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Enzyme Nomenclature
Information on EC 1.1.1.102 - 3-dehydrosphinganine reductase
for references in articles please use BRENDA:EC1.1.1.102
Word Map on EC 1.1.1.102
- 1.1.1.102
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sphingolipids
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nadph-dependent
- ceramide
- l-serine
- sphingomyelin
- palmitoyl-coa
- phytosphingosine
-
inositolphosphorylceramide
- food industry
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.102
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RECOMMENDED NAME
GeneOntology No.
3-dehydrosphinganine reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sphinganine + NADP+ = 3-dehydrosphinganine + NADPH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
S4SCP5
the enzyme is involved in de novo generation of ceramide and in invertebrate stress response
physiological function
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3-KDS reductase is essential for sphingolipid biosynthesis. Reduced 3-KDS reductase activity in Arabidopsis thaliana roots drives changes in the leaf Ionome
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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
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?
(S)-2-amino-1-hydroxyoctadecane-3-one + NADPH
(S)-2-amino-1-(R)-3-dihydroxyoctadecane + NADP+
2-amino-1-hydroxyoctadecane-3-one + NADPH
2-amino-1,3-dihydroxyoctadecane + NADP+
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?
3-oxosphinganine + NADPH + H+
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
(S)-2-amino-1-hydroxyoctadecane-3-one + NADPH
(S)-2-amino-1-(R)-3-dihydroxyoctadecane + NADP+
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(S)-2-amino-1-hydroxyoctadecane-3-one + NADPH
(S)-2-amino-1-(R)-3-dihydroxyoctadecane + NADP+
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?
(S)-2-amino-1-hydroxyoctadecane-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-hydroxyoctadecane-3-one + NADPH
2-amino-1-(R)-3-dihydroxyoctadecane + NADP+
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?
2-amino-1-hydroxyoctadecane-3-one + NADPH
2-amino-1-(R)-3-dihydroxyoctadecane + NADP+
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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-hydroxyoctadecane-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-hydroxyoctadecane-3-one + NADPH
2-amino-1,3-dihydroxyoctadecane + NADP+
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?
3-oxosphinganine + NADPH + H+
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
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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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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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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the 3-KDS reductase genes are functionally redundant and ubiquitously expressed in Arabidopsis thaliana
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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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N-terminal membrane-spanning domain in FVT1 orients to place it in the endoplasmic reticulum lumen
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Tsc10p localizes to the yeast endoplasmic reticulum membrane
of endoplasmic reticulum, the large hydrophilic domain, which contains putative active site residues, faces the cytosol
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
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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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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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ENGINEERING
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
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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
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construction of an enzyme-deficient mutant by gene replacement, the mutant produces lower levels of inositolphosphorylceramides
additional information
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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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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.102)
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