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Information on EC 1.3.1.93 - very-long-chain enoyl-CoA reductase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q99190

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IUBMB 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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Saccharomyces cerevisiae
UNIPROT: Q99190
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
tsc13, cer10, at3g55360, very-long-chain enoyl-coa reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CER10
-
-
-
-
enoyl reductase
-
-
trans-2-enoyl-CoA reductase
-
-
TSC13
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY hide
69403-06-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-hexadecenoyl-CoA + NADPH + H+
palmitoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
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
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+
a very-long-chain acyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-hexadecenoyl-CoA + NADPH + H+
palmitoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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
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
physiological function
additional information
-
homology modeling of Tsc13 based on the structure of a trans-2-enoyl reductase from Homo sapiens, PDB ID 1YXM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
the native glycosylation sites at residues 38 and 255 of the enzyme are not modified
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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gene TSC13, TSC13 SSM library screening
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Arabidopsis thaliana (Q9M2U2), Saccharomyces cerevisiae (Q99190)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
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 (Q9NZ01), Rattus norvegicus (Q64232), Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Manually annotated by BRENDA team