Information on EC 1.14.19.39 - acyl-lipid DELTA12-acetylenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.19.39
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RECOMMENDED NAME
GeneOntology No.
acyl-lipid DELTA12-acetylenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = crepenynyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
crepenynate biosynthesis
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Linoleic acid metabolism
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SYSTEMATIC NAME
IUBMB Comments
DELTA12 acyl-lipid,ferrocytochrome-b5:oxygen oxidoreductase (12,13-dehydrogenating)
The enzyme, characterized from the plant Crepis alpina, converts the double bond at position 12 of linoleate into a triple bond. The product is the main fatty acid found in triacylglycerols in the seed oil of Crepis alpina.
CAS REGISTRY NUMBER
COMMENTARY hide
197025-40-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene fat-2
UniProt
Manually annotated by BRENDA team
gene Cf0807 or CfACET
UniProt
Manually annotated by BRENDA team
strain TD#822-2, isolated from soil, gene Cop-odeA
TrEMBL
Manually annotated by BRENDA team
strain TD#822-2, isolated from soil, gene Cop-odeA
TrEMBL
Manually annotated by BRENDA team
isoforms FAD2-2 and acetylenase
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the microsomal DELTA12-fatty acid desaturase (FAD2) is located in the endoplasmic reticulum and uses phosphatidylcholine as acyl substrate and NADH, NADH-cytochrome b5 reductase, and cytochrome b5 as electron donors. This reaction involves concomitant reduction of molecular oxygen to water. In contrast, the plastidial DELTA12-fatty acid desaturase (FAD6) is located in the chloroplast and uses primarily glycolipids as acyl carriers and NAD(P)H, ferredoxin-NAD(P) reductase, and ferredoxin as electron donors; the microsomal DELTA12-fatty acid desaturase (FAD2) is located in the endoplasmic reticulum and uses phosphatidylcholine as acyl substrate and NADH, NADH-cytochrome b5 reductase, and cytochrome b5 as electron donors. This reaction involves concomitant reduction of molecular oxygen to water. In contrast, the plastidial DELTA12-fatty acid desaturase (FAD6) is located in the chloroplast and uses primarily glycolipids as acyl carriers and NAD(P)H, ferredoxin-NAD(P) reductase, and ferredoxin as electron donors
metabolism
the bifunctional desaturase and the acetylenase provide the enzymatic activities required to drive oleate through linoleate to crepenynate and the conjugated enyne (14Z)-dehydrocrepenynate, the branchpoint precursors to a major class of acetylenic natural products, biosynthesis of polyacetylenic metabolites in Basidiomycetes, overview
physiological function
to produce the accumulated natural product dehydrocrepenynic acid, chanterelle must have both FAD2/3 desaturase, EC 1.14.19.6. and acetylenase activities, production of the trans DELTA12 double bond by H6Cf0807
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
linoleate + AH2 + O2
crepenynate + A + 2 H2O
show the reaction diagram
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?
linoleate + NAD(P)H + O2
crepenynate + NAD(P)+ + H2O
show the reaction diagram
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enzyme is involved in biosynthesis of crepenynic acid
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?
linoleate + NADH + O2
crepenynate + NAD+ + H2O
show the reaction diagram
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?
linoleate + NADPH + O2
crepenynate + NADP+ + H2O
show the reaction diagram
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?
linoleate + reduced acceptor + O2
crepenynate + acceptor + H2O
show the reaction diagram
oleate + AH2 + O2
linoleate + A + H2O
show the reaction diagram
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oxygenation at the sn-2 position
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?
oleate + AH2 + O2
linoleic acid + linolenic acid + A + 2 H2O
show the reaction diagram
recombinant enzyme
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?
oleate + reduced acceptor + O2
crepenynate + acceptor + H2O
show the reaction diagram
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enzyme is equally efficient with linoleate and oleate, via intermediates 9(Z),12(E)-octadecadienoate and 9,12(Z)-octadecadienoate, only the latter of which is further catalysed to give crepenynate, i.e. 9(Z)-octadecen-12-ynoate
product enantiomers in a ration of 3:1
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?
palmitoleic acid + O2
hexadecadienoic acid + hexadecatrienoic acid + A + 2 H2O
show the reaction diagram
recombinant enzyme
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?
palmitoleoate + AH2 + O2
9,12,15-hexadecatrienoate + A + H2O
show the reaction diagram
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via intermediate DELTA9,12 hexadecadienoate
the product is n-1 polyunsaturated
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?
phosphatidylcholine + AH2 + O2
?
show the reaction diagram
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?
phosphatidylcholine + reduced cytochrome b5 + O2
? + cytochrome b5 + 2 H2O
show the reaction diagram
with NADH
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?
additional information
?
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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
linoleate + NAD(P)H + O2
crepenynate + NAD(P)+ + H2O
show the reaction diagram
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enzyme is involved in biosynthesis of crepenynic acid
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?
linoleate + reduced acceptor + O2
crepenynate + acceptor + H2O
show the reaction diagram
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first committed step in the biosynthesis of fatty acid-derived acetylenic secondary natural products, e.g. matricaria esters
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?
phosphatidylcholine + reduced cytochrome b5 + O2
? + cytochrome b5 + 2 H2O
show the reaction diagram
A9RQ27, A9RV06
with NADH
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
the enzyme contains positionally conserved histidine box motifs that are believed to bind two active-site iron atoms and are critical to enzyme function
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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the enzyme is independently induced by oxygen, and temperature, while chilling alone is not sufficient to raise the enzyme activity. Chilling and lowered temperature cause an increase in desaturase activity, increased membrane unsaturation and subsequently fluidity, followed by phagocytosis, overview
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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cell growth between 4°C and 32°C
Manually annotated by BRENDA team
high expression of isoforms FAD2-3 and FAD3in flower heads, moderate expression of isoforms FAD2-2 and acetylenase
Manually annotated by BRENDA team
additional information
both the acetylenase expression level and the co-expression of other desaturases may contribute to the tissue specificity of crepynate production
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the transmembrane protein PpFAD2-1 contains three conserved histidine-rich motifs: the HXXXH motif from amino acid residue 99 to 103 (HECGH), the HXXHH motif from amino acid residue 135 to 139 (HRRHH), and the HXXHH motif from amino acid residue 309 to 313 (HVAHH) in the C-terminus; the transmembrane protein PpFAD2-2 contains three conserved histidine-rich motifs: the HXXXH motif from amino acid residue 99 to 103 (HECGH), the HXXHH motif from amino acid residue 135 to 139 (HRRHH), and the HXXHH motif from amino acid residue 309 to 313 (HVAHH) in the C-terminus
Manually annotated by BRENDA team
additional information
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strong expression of isoform acetylenase in young sunflowers. Functional expression of isoform appears to be affected by competition and collaboration with other enzymes
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Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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secondary structure of the enzyme in a membrane bilayer, modeling, conformational studies of the recombinant segment of transmembrane domain TM-A, a hydrophobic peptide, which mainly folds into an alpha-helical structure, the helical content of the structure is increased in 40-80% 2,2,2-trifluoroethanol, overview
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chemically constructed segment of the amino-proximate transmembrane domain TM-A by reversed phase chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chemical in vitro synthesis of a segment of the amino-proximate transmembrane domain TM-A, overview
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expression in Saccharomyces cerevisiae
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gene Cf0807 or CfACET, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged ACTE in Saccharomyces cerevisiae
gene Cop-odeA, DNA and amino acid sequence determination and analysis, expression in Saccharomyces cerevisiae EH1315, fatty acid compositions of the yeast transformants compared to the wild-type cells, overview
gene Crep1 expressed in Saccharomyces cerevisiae YN94-1 strain
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gene CREP1, expression in Arabidopsis thaliana and in Saccharomyces cerevisiae, determination and identification of fatty acid content of transgenic plant lines and yeast strains
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gene fat-2, sequence comparison and phylogenetic tree, expression in Saccharomyces cerevisiae strain S288C
gene PpFAD2-2, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, expression in Saccharomyces cerevisiae strain INVSc1; genes PpFAD2-1, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, expression in Saccharomyces cerevisiae strain INVSc1