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Information on EC 1.1.1.102 - 3-dehydrosphinganine reductase
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EC Tree
1.1.1.102 3-dehydrosphinganine reductaseSpecify your search results
Word Map
- 1.1.1.102
- sphingolipids
- ceramide
-
nadph-dependent
- phytosphingosine
- sphingomyelin
-
inositolphosphorylceramide
- palmitoyl-coa
- food industry
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
tsc10, tsc10p, 3-ketosphinganine reductase, 3-ketodihydrosphingosine reductase, fvt-1, kds reductase, 3-kds reductase, tsc10a, 3-dehydrosphinganine reductase, ksr1p, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-ketodihydrosphingosine reductase
3-ketosphinganine reductase
3-oxosphinganine reductase
-
-
-
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3-oxosphinganine:NADPH oxidoreductase
-
-
-
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D-3-dehydrosphinganine reductase
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-
-
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D-3-oxosphinganine reductase
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-
-
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D-3-oxosphinganine:B-NADPH oxidoreductase
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-
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DSR
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-
-
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FVT-1
Fvt1
KDS reductase
additional information
additional information
-
the enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes
additional information
-
the enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes
additional information
-
the enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sphinganine + NADP+ = 3-dehydrosphinganine + NADPH + H+
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
D-erythro-dihydrosphingosine:NADP+ 3-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
37250-36-5
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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
(S)-2-amino-1-hydroxyeicosane-3-one + NADPH
(S)-2-amino-1-(R)-3-dihydroxyeicosane + NADP+
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slower reduced than (S)-2-amino-1-hydroxyoctadecane-3-one
-
?
(S)-2-amino-1-hydroxyoctadecan-3-one + NADPH
(S)-2-amino-1-(R)-3-dihydroxyoctadecane + NADP+
2-amino-1-hydroxyoctadecan-3-one + NADPH
2-amino-1,3-dihydroxyoctadecane + NADP+
-
-
-
?
3-oxosphinganine + NADPH + H+
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
(S)-2-amino-1-hydroxyoctadecan-3-one + NADPH
(S)-2-amino-1-(R)-3-dihydroxyoctadecane + NADP+
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-
-
?
(S)-2-amino-1-hydroxyoctadecan-3-one + NADPH
(S)-2-amino-1-(R)-3-dihydroxyoctadecane + NADP+
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-
-
?
(S)-2-amino-1-hydroxyoctadecan-3-one + NADPH
(S)-2-amino-1-(R)-3-dihydroxyoctadecane + NADP+
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enzyme acts at the cytoplasmic side of endoplasmic reticulum
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?
2-amino-1-hydroxyoctadecan-3-one + NADPH
(2S,3R)-2-aminooctadecane-1,3-diol + NADP+
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-
-
?
2-amino-1-hydroxyoctadecan-3-one + NADPH
(2S,3R)-2-aminooctadecane-1,3-diol + NADP+
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-
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?
3-dehydrosphinganine + NADPH
sphinganine + NADP+
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the enzyme is not essential for cell viability, but enzyme-deficient mutants produce lower levels of inositolphosphorylceramides
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-
?
3-dehydrosphinganine + NADPH
sphinganine + NADP+
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C18 substrate, molecular modeling of substrate binding, overview
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-
?
3-dehydrosphinganine + NADPH
sphinganine + NADP+
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the enzyme catalyzes an early step in the sphingolipid biosynthesis, overview
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-
?
3-oxosphinganine + NADPH + H+
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
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-
-
-
?
3-oxosphinganine + NADPH + H+
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
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-
-
-
?
3-oxosphinganine + NADPH + H+
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
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-
-
-
?
additional information
?
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-
FVT1 is able to support growth of tsc10DELTA mutant cells at 26°C, but not at 37°C
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-
?
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NATURAL SUBSTRATE
NATURAL 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
(S)-2-amino-1-hydroxyoctadecan-3-one + NADPH
(S)-2-amino-1-(R)-3-dihydroxyoctadecane + NADP+
-
enzyme acts at the cytoplasmic side of endoplasmic reticulum
-
?
2-amino-1-hydroxyoctadecan-3-one + NADPH
2-amino-1,3-dihydroxyoctadecane + NADP+
-
-
-
?
3-oxosphinganine + NADPH + H+
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
3-dehydrosphinganine + NADPH
sphinganine + NADP+
-
the enzyme is not essential for cell viability, but enzyme-deficient mutants produce lower levels of inositolphosphorylceramides
-
-
?
3-dehydrosphinganine + NADPH
sphinganine + NADP+
-
the enzyme catalyzes an early step in the sphingolipid biosynthesis, overview
-
-
?
3-oxosphinganine + NADPH + H+
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
-
-
-
-
?
3-oxosphinganine + NADPH + H+
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
-
-
-
-
?
3-oxosphinganine + NADPH + H+
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
siRNA
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reduces expression of transfected FVT1 mRNA and protein by at least 70%
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tergitol
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0.2%, 10fold activation of 2-amino-1-hydroxyoctadecane-3-one reduction
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinogenesis
Identification of target genes regulated by FOXC1 using nickel agarose-based chromatin enrichment.
Ichthyosis
Progressive symmetrical erythrokeratoderma manifesting as harlequin-like ichthyosis with severe thrombocytopenia secondary to a homozygous 3-ketodihydrosphingosine reductase mutation.
Leukemia
3-Ketodihydrosphingosine reductase maintains ER homeostasis and unfolded protein response in leukemia.
Lymphoma, Follicular
FVT-1, a novel human transcription unit affected by variant translocation t(2;18)(p11;q21) of follicular lymphoma.
Muscular Atrophy, Spinal
A missense mutation in the 3-ketodihydrosphingosine reductase FVT1 as candidate causal mutation for bovine spinal muscular atrophy.
Neoplasms
FVT-1, a novel human transcription unit affected by variant translocation t(2;18)(p11;q21) of follicular lymphoma.
Thrombocytopenia
Progressive symmetrical erythrokeratoderma manifesting as harlequin-like ichthyosis with severe thrombocytopenia secondary to a homozygous 3-ketodihydrosphingosine reductase mutation.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
binding kinetics of substrate analogues with shorter chain lengths
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genes At3g06060/TSC10A and At5g19200/TSC10B, i.e. tsc10A and tsc10B
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
the 3-KDS reductase genes are functionally redundant and ubiquitously expressed in Arabidopsis thaliana
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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the plant isozymes contain an N-terminal membrane-spanning domain, subcellular localization study, overview
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brenda
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N-terminal membrane-spanning domain in FVT1 orients to place it in the endoplasmic reticulum lumen
brenda
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Tsc10p localizes to the yeast endoplasmic reticulum membrane
brenda
of endoplasmic reticulum, the large hydrophilic domain, which contains putative active site residues, faces the cytosol
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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perturbation of sphingolipid biosynthesis in the Arabidopsis tsc10a mutant leads to an altered leaf ionome, including increases in Na, K, and Rb and decreases in Mg, Ca, Fe, and Mo, associated with increases in root suberin and alterations in Fe homeostasis. Loss of function of both TSC10A and TSC10B Is lethal in Arabidopsis thaliana
physiological function
physiological function
-
3-KDS reductase is essential for sphingolipid biosynthesis. Reduced 3-KDS reductase activity in Arabidopsis thaliana roots drives changes in the leaf Ionome
physiological function
S4SCP5
the enzyme is involved in de novo generation of ceramide and in invertebrate stress response
Show AA Sequence and Transmembrane Helices (243 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
-
molecular modeling of the enzyme with bound substrates, a significant portion of the aliphatic chain of 3-dehydrosphinganine protrudes from the enzyme, overview
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A175T
additional information
A175T
site-directed mutagenesis, naturally occuring missense mutation linked to animals with bovine spinal muscular atrophy. Protein exhibits no detectable in vitro catalytic activity, but the mutated gene complements the growth defect of a homologous yeast knock-out strain as well as the healthy variant
additional information
-
identification of Arabidopsis thaliana leaf ionomic mutant 7113, termed tsc10a-1. Double mutant progeny plants lacking both genes are not recovered from crosses of single tsc10A and tsc10B mutants. Plant 3-KDS reductase activity is reduced to 10% of wild-type levels in the loss-of-function tsc10a mutant, leading to an altered sphingolipid profile
additional information
-
construction of an enzyme-deficient mutant by gene replacement, the mutant produces lower levels of inositolphosphorylceramides
additional information
-
mutation of any of the three residues that constitute the catalytic triad of FVT1 do not completely inactivate the enzyme, as it is able to support growth of tsc10DELTA mutant cells at 26°C, but not at 37°C. Deletion of residues 4-26 from the FVT1-GFP protein abolishes ER localization
additional information
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construction of the deletion mutant TscDELTA38p
additional information
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cobstruction of a tsc10 knockout mutant strain, analysis of lipid and ceramide profiles compared to wild-type strain, quantitative real time RT-PCR expression analysis, phenotype, overview
additional information
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cobstruction of a tsc10 knockout mutant strain, analysis of lipid and ceramide profiles compared to wild-type strain, quantitative real time RT-PCR expression analysis, phenotype, overview
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in yeast cells
gene 3kdsr, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative expression analysis
S4SCP5
gene ksr1, DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain JM109(DE3)
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gene ksrA, DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain JM109(DE3)
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gene tsc10, expression of mutant tscDELTA38 in Escherichia coli strain BL21(DE3)
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genes At3g06060/TSC10A and At5g19200/TSC10B, i.e. tsc10A and tsc10B, expression of GFP-TSC10A and GFP-TSC10B in tsc10DELTA yeast mutant cells, heterologous expression of the two genes from Arabidopsis thaliana in 3-KDS reductase-deficient Saccharomyces cerevisiae mutant strain, tsc10DELTA, restores the enzyme activity
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is upregulated showing increased expression during the bacterial challenge
S4SCP5
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
naturally occuring missense mutation A175T is linked to animals with bovine spinal muscular atrophy. Protein exhibits no detectable in vitro catalytic activity, but the mutated gene complements the growth defect of a homologous yeast knock-out strain as well as the healthy variant
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beeler, T.; Bacikova, D.; Gable, K.; Hopkins, L.; Johnson, C.; Slife, H.; Dunn, T.
The Saccharomyces cerevisiae TSC10/BR265w gene encoding 3-ketosphinganine reductase is identified in a screen for temperature-sensitive suppressors of the Ca2+-sensitive csg2delta mutant
J. Biol. Chem.
273
30688-30694
1998
Saccharomyces cerevisiae
brenda
Mandon, E.C.; Ehses, I.; Rother, J.; van Echten, G.; Sandhoff, K.
Subcellular localization and membrane topology of serine palmitoyltransferase, 3-dehydrosphinganine reductase, and sphinganine N-acyltransferase in mouse liver
J. Biol. Chem.
267
11144-11148
1992
Mus musculus
brenda
Stoffel, W.; LeKim, D.; Sticht, G.
Stereospecificity of the NADPH-dependent reduction reaction of 3-oxodihydrosphingosine (2-amino-1-hydroxyoctadecane-3-one)
Hoppe-Seyler's Z. Physiol. Chem.
349
1637-1644
1968
Bos taurus, Rattus norvegicus
brenda
Stoffel, W.; LeKim, D.; Sticht, G.
Biosynthesis of dihydrosphingosine in vitro
Hoppe-Seyler's Z. Physiol. Chem.
349
664-670
1968
Wickerhamomyces ciferrii, Rattus norvegicus
brenda
Kihara, A.; Igarashi, Y.
FVT-1 is a mammalian 3-ketodihydrosphingosine reductase with an active site that faces the cytosolic side of the endoplasmic reticulum membrane
J. Biol. Chem.
279
49243-49250
2004
Homo sapiens (Q06136), Homo sapiens, Mus musculus (Q6GV12), Mus musculus
brenda
Fornarotto, M.; Xiao, L.; Hou, Y.; Koch, K.A.; Chang, E.; OMalley, R.M.; Black, T.A.; Cable, M.B.; Walker, S.S.
Sphingolipid biosynthesis in pathogenic fungi: identification and characterization of the 3-ketosphinganine reductase activity of Candida albicans and Aspergillus fumigatus
Biochim. Biophys. Acta
1761
52-63
2006
Aspergillus fumigatus, Saccharomyces cerevisiae, Candida albicans
brenda
Krebs, S.; Medugorac, I.; Roether, S.; Straesser, K.; Foerster, M.
A missense mutation in the 3-ketodihydrosphingosine reductase FVT1 as candidate causal mutation for bovine spinal muscular atrophy
Proc. Natl. Acad. Sci. USA
104
6746-6751
2007
Bos taurus (Q2KIJ5), Bos taurus
brenda
Gupta, S.D.; Gable, K.; Han, G.; Borovitskaya, A.; Selby, L.; Dunn, T.M.; Harmon, J.M.
Tsc10p and FVT1: Topologically distinct short-chain reductases required for long-chain base synthesis in yeast and mammals
J. Lipid Res.
50
1630-1640
2009
Saccharomyces cerevisiae, Homo sapiens
brenda
Kim, S.; Noh, Y.; Koo, J.; Da Silva, N.; Yun, H.
Effects of expression of lcb1/lcb2 and lac1/lag1 genes on the biosynthesis of ceramides
Biotechnol. Bioprocess Eng.
16
1-6
2011
Saccharomyces cerevisiae, Saccharomyces cerevisiae KCCM 50515
-
brenda
Timmins-Schiffman, E.; Roberts, S.
Characterization of genes involved in ceramide metabolism in the Pacific oyster (Crassostrea gigas)
BMC Res. Notes
5
502
2012
Crassostrea gigas ( S4SCP5), Crassostrea gigas
brenda
Chao, D.Y.; Gable, K.; Chen, M.; Baxter, I.; Dietrich, C.R.; Cahoon, E.B.; Guerinot, M.L.; Lahner, B.; Lue, S.; Markham, J.E.; Morrissey, J.; Han, G.; Gupta, S.D.; Harmon, J.M.; Jaworski, J.G.; Dunn, T.M.; Salt, D.E.
Sphingolipids in the root play an important role in regulating the leaf ionome in Arabidopsis thaliana
Plant Cell
23
1061-1081
2011
Arabidopsis thaliana
brenda
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