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Information on EC 1.3.1.38 - trans-2-enoyl-CoA reductase (NADPH) and Organism(s) Homo sapiens and UniProt Accession Q9BY49

for references in articles please use BRENDA:EC1.3.1.38
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EC Tree
IUBMB Comments
Not identical with EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) [cf. EC 1.3.1.8 acyl-CoA dehydrogenase (NADP+)].
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This record set is specific for:
Homo sapiens
UNIPROT: Q9BY49
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
trans-2-enoyl-coa reductase, mecr-1, nadph-dependent trans-2-enoyl-coa reductase, mitochondrial 2-trans-enoyl-thioester reductase, egter1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NADPH-dependent trans-2-enoyl-CoA reductase
reductase, trans-enoyl coenzyme A
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
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-
-
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reduction
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-
-
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dehydrogenation
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:NADP+ trans-2-oxidoreductase
Not identical with EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) [cf. EC 1.3.1.8 acyl-CoA dehydrogenase (NADP+)].
CAS REGISTRY NUMBER
COMMENTARY hide
77649-64-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nervonyl-CoA + NADPH
tetracosanoyl-CoA + NADP+
show the reaction diagram
-
-
1% of the activity with trans-phytenoyl-CoA
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ir
octa-2-enoyl-CoA + NADPH
octanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
ir
trans-2,3-dehydrostearoyl-CoA + NADPH
stearoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-enoyl-CoA + NADPH + H+
acyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-hexadecenoyl-CoA + NADPH + H+
palmitoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-phytenoyl-CoA + NADPH + H+
phytanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
ir
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
trans-2-enoyl-CoA + NADPH + H+
acyl-CoA + NADP+
show the reaction diagram
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.106
NADPH
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37°C, pH 7.2
0.018
trans-phytenoyl-CoA
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37°C, pH 7.2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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TER mRNA
Manually annotated by BRENDA team
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TER mRNA
Manually annotated by BRENDA team
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TER mRNA
Manually annotated by BRENDA team
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TER mRNA
Manually annotated by BRENDA team
-
TER mRNA
Manually annotated by BRENDA team
-
TER mRNA
Manually annotated by BRENDA team
-
TER mRNA
Manually annotated by BRENDA team
-
TER mRNA
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PECR_HUMAN
303
0
32544
Swiss-Prot
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32300
? * 32300, sequence determination
75000
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x * 75000, calculated and SDs-PAGE of enzyme fused to maltose-binding protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
? * 32300, sequence determination
?
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x * 75000, calculated and SDs-PAGE of enzyme fused to maltose-binding protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P182L
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the mutant exhibits lower trans-2-enoyl-CoA reductase activity as compared with the wild type enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable for at least a month, when stored at -20°C in PBS containing 50% (v/v) glycerol
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of cDNA, expression of TER in HEK-293 cells
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expressed in Saccharomyces cerevisiae
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Das, A.K.; Uhler, M.D.; Hajra, A.K.
Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs
J. Biol. Chem.
275
24333-24340
2000
Cavia porcellus (Q9JIF5), Cavia porcellus, Homo sapiens (Q9BY49), Homo sapiens, Mus musculus (Q99MZ7), Mus musculus
Manually annotated by BRENDA team
Moon, Y.A.; Horton, J.D.
Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade
J. Biol. Chem.
278
7335-7343
2003
Homo sapiens, Mus musculus (Q9CY27)
Manually annotated by BRENDA team
Gloerich, J.; Ruiter, J.P.; van den Brink, D.M.; Ofman, R.; Ferdinandusse, S.; Wanders, R.J.
Peroxisomal trans-2-enoyl-CoA reductase is involved in phytol degradation
FEBS Lett.
580
2092-2096
2006
Homo sapiens
Manually annotated by BRENDA team
Abe, K.; Ohno, Y.; Sassa, T.; Taguchi, R.; Caliskan, M.; Ober, C.; Kihara, A.
Mutation for nonsyndromic mental retardation in the trans-2-enoyl-CoA reductase TER gene involved in fatty acid elongation impairs the enzyme activity and stability, leading to change in sphingolipid profile
J. Biol. Chem.
288
36741-36749
2013
Homo sapiens
Manually annotated by BRENDA team
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
Homo sapiens
Manually annotated by BRENDA team