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Enzyme Nomenclature
Information on EC 1.3.1.93 - very-long-chain enoyl-CoA reductase
for references in articles please use BRENDA:EC1.3.1.93
Word Map on EC 1.3.1.93
- 1.3.1.93
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vlcfas
- cuticular
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sphingolipids
- acyl-coas
- sumatrana
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piecemeal
- taxus
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invaginations
- elongase
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microautophagy
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endophytic
- colletotrichum
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oleic
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antidiabetic
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linoleic
- triacylglycerols
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aerial
- palmitate
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.3.1.93
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RECOMMENDED NAME
GeneOntology No.
very-long-chain enoyl-CoA reductase
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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-[acyl-carrier protein] dehydratase.
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CAS REGISTRY NUMBER
COMMENTARY
69403-06-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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
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
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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
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
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
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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
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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
heterologous expression functionally complements the temperature-sensitive phenotype of a yeast tsc13 mutant that is dfficient in enoyl reductase activity; 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
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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
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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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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
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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
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
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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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+
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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?
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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-
-
?
trans-2-hexadecenoyl-CoA + NADPH + H
palmitoyl-CoA + NADP+
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-
?
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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
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+
Q9NZ01
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?
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H
a very-long-chain acyl-CoA + NADP+
Q64232
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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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-
-
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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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?
trans-2-hexadecenoyl-CoA + NADPH + H
palmitoyl-CoA + NADP+
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
enzyme harbours a non-classical NADPH binding site; enzyme harbours a non-classical NADPH binding site
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
predominantly expressed in the fibres and young leaves
low expression in root, stem, mature leaves, and flowers
predominantly expressed in the fibres and young leaves, low expression in root, stem, mature leaves, and flowers
low expression in root, stem, mature leaves, and flowers
low expression in root, stem, mature leaves, and flowers
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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protein accumulates at nucleus-vacuole junctions
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highly enriched in a structure marking nuclear-vacuolar junctions
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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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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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heterologously expressed protein interacts physically with the Elo2p and Elo3p components of the yeast elongase 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
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the native glycosylation sites at residues N76 and N244 of the enzyme are not modified
no glycoprotein
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the native glycosylation sites at residues 38 and 255 of the enzyme are not modified
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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; expression is upregulated during cotton fibre elongation
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ENGINEERING
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
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
E144A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
E259A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
E91A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
H137A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
H149A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
K140A
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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
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
R141A
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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
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
Y138A
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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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