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Literature summary extracted from

  • 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 (2014), J. Biol. Chem., 289, 24736-24748.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.93 gene TECR Rattus norvegicus
1.3.1.93 gene TECR, cloning from liver cDNA, Ectopic expression of human trans-2-enoyl-CoA reductase TER in Saccharomyces cerevisiae TER homologue Tsc13-lowered cells Homo sapiens
1.3.1.93 gene TSC13, recombinant expression as N-terminal FLAG3-tagged enzyme from pAKNF313 and pAKNF315, or as N-terminal HA2-tagged enzyme Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.3.1.93 additional information 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 Saccharomyces cerevisiae
1.3.1.93 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 Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.1.38 membrane
-
Homo sapiens 16020
-
1.3.1.93 endoplasmic reticulum
-
Saccharomyces cerevisiae 5783
-
1.3.1.93 endoplasmic reticulum
-
Homo sapiens 5783
-
1.3.1.93 endoplasmic reticulum
-
Rattus norvegicus 5783
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.93 a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+ Saccharomyces cerevisiae
-
a very-long-chain acyl-CoA + NADP+
-
?
1.3.1.93 a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+ Homo sapiens
-
a very-long-chain acyl-CoA + NADP+
-
?
1.3.1.93 a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+ Rattus norvegicus
-
a very-long-chain acyl-CoA + NADP+
-
?
1.3.1.93 a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+ Saccharomyces cerevisiae BY4741
-
a very-long-chain acyl-CoA + NADP+
-
?
1.3.1.93 trans-2-hexadecenoyl-CoA + NADPH + H+ Saccharomyces cerevisiae
-
palmitoyl-CoA + NADP+
-
?
1.3.1.93 trans-2-hexadecenoyl-CoA + NADPH + H+ Homo sapiens
-
palmitoyl-CoA + NADP+
-
?
1.3.1.93 trans-2-hexadecenoyl-CoA + NADPH + H+ Rattus norvegicus
-
palmitoyl-CoA + NADP+
-
?
1.3.1.93 trans-2-hexadecenoyl-CoA + NADPH + H+ Saccharomyces cerevisiae BY4741
-
palmitoyl-CoA + NADP+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.38 Homo sapiens
-
-
-
1.3.1.93 Homo sapiens Q9NZ01
-
-
1.3.1.93 Rattus norvegicus Q64232
-
-
1.3.1.93 Saccharomyces cerevisiae
-
-
-
1.3.1.93 Saccharomyces cerevisiae BY4741
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.1.38 liver
-
Homo sapiens
-
1.3.1.93 HeLa cell
-
Homo sapiens
-
1.3.1.93 Hep-G2 cell
-
Homo sapiens
-
1.3.1.93 hepatocyte
-
Homo sapiens
-
1.3.1.93 IEC-6 cell
-
Rattus norvegicus
-
1.3.1.93 intestinal epithelial cell
-
Rattus norvegicus
-
1.3.1.93 neuronal cell
-
Rattus norvegicus
-
1.3.1.93 PC-12 cell
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.38 trans-2-hexadecenoyl-CoA + NADPH + H+
-
Homo sapiens palmitoyl-CoA + NADP+
-
?
1.3.1.93 a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
-
Saccharomyces cerevisiae a very-long-chain acyl-CoA + NADP+
-
?
1.3.1.93 a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
-
Homo sapiens a very-long-chain acyl-CoA + NADP+
-
?
1.3.1.93 a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
-
Rattus norvegicus a very-long-chain acyl-CoA + NADP+
-
?
1.3.1.93 a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
-
Saccharomyces cerevisiae BY4741 a very-long-chain acyl-CoA + NADP+
-
?
1.3.1.93 trans-2-hexadecenoyl-CoA + NADPH + H+
-
Saccharomyces cerevisiae palmitoyl-CoA + NADP+
-
?
1.3.1.93 trans-2-hexadecenoyl-CoA + NADPH + H+
-
Homo sapiens palmitoyl-CoA + NADP+
-
?
1.3.1.93 trans-2-hexadecenoyl-CoA + NADPH + H+
-
Rattus norvegicus palmitoyl-CoA + NADP+
-
?
1.3.1.93 trans-2-hexadecenoyl-CoA + NADPH + H+
-
Saccharomyces cerevisiae BY4741 palmitoyl-CoA + NADP+
-
?

Synonyms

EC Number Synonyms Comment Organism
1.3.1.38 TER
-
Homo sapiens
1.3.1.93 TER
-
Saccharomyces cerevisiae
1.3.1.93 TER
-
Homo sapiens
1.3.1.93 TER
-
Rattus norvegicus
1.3.1.93 trans-2-enoyl-CoA reductase
-
Saccharomyces cerevisiae
1.3.1.93 trans-2-enoyl-CoA reductase
-
Homo sapiens
1.3.1.93 trans-2-enoyl-CoA reductase
-
Rattus norvegicus
1.3.1.93 TSC13
-
Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.38 NADPH
-
Homo sapiens
1.3.1.93 NADPH
-
Saccharomyces cerevisiae
1.3.1.93 NADPH
-
Homo sapiens
1.3.1.93 NADPH
-
Rattus norvegicus

General Information

EC Number General Information Comment Organism
1.3.1.38 metabolism the enzyme is involved in both the production of very long-chain fatty acids for sphingolipid synthesis and the degradation of sphingosine in sphingolipids through the sphingosine 1-phosphate metabolic pathway Homo sapiens
1.3.1.93 malfunction 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 Saccharomyces cerevisiae
1.3.1.93 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 Homo sapiens
1.3.1.93 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 Saccharomyces cerevisiae
1.3.1.93 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 Homo sapiens
1.3.1.93 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 Rattus norvegicus
1.3.1.93 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 Saccharomyces cerevisiae
1.3.1.93 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 Homo sapiens
1.3.1.93 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 Rattus norvegicus