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

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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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-
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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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-
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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.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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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-
-
-
?
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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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-
-
-
?
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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
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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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.19.46)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)