Any feedback?
Information on EC 1.14.19.39 - acyl-lipid DELTA12-acetylenase
for references in articles please use BRENDA:EC1.14.19.39Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.19.39 acyl-lipid DELTA12-acetylenaseIUBMB Comments
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.
Specify your search results
Word Map
- 1.14.19.39
-
linoleic
-
oleic
-
desaturation
-
polyunsaturated
-
high-oleic
- alpina
- mortierella
- crepis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
fad2-1, oleate desaturase, fad2-2, acetylenase, delta12-desaturase, delta12-fatty acid desaturase, delta12 fatty acid desaturase, crep1, delta12 acetylenase, delta12-fatty acid desaturases, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylenase
bifunctional D12/D15 fatty acid desaturase
crepenylate synthase linoleate DELTA12-fatty acid acetylenase (desaturase)
-
-
-
-
Crepenynate synthase
-
-
-
-
Delta-12 fatty acid acetylenase
-
-
-
-
DELTA12 fatty acid desaturase
DELTA12 linoleate acetylenase
-
-
-
-
DELTA12-desaturase
DELTA12-fatty acid dehydrogenase
-
-
-
-
DELTA12DS
EC 1.14.99.33
-
-
formerly
-
FAD2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
-
linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = crepenynyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
stereochemical mechanism in reaction with oleate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
197025-40-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
enzyme is involved in biosynthesis of crepenynic acid
-
?
oleate + AH2 + O2
linoleate + A + 2 H2O
-
oxygenation at the sn-2 position
-
-
?
oleate + AH2 + O2
linoleic acid + linolenic acid + A + 2 H2O
recombinant enzyme
-
-
?
oleate + reduced acceptor + O2
crepenynate + acceptor + H2O
-
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
-
?
palmitoleic acid + O2
hexadecadienoic acid + hexadecatrienoic acid + A + 2 H2O
recombinant enzyme
-
-
?
palmitoleoate + AH2 + O2
9,12,15-hexadecatrienoate + A + H2O
-
via intermediate DELTA9,12 hexadecadienoate
the product is n-1 polyunsaturated
-
?
phosphatidylcholine + reduced cytochrome b5 + O2
? + cytochrome b5 + 2 H2O
with NADH
-
-
?
linoleate + reduced acceptor + O2
crepenynate + acceptor + H2O
-
first committed step in the biosynthesis of fatty acid-derived acetylenic secondary natural products, e.g. matricaria esters
-
-
?
linoleate + reduced acceptor + O2
crepenynate + acceptor + H2O
-
enzyme is equally efficient with linoleate and oleate
-
-
?
additional information
?
-
-
key enzyme in adaptation to low temperature, sequential changes in fatty acid composition on lowering environmental temperature, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
-
enzyme is involved in biosynthesis of crepenynic acid
-
?
linoleate + reduced acceptor + O2
crepenynate + acceptor + H2O
-
first committed step in the biosynthesis of fatty acid-derived acetylenic secondary natural products, e.g. matricaria esters
-
-
?
phosphatidylcholine + reduced cytochrome b5 + O2
? + cytochrome b5 + 2 H2O
with NADH
-
-
?
additional information
?
-
-
key enzyme in adaptation to low temperature, sequential changes in fatty acid composition on lowering environmental temperature, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Chagas Disease
Trypanosoma cruzi oleate desaturase: molecular characterization and comparative analysis in other trypanosomatids.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
additional information
additional information
both the acetylenase expression level and the co-expression of other desaturases may contribute to the tissue specificity of crepynate production
brenda
additional information
-
both the acetylenase expression level and the co-expression of other desaturases may contribute to the tissue specificity of crepynate production
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
strong expression of isoform acetylenase in young sunflowers. Functional expression of isoform appears to be affected by competition and collaboration with other enzymes
-
brenda
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
brenda
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
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
additional information
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
evolution
-
in plants, membrane-bound fatty acid desaturases are present in the plastid and the endoplasmic reticulum. The electron donors for plastid desaturases are typically ferredoxins, while endoplasmic reticulum enzymes use cytochrome b5 (Cytb5)
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
physiological function
-
in plants, seed-specific delta-12 fatty acid desaturase 2 (FAD2) is responsible for the high content of linoleic acid by inserting a double bond at the delta-12 (omega-6) position of oleic acid. FAD2-2 genes encoding isoforms of the large and functionally diverse FAD2 gene family are detected in developing seeds suggesting their major roles in storage oil desaturation in seed
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 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
additional information
the isozyme contains the three histidine clusters typical of the catalytic domains of DELTA12-desaturase enzymes
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FAD12_CREAL
375
4
43382
Swiss-Prot
other Location (Reliability: 5)
B9SI38_RICCO
506
3
57344
TrEMBL
Chloroplast (Reliability: 3)
G9I194_JATCU
387
5
44389
TrEMBL
other Location (Reliability: 3)
A2BSW4_PROMS
Prochlorococcus marinus (strain AS9601)
344
5
38854
TrEMBL
-
A0A0B2RTJ8_GLYSO
361
4
41459
TrEMBL
other Location (Reliability: 2)
Q10W96_TRIEI
Trichodesmium erythraeum (strain IMS101)
357
5
41991
TrEMBL
-
A0A2G9I586_9LAMI
426
3
49046
TrEMBL
Chloroplast (Reliability: 1)
B8HN41_CYAP4
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
360
5
42126
TrEMBL
-
A0A072UBF9_MEDTR
446
3
50909
TrEMBL
Chloroplast (Reliability: 4)
A2C9J9_PROM3
Prochlorococcus marinus (strain MIT 9303)
361
4
41211
TrEMBL
-
B9T1J7_RICCO
452
2
51688
TrEMBL
Chloroplast (Reliability: 1)
Q078Z1_NICLS
192
0
21095
TrEMBL
other Location (Reliability: 5)
A2BSV9_PROMS
Prochlorococcus marinus (strain AS9601)
368
5
43089
TrEMBL
-
A0A2P6R904_ROSCH
445
5
50773
TrEMBL
Chloroplast (Reliability: 3)
D3HSA2_LEGLN
Legionella longbeachae serogroup 1 (strain NSW150)
349
4
41217
TrEMBL
-
B9T3Z1_RICCO
440
4
51026
TrEMBL
other Location (Reliability: 5)
A3PEM4_PROM0
Prochlorococcus marinus (strain MIT 9301)
388
5
43944
TrEMBL
-
A2C2D0_PROM1
Prochlorococcus marinus (strain NATL1A)
405
6
46434
TrEMBL
-
A0A2G9GLE2_9LAMI
449
2
51435
TrEMBL
Chloroplast (Reliability: 4)
A0A0B2PT90_GLYSO
386
5
44192
TrEMBL
Chloroplast (Reliability: 4)
Q3M5C6_TRIV2
Trichormus variabilis (strain ATCC 29413 / PCC 7937)
350
4
41373
TrEMBL
-
W0SAL2_FISSO
461
5
50720
TrEMBL
Secretory Pathway (Reliability: 4)
B2IW53_NOSP7
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
359
5
41881
TrEMBL
-
B2IW54_NOSP7
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
353
4
41531
TrEMBL
-
Q3M5C7_TRIV2
Trichormus variabilis (strain ATCC 29413 / PCC 7937)
359
3
41997
TrEMBL
-
G9I193_JATCU
383
5
44446
TrEMBL
other Location (Reliability: 2)
A2BYA6_PROM5
Prochlorococcus marinus (strain MIT 9515)
375
5
42293
TrEMBL
-
K9ZLJ5_ANACC
Anabaena cylindrica (strain ATCC 27899 / PCC 7122)
358
4
42025
TrEMBL
-
W0S9B7_FISSO
462
5
50905
TrEMBL
Secretory Pathway (Reliability: 4)
G7JN29_MEDTR
440
3
50085
TrEMBL
Chloroplast (Reliability: 3)
K9U0S3_CHRTP
Chroococcidiopsis thermalis (strain PCC 7203)
359
5
42070
TrEMBL
-
A0T1K2_RICCO
383
5
43954
TrEMBL
other Location (Reliability: 3)
D9ZGG6_9AGAM
415
2
48248
TrEMBL
other Location (Reliability: 2)
Q46KU3_PROMT
Prochlorococcus marinus (strain NATL2A)
405
6
46370
TrEMBL
-
A2CBI3_PROM3
Prochlorococcus marinus (strain MIT 9303)
380
4
42580
TrEMBL
-
A0A0B2QXV9_GLYSO
383
6
43833
TrEMBL
other Location (Reliability: 4)
A0A0J0UW71_9ACTN
367
5
40920
TrEMBL
-
B9SQN0_RICCO
460
1
52561
TrEMBL
Chloroplast (Reliability: 3)
A3PEM0_PROM0
Prochlorococcus marinus (strain MIT 9301)
368
4
43018
TrEMBL
-
Q319A9_PROM9
Prochlorococcus marinus (strain MIT 9312)
391
5
44229
TrEMBL
-
A2BY98_PROM5
Prochlorococcus marinus (strain MIT 9515)
368
6
43051
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chemically constructed segment of the amino-proximate transmembrane domain TM-A by reversed phase chromatography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chemical in vitro synthesis of a segment of the amino-proximate transmembrane domain TM-A, overview
-
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
-
gene FAD2, DNA and amino acid sequence deterination and analysis, encoded motifs in comparison, sequence comparisons and phylogenetic analysis
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, M.; Lenman, M.; Banas, A.; Bafor, M.; Singh, S.; Schweizer, M.; Nilsson, R.; Liljenberg, C.; Dahlqvist, A.; Gummeson, P.O.; Sjoedahl, S.; Green, A.; Stymne, S.
Identification of non-heme diiron proteins that catalyze triple bond and epoxy group formation
Science
280
915-918
1998
Crepis alpina
brenda
Minto, R.E.; Gibbons, W.J., Jr.; Cardon, T.B.; Lorigan, G.A.
Synthesis and conformational studies of a transmembrane domain from a diverged microsomal DELTA12-desaturase
Anal. Biochem.
308
134-140
2002
Crepis alpina
brenda
Carlsson, A.S.; Thomaeus, S.; Hamberg, M.; Stymne, S.
Properties of two multifunctional plant fatty acid acetylenase/desaturase enzymes
Eur. J. Biochem.
271
2991-2997
2004
Crepis alpina
brenda
Nam, J.W.; Kappock, T.J.
Cloning and transcriptional analysis of Crepis alpina fatty acid desaturases affecting the biosynthesis of crepenynic acid
J. Exp. Bot.
58
1421-1432
2007
Crepis alpina (A9X2G9), Crepis alpina, Helianthus annuus
brenda
Zhang, S.; Sakuradani, E.; Ito, K.; Shimizu, S.
Identification of a novel bifunctional DELTA12/DELTA15 fatty acid desaturase from a basidiomycete, Coprinus cinereus TD#822-2
FEBS Lett.
581
315-319
2007
Coprinopsis cinerea (A2A1C4), Coprinopsis cinerea TD#822-2 (A2A1C4)
brenda
Harwood, J.L.
Temperature stress: reacting and adapting: lessons from poikilotherms
Ann. N. Y. Acad. Sci.
1113
52-57
2007
Acanthamoeba castellanii
brenda
Blacklock, B.J.; Scheffler, B.E.; Shepard, M.R.; Jayasuriya, N.; Minto, R.E.
Functional diversity in fungal fatty acid synthesis: the first acetylenase from the Pacific golden chanterelle, Cantharellus formosus
J. Biol. Chem.
285
28442-28449
2010
Cantharellus formosus (D9ZGG6), Cantharellus formosus
brenda
Zhou, X.; Green, A.; Singh, S.
Caenorhabditis elegans ?12-desaturase FAT-2 is a bifunctional desaturase able to desaturate a diverse range of fatty acid substrates at the DELTA12 and DELTA15 positions
J. Biol. Chem.
286
43644-43650
2011
Caenorhabditis elegans (G5EGA5), Caenorhabditis elegans
brenda
Chodok, P.; Eiamsa-ard, P.; Cove, D.J.; Quatrano, R.S.; Kaewsuwan, S.
Identification and functional characterization of two DELTA12-fatty acid desaturases associated with essential linoleic acid biosynthesis in Physcomitrella patens
J. Ind. Microbiol. Biotechnol.
40
901-913
2013
Physcomitrium patens (A9RQ27), Physcomitrium patens (A9RV06)
brenda
Dehghan Nayeri, F.; Yarizade, K.
Bioinformatics study of delta-12 fatty acid desaturase 2 (FAD2) gene in oilseeds
Mol. Biol. Rep.
41
5077-5087
2014
Ricinus communis
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.14.19.39)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
