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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
- cuticular
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vlcfas
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sphingolipids
- acyl-coas
- sumatrana
- colletotrichum
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linoleic
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piecemeal
- palmitate
- triacylglycerols
- taxus
- elongase
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invaginations
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endophytic
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antidiabetic
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oleic
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aerial
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microautophagy
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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
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
physiological function
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
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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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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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.93)
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