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Enzyme Nomenclature
Information on EC 1.14.19.39 - acyl-lipid DELTA12-acetylenase
Word Map on EC 1.14.19.39
- 1.14.19.39
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linoleic
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oleic
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polyunsaturated
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desaturation
- alpina
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seed-specific
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monounsaturated
- mortierella
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alpha-linolenic
- crepis
- epoxygenase
- delta6-desaturase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.19.39
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RECOMMENDED NAME
GeneOntology No.
acyl-lipid DELTA12-acetylenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = crepenynyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = crepenynyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
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linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = crepenynyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
stereochemical mechanism in reaction with oleate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
197025-40-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain TD#822-2, isolated from soil, gene Cop-odeA
TrEMBL
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
additional information
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the acetylenase gene, identified from the fungus, is phylogenetically distinct from known plant and fungal desaturases. The enzyme contains positionally conserved histidine box motifs that are believed to bind two active-site iron atoms and are critical to enzyme function
additional information
the acetylenase gene, identified from the fungus, is phylogenetically distinct from known plant and fungal desaturases. The enzyme contains positionally conserved histidine box motifs that are believed to bind two active-site iron atoms and are critical to enzyme function
additional information
the isozyme contains the three histidine clusters typical of the catalytic domains of DELTA12-desaturase enzymes; the isozyme contains the three histidine clusters typical of the catalytic domains of DELTA12-desaturase enzymes
additional information
the isozyme contains the three histidine clusters typical of the catalytic domains of DELTA12-desaturase enzymes; the isozyme contains the three histidine clusters typical of the catalytic domains of DELTA12-desaturase enzymes
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
linoleate + NAD(P)H + O2
crepenynate + NAD(P)+ + H2O
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enzyme is involved in biosynthesis of crepenynic acid
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?
oleate + AH2 + O2
linoleate + A + H2O
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oxygenation at the sn-2 position
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?
oleate + AH2 + O2
linoleic acid + linolenic acid + A + 2 H2O
recombinant enzyme
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oleate + reduced acceptor + O2
crepenynate + acceptor + H2O
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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
recombinant enzyme
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palmitoleoate + AH2 + O2
9,12,15-hexadecatrienoate + A + H2O
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via intermediate DELTA9,12 hexadecadienoate
the product is n-1 polyunsaturated
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?
phosphatidylcholine + reduced cytochrome b5 + O2
? + cytochrome b5 + 2 H2O
with NADH
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linoleate + reduced acceptor + O2
crepenynate + acceptor + H2O
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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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linoleate + reduced acceptor + O2
crepenynate + acceptor + H2O
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enzyme is equally efficient with linoleate and oleate
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additional information
?
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key enzyme in adaptation to low temperature, sequential changes in fatty acid composition on lowering environmental temperature, overview
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additional information
?
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substrate specificity, the recombinant enzyme catalyzes also the DELTA15-desaturation of fatty acids, and is capable of producing very unusual n-1 polyunsaturated products, overview
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additional information
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the enzyme is able to desaturate C16 and C18 fatty acids. When recombinantly expressed in yeast cells, the enzyme can also catalyze DELTA15 desaturation. The recombinant enzyme can also produce C14:2DELTA9,12, C15:2DELTA9,12, C17:2DELTA9,12, and C18:4DELTA6,9,12,15 when C14:1DELTA9, C15:1DELTA9, C17:1DELTA9, and C18:3DELTA6,9,12 substrates are available in yeast cells, product mass spectrometry analysis
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additional information
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H6Cf0807 is an acetylenase, that produces a trans DELTA12 double bond, while H6Cf0745 is a classical FAD2 desaturase. The Cantharellus formosus FAD2 homologue H6Cf0745 expression results in the production of only 16:2 DELTA9,12 and 18:2 DELTA9,12 in recombinant yeast cells supplemented with 18:2 DELTA9c,12c. Expression ofH6Cf0807 results in the production of crepenynic acid, 18:1 DELTA9c,12a. No C16 acetylenic fatty acid is detected. Supplementation with 18:2 DELTA9c,12t, alpha-linolenic acid, 18:3 DELTA9,12,15, or gamma-linolenic acid, 18:3 DELTA6,9,12, does not result in the production of other fatty acids, overview
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additional information
?
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H6Cf0807 is an acetylenase, that produces a trans DELTA12 double bond, while H6Cf0745 is a classical FAD2 desaturase. The Cantharellus formosus FAD2 homologue H6Cf0745 expression results in the production of only 16:2 DELTA9,12 and 18:2 DELTA9,12 in recombinant yeast cells supplemented with 18:2 DELTA9c,12c. Expression ofH6Cf0807 results in the production of crepenynic acid, 18:1 DELTA9c,12a. No C16 acetylenic fatty acid is detected. Supplementation with 18:2 DELTA9c,12t, alpha-linolenic acid, 18:3 DELTA9,12,15, or gamma-linolenic acid, 18:3 DELTA6,9,12, does not result in the production of other fatty acids, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
linoleate + NAD(P)H + O2
crepenynate + NAD(P)+ + H2O
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enzyme is involved in biosynthesis of crepenynic acid
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?
linoleate + reduced acceptor + O2
crepenynate + acceptor + H2O
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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
A9RQ27, A9RV06
with NADH
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?
additional information
?
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key enzyme in adaptation to low temperature, sequential changes in fatty acid composition on lowering environmental temperature, overview
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additional information
?
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H6Cf0807 is an acetylenase, that produces a trans DELTA12 double bond, while H6Cf0745 is a classical FAD2 desaturase. The Cantharellus formosus FAD2 homologue H6Cf0745 expression results in the production of only 16:2 DELTA9,12 and 18:2 DELTA9,12 in recombinant yeast cells supplemented with 18:2 DELTA9c,12c. Expression ofH6Cf0807 results in the production of crepenynic acid, 18:1 DELTA9c,12a. No C16 acetylenic fatty acid is detected. Supplementation with 18:2 DELTA9c,12t, alpha-linolenic acid, 18:3 DELTA9,12,15, or gamma-linolenic acid, 18:3 DELTA6,9,12, does not result in the production of other fatty acids, overview
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additional information
?
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D9ZGG6
H6Cf0807 is an acetylenase, that produces a trans DELTA12 double bond, while H6Cf0745 is a classical FAD2 desaturase. The Cantharellus formosus FAD2 homologue H6Cf0745 expression results in the production of only 16:2 DELTA9,12 and 18:2 DELTA9,12 in recombinant yeast cells supplemented with 18:2 DELTA9c,12c. Expression ofH6Cf0807 results in the production of crepenynic acid, 18:1 DELTA9c,12a. No C16 acetylenic fatty acid is detected. Supplementation with 18:2 DELTA9c,12t, alpha-linolenic acid, 18:3 DELTA9,12,15, or gamma-linolenic acid, 18:3 DELTA6,9,12, does not result in the production of other fatty acids, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
SOURCE
high expression of isoforms FAD2-3 and FAD3in flower heads, moderate expression of isoforms FAD2-2 and acetylenase
additional information
both the acetylenase expression level and the co-expression of other desaturases may contribute to the tissue specificity of crepynate production
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
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
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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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
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
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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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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, 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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.19.39)
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