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Information on EC 1.3.1.93 - very-long-chain enoyl-CoA reductase
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EC Tree
1.3.1.93 very-long-chain enoyl-CoA reductaseIUBMB Comments
This is the fourth component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase.
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Word Map
- 1.3.1.93
- cuticular
-
vlcfas
- sphingolipids
- acyl-coas
- triacylglycerols
-
piecemeal
- taxus
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antidiabetic
-
eceriferum
- sumatrana
- alkane
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invaginations
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endophytic
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nucleus-vacuole
- cuticle
- colletotrichum
- elongase
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
tsc13, cer10, at3g55360, very-long-chain enoyl-coa reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CER10
-
-
-
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EC 2.3.1.119
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-
formerly, part transferred
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enoyl reductase
TER
trans-2-enoyl-CoA reductase
TSC13
TSC13
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a very-long-chain acyl-CoA + NADP+ = a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
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PATHWAY SOURCE
PATHWAYS
KEGG
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, , , arachidonate biosynthesis, arachidonate biosynthesis, arachidonate biosynthesis, arachidonate biosynthesis, Biosynthesis of unsaturated fatty acids, Biosynthesis of unsaturated fatty acids, Biosynthesis of unsaturated fatty acids, Fatty acid elongation, Fatty acid elongation, Fatty acid elongation, Fatty acid elongation, Fatty acid elongation, Fatty acid elongation, lipid metabolism, lipid metabolism, lipid metabolism, lipid metabolism
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SYSTEMATIC NAME
IUBMB Comments
very-long-chain acyl-CoA:NADP+ oxidoreductase
This is the fourth component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase.
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CAS REGISTRY NUMBER
COMMENTARY
69403-06-1
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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
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
additional information
?
-
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novel micro RNA R201 is involved in the catalysis of the enoyl-CoA reduction to an acyl-CoA by targeting the enzyme
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-
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a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
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-
-
-
?
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
-
-
-
?
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
-
-
-
?
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
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-
-
-
?
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
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-
-
-
?
trans-2-hexadecenoyl-CoA + NADPH + H+
palmitoyl-CoA + NADP+
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-
-
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?
trans-2-hexadecenoyl-CoA + NADPH + H+
palmitoyl-CoA + NADP+
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-
-
-
?
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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
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
-
-
-
-
?
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
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-
-
?
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
-
-
-
?
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
-
-
-
-
?
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
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-
-
-
?
trans-2-hexadecenoyl-CoA + NADPH + H+
palmitoyl-CoA + NADP+
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-
-
-
?
trans-2-hexadecenoyl-CoA + NADPH + H+
palmitoyl-CoA + NADP+
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-
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
predominantly expressed in the fibres and young leaves
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low expression in root, stem, mature leaves, and flowers
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predominantly expressed in the fibres and young leaves, low expression in root, stem, mature leaves, and flowers
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low expression in root, stem, mature leaves, and flowers
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low expression in root, stem, mature leaves, and flowers
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
highly enriched in a structure marking nuclear-vacuolar junctions
brenda
protein accumulates at nucleus-vacuole junctions
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presence of six putative membrane-spanning domains
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the N and C termini of the enzyme reside in the cytoplasm, and six putative membrane-spanning domains have been identified. The N-terminal domain including the first membrane-spanning segment contains sufficient information for targeting to the endoplasmic reticulum membrane
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
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homology modeling of Tsc13 based on the structure of a trans-2-enoyl reductase from Homo sapiens, PDB ID 1YXM
malfunction
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ectopic expression of human trans-2-enoyl-CoA reductase TER in Saccharomyces cerevisiae TER homologue Tsc13-lowered cells causes recovery in the deficient sphingosine 1-phosphate metabolic pathway, lethality of VLCFA-deficient mutations
malfunction
in membrane fractions prepared from TER siRNA-treated HeLa cells, the conversion of trans-2-hexadecenoyl-CoA to palmitoyl-CoA is largely impaired, and only a small amount of palmitoyl-CoA is produced. Instead, trans-2-hexadecenoyl-CoA is the main product, and C14:0-CoA is also detected
malfunction
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ectopic expression of human trans-2-enoyl-CoA reductase TER in Saccharomyces cerevisiae TER homologue Tsc13-lowered cells causes recovery in the deficient sphingosine 1-phosphate metabolic pathway, lethality of VLCFA-deficient mutations
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metabolism
enzyme Tsc13p is sequestered into nucleus-vacuole junctions from the peripheral endoplasmic reticulum through Vac8p-independent interactions with Nvj1p. During nutrient limitation, Tsc13p is incorporated into piecemeal microautophagy vesicles in an Nvj1p-dependent manner. The lumenal diameters of piecemeal microautophagy blebs and vesicles are significantly reduced in tsc13 and tsc13 elo3 mutant cells. Piecemeal microautophagy structures are also smaller in cells treated with cerulenin, an inhibitor of de novo fatty acid synthesis and elongation. The targeting of Tsc13p-green fluorescent protein into nucleus-vacuole junctions is perturbed by cerulenin
metabolism
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TER is involved sphingosine degradation within sphingolipids in the S1P metabolic pathway. trans-2-enoyl-CoA reductase TER catalyzes the saturation step of the sphingosine 1-phosphate (S1P) metabolic pathway. The pathways of sphingolipid degradation and synthesis, overview
metabolism
TER is involved sphingosine degradation within sphingolipids in the S1P metabolic pathway. trans-2-enoyl-CoA reductase TER catalyzes the saturation step of the sphingosine 1-phosphate (S1P) metabolic pathway. The pathways of sphingolipid degradation and synthesis, overview
metabolism
TER is involved sphingosine degradation within sphingolipids in the S1P metabolic pathway. trans-2-enoyl-CoA reductase TER catalyzes the saturation step of the sphingosine 1-phosphate (S1P) metabolic pathway. The pathways of sphingolipid degradation and synthesis, overview. Ectopic expression of human trans-2-enoyl-CoA reductase TER in Saccharomyces cerevisiae TER homologue Tsc13-lowered cells causes recovery in the deficient sphingosine 1-phosphate metabolic pathway
metabolism
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TER is involved sphingosine degradation within sphingolipids in the S1P metabolic pathway. trans-2-enoyl-CoA reductase TER catalyzes the saturation step of the sphingosine 1-phosphate (S1P) metabolic pathway. The pathways of sphingolipid degradation and synthesis, overview
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physiological function
gene disruption results in a reduction of cuticular wax load and affects very long chain fatty acid composition of seed triacylglycerols and sphingolipids. Epidermal and seed-specific silencing of enzyme activity results in a reduction of cuticular wax load and the very long chaind fatty acid content of seed triacylglycerols, respectively, with no effects on plant morphogenesis. Cellular analysis reveals aberrant endocytic membrane traffic and defective cell expansion underlying the morphological defects of the disruption mutants
physiological function
heterologous expression functionally complements the temperature-sensitive phenotype of a yeast tsc13 mutant that is dfficient in enoyl reductase activity
physiological function
heterologous expression functionally complements the temperature-sensitive phenotype of a yeast tsc13 mutant that is dfficient in enoyl reductase activity. The heterologous protein interacts physically with the Elo2p and Elo3p components of the yeast elongase complex. Gene apparently encodes the sole enoyl reductase activity associated with microsomal fatty acid elongation in Arabidopsis thaliana
physiological function
heterologous expression functionally complements the temperature-sensitive phenotype of a yeast tsc13 mutant that is dfficient in enoyl reductase activity. Tsc13 cells expressing the reductase produce very long chain fatty acids, espcially C26:0
physiological function
the tsc13 mutant accumulates high levels of long-chain bases as well as ceramides that harbor fatty acids with chain lengths shorter than 26 carbons. These phenotypes are exacerbated by the deletion of either the ELO2 or ELO3 gene, both of which are required for synthesis of very long chain fatty acids. Compromising the synthesis of malonyl coenzyme A by inactivating acetyl-CoA carboxylase in a tsc13 mutant is lethal
physiological function
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the enoyl reductase Tsc13 is responsible for the accumulation of phloretic acid via reduction of p-coumaroyl-CoA. Tsc13 is an essential enzyme involved in fatty acid synthesis and cannot be deleted
physiological function
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the trans-2-enoyl-CoA reductase, TER, functions in very long-chain fatty acid (VLCFA) synthesis and is involved in the fatty acid elongation cycle, where palmitic acid synthesized by fatty acid synthase or fatty acids taken from foods are elongated to very long-chain fatty acids (VLCFAs) with carbon chain lengths greater than 20
physiological function
the trans-2-enoyl-CoA reductase, TER, functions in very long-chain fatty acid (VLCFA) synthesis and is involved in the fatty acid elongation cycle, where palmitic acid synthesized by fatty acid synthase or fatty acids taken from foods are elongated to very long-chain fatty acids (VLCFAs) with carbon chain lengths greater than 20
physiological function
the trans-2-enoyl-CoA reductase, TER, functions in very long-chain fatty acid (VLCFA) synthesis and is involved in the fatty acid elongation cycle, where palmitic acid synthesized by fatty acid synthase or fatty acids taken from foods are elongated to very long-chain fatty acids (VLCFAs) with carbon chain lengths greater than 20
physiological function
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the trans-2-enoyl-CoA reductase, TER, functions in very long-chain fatty acid (VLCFA) synthesis and is involved in the fatty acid elongation cycle, where palmitic acid synthesized by fatty acid synthase or fatty acids taken from foods are elongated to very long-chain fatty acids (VLCFAs) with carbon chain lengths greater than 20
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Show AA Sequence and Transmembrane Helices (1177 entries)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
heterologously expressed protein interacts physically with the Elo2p and Elo3p components of the yeast elongase complex
additional information
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heterologously expressed protein interacts physically with the Elo2p and Elo3p components of the yeast elongase complex
additional information
Tsc13p coimmunoprecipitates with Elo2p and Elo3p, which are required for veryl long chain fatty acid synthesis, suggesting that the elongating proteins are organized in a complex
additional information
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Tsc13p coimmunoprecipitates with Elo2p and Elo3p, which are required for veryl long chain fatty acid synthesis, suggesting that the elongating proteins are organized in a complex
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
no glycoprotein
the native glycosylation sites at residues N76 and N244 of the enzyme are not modified
no glycoprotein
the native glycosylation sites at residues 38 and 255 of the enzyme are not modified
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G225A
mutant is not able to complement the growth defect of a yeast tsc13 mutant
G234A
mutant is not able to complement the growth defect of a yeast tsc13 mutant
I231A
mutant is not able to complement the growth defect of a yeast tsc13 mutant
P232A
mutant is not able to complement the growth defect of a yeast tsc13 mutant
D77A
mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
E144A
mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
E259A
mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
E91A
mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
H137A
mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
H149A
mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
K140A
mutant is not able to complement an enzyme deletion mutant. Mutant protein is present at wild-type levels and does not show altered membrane topology
K76A
mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
R141A
mutant is not able to complement an enzyme deletion mutant. Mutant protein is present at wild-type levels and does not show altered membrane topology
Y103A
mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
Y138A
mutant is not able to complement an enzyme deletion mutant, protein is unstable
additional information
additional information
HeLa cells are transfected with control siRNA or TER si RNA, siRNA-generated enzyme knockout mutant. Knockdown of TER in HeLa cells causes decreased sphingosine 1-phosphate metabolism in vitro and a reduction in the dihydrosphingosine metabolism
additional information
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with the aim of commercially interesting production of phenylpropanoids, such as flavonoids and stilbenoids, site saturation mutagenesis is used for modification of the enzyme to reduce the side activity without disrupting the natural function, identification of a number of amino acid changes which slightly increase flavonoid production but without reducing the formation of side product. The complementation of TSC13 by the gene homologue from plants essentially eliminates the unwanted side reaction, while retaining the productivity of phenylpropanoids in a simulated fed batch fermentation. The native open reading frame (ORF) of TSC13 is replaced by gene homologues from Arabidospis thaliana (AtECR), Gossypium hirsutum (GhECR2) and Malus domestica (MdECR), using a split URA3 cassette under the control of the native TSC13 promoter
additional information
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YRF50 cells (BY4741,pTSC13::KanMX4-tTA-ptetO7) are constructed by replacing the promoter of the TSC13 gene (pTSC13) with tetO7 promoter (ptetO7) using the KanMX4-tTA-ptetO7 cassette from the pCM225 plasmid. Strains ABY83 and ABY80 cells are constructed by deletion of the TSC13 gene in BY4741 cells bearing the pTW6 or pAB119 plasmid, respectively, using a tsc13DELTA::LEU2 fragment by homologous recombination. Generation of Saccharomyces cerevisiae Tsc13-lowered cells
additional information
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YRF50 cells (BY4741,pTSC13::KanMX4-tTA-ptetO7) are constructed by replacing the promoter of the TSC13 gene (pTSC13) with tetO7 promoter (ptetO7) using the KanMX4-tTA-ptetO7 cassette from the pCM225 plasmid. Strains ABY83 and ABY80 cells are constructed by deletion of the TSC13 gene in BY4741 cells bearing the pTW6 or pAB119 plasmid, respectively, using a tsc13DELTA::LEU2 fragment by homologous recombination. Generation of Saccharomyces cerevisiae Tsc13-lowered cells
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene TECR, cloning from liver cDNA, Ectopic expression of human trans-2-enoyl-CoA reductase TER in Saccharomyces cerevisiae TER homologue Tsc13-lowered cells
gene TSC13, recombinant expression as N-terminal FLAG3-tagged enzyme from pAKNF313 and pAKNF315, or as N-terminal HA2-tagged enzyme
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is about 9fold upregulated during cotton fibre elongation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Song, W.Q.; Qin, Y.M.; Saito, M.; Shirai, T.; Pujol, F.M.; Kastaniotis, A.J.; Hiltunen, J.K.; Zhu, Y.X.
Characterization of two cotton cDNAs encoding trans-2-enoyl-CoA reductase reveals a putative novel NADPH-binding motif
J. Exp. Bot.
60
1839-1848
2009
Gossypium hirsutum (A9XUG7), Gossypium hirsutum (A9XUG8)
brenda
Paul, S.; Gable, K.; Dunn, T.
A six-membrane-spanning topology for yeast and Arabidopsis Tsc13p, the enoyl reductases of the microsomal fatty acid elongating system
J. Biol. Chem.
282
19237-19246
2007
Saccharomyces cerevisiae (Q99190), Arabidopsis thaliana (Q9M2U2)
brenda
Gable, K.; Garton, S.; Napier, J.A.; Dunn, T.M.
Functional characterization of the Arabidopsis thaliana orthologue of Tsc13p, the enoyl reductase of the yeast microsomal fatty acid elongating system
J. Exp. Bot.
55
543-545
2004
Arabidopsis thaliana (Q9M2U2), Arabidopsis thaliana
brenda
Kvam, E.; Gable, K.; Dunn, T.M.; Goldfarb, D.S.
Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles
Mol. Biol. Cell
16
3987-3998
2005
Saccharomyces cerevisiae (Q99190), Saccharomyces cerevisiae
brenda
Kohlwein, S.D.; Eder, S.; Oh, C.S.; Martin, C.E.; Gable, K.; Bacikova, D.; Dunn, T.
Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae
Mol. Cell. Biol.
21
109-125
2001
Saccharomyces cerevisiae (Q99190), Saccharomyces cerevisiae
brenda
Zheng, H.; Rowland, O.; Kunst, L.
Disruptions of the Arabidopsis enoyl-CoA reductase gene reveal an essential role for very-long-chain fatty acid synthesis in cell expansion during plant morphogenesis
Plant Cell
17
1467-1481
2005
Arabidopsis thaliana (Q9M2U2), Arabidopsis thaliana
brenda
Lehka, B.J.; Eichenberger, M.; Bjoern-Yoshimoto, W.E.; Vanegas, K.G.; Buijs, N.; Jensen, N.B.; Dyekjaer, J.D.; Jenssen, H.; Simon, E.; Naesby, M.
Improving heterologous production of phenylpropanoids in Saccharomyces cerevisiae by tackling an unwanted side reaction of Tsc13, an endogenous double-bond reductase
FEMS Yeast Res.
17
fox004
2017
Saccharomyces cerevisiae
brenda
Wakashima, T.; Abe, K.; Kihara, A.
Dual functions of the trans-2-enoyl-CoA reductase TER in the sphingosine 1-phosphate metabolic pathway and in fatty acid elongation
J. Biol. Chem.
289
24736-24748
2014
Saccharomyces cerevisiae, Rattus norvegicus (Q64232), Homo sapiens (Q9NZ01), Saccharomyces cerevisiae BY4741
brenda
Zheng, Y.; Chen, C.; Liang, Y.; Sun, R.; Gao, L.; Liu, T.; Li, D.
Genome-wide association analysis of the lipid and fatty acid metabolism regulatory network in the mesocarp of oil palm (Elaeis guineensis Jacq.) based on small noncoding RNA sequencing
Tree Physiol.
39
356-371
2019
Elaeis guineensis
brenda
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EXTERNAL LINKS (specific for EC-Number 1.3.1.93)
Transporter Classification Database (TCDB): 2.A.90.3.2, 2.A.90.3.3
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