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
gamma-linolenic acid + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
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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
1-linoleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-gamma-linolenoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
linoleic acid + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
gamma-linolenic acid + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FADH2
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about 50% increase of activity in the presence of FADH2
NADPH
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about 50% increase of activity in the presence of NADPH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
linoleic acid
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mutant enzyme R123N, at pH 7.5 and 25°C; wild type enzyme, at pH 7.5 and 25°C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47000
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x * 47000, SDS-PAGE
50000
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x * 50000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as N-terminally fused and co-expressed protein with the cytochrome b5 domain from Mucor rouxii, in Escherichia coli DH5alpha cells and Saccharomyces cerevisiae strain DBY746
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expressed in Escherichia coli DH5alpha cells
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expressed in Saccharomyces cerevisiae strain DBY746
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D138N
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inactive
E140Q
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inactive
G136H
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inactive
H124R
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inactive
H128R
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inactive
H129R
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inactive
H305R
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the mutant shows 17% of wild type activity
H306R
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inactive
H313R
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inactive
H315N
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inactive
H89R
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inactive
H93R
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the mutant shows 11% of wild type activity
R123N
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the mutant shows 91% of wild type activity
W294G
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inactive