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Information on EC 1.1.1.102 - 3-dehydrosphinganine reductase for references in articles please use BRENDA:EC1.1.1.102
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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
tsc10, tsc10p, fvt-1, 3-ketosphinganine reductase, kds reductase, 3-kds reductase, tsc10a, 3-ketodihydrosphingosine reductase, ksr1p, 3-oxosphinganine reductase,
more
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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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D-3-oxosphinganine reductase
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D-3-oxosphinganine:B-NADPH oxidoreductase
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3-ketodihydrosphingosine reductase
S4SCP5
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3-ketodihydrosphingosine reductase
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3-ketodihydrosphingosine reductase
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3-ketosphinganine reductase
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3-ketosphinganine reductase
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3-ketosphinganine reductase
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3-ketosphinganine reductase
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FVT-1
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Fvt1
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KDS reductase
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additional information
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the enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes
additional information
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the enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes
additional information
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the enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes
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sphinganine + NADP+ = 3-dehydrosphinganine + NADPH + H+
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D-erythro-dihydrosphingosine:NADP+ 3-oxidoreductase
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(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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-
-
?
2-amino-1-hydroxyoctadecane-3-one + NADPH
2-amino-1-(R)-3-dihydroxyoctadecane + NADP+
3-dehydrosphinganine + NADPH
sphinganine + NADP+
3-dehydrosphinganine + NADPH + H+
sphinganine + NADP+
3-ketodihydrosphingosine + NADPH
dihydrosphingosine + NADP+
3-oxosphinganine + NADPH + H+
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
3-oxosphinganine + NADPH + H+
dihydrosphingosine + NADP+
S4SCP5
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-
-
?
additional information
?
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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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-
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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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?
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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?
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-dehydrosphinganine + NADPH + H+
sphinganine + NADP+
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?
3-dehydrosphinganine + NADPH + H+
sphinganine + NADP+
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-
-
-
?
3-ketodihydrosphingosine + NADPH
dihydrosphingosine + NADP+
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-
-
?
3-ketodihydrosphingosine + NADPH
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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-
?
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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TSC10A lacks stereospecificity
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additional information
?
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FVT1 can replace Tsc10p in yeast
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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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(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-dehydrosphinganine + NADPH
sphinganine + NADP+
3-oxosphinganine + NADPH + H+
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
3-oxosphinganine + NADPH + H+
dihydrosphingosine + NADP+
S4SCP5
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?
3-dehydrosphinganine + NADPH
sphinganine + 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
-
-
?
3-dehydrosphinganine + NADPH
sphinganine + NADP+
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the enzyme catalyzes an early step in the sphingolipid biosynthesis, overview
-
-
?
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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NADPH
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siRNA
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reduces expression of transfected FVT1 mRNA and protein by at least 70%
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tergitol
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0.2%, 10fold activation of 2-amino-1-hydroxyoctadecane-3-one reduction
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Carcinogenesis
Identification of target genes regulated by FOXC1 using nickel agarose-based chromatin enrichment.
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.
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0.03
(S)-2-amino-1-hydroxyeicosane-3-one
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0.015
(S)-2-amino-1-hydroxyoctadecane-3-one
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0.009
3-dehydrosphinganine
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pH 7.5, recombinant enzyme
0.003
3-ketodihydrosphingosine
pH 7.5, 37°C
additional information
additional information
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binding kinetics of substrate analogues with shorter chain lengths
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1.07
3-dehydrosphinganine
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pH 7.5, recombinant enzyme
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0.000121
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vesicles from smooth and rough endoplasmic reticulum
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7.5
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assay at
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genes At3g06060/TSC10A and At5g19200/TSC10B, i.e. tsc10A and tsc10B
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brenda
gene ksrA
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gene ksr1
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brenda
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S4SCP5
UniProt
brenda
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gene tsc10
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brenda
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brenda
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brenda
isoform Fvt1
SwissProt
brenda
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SwissProt
brenda
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brenda
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brenda
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SwissProt
brenda
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brenda
gene tsc10
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-
brenda
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-
brenda
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-
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low expression
brenda
S4SCP5
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brenda
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-
brenda
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-
brenda
pheripheral blood, low expression
brenda
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-
brenda
highest expression
brenda
high expression
brenda
high expression
brenda
low expression
brenda
additional information
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the 3-KDS reductase genes are functionally redundant and ubiquitously expressed in Arabidopsis thaliana
brenda
high expression
brenda
low level of expression
brenda
high expression
brenda
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-
brenda
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-
brenda
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-
brenda
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-
brenda
high expression
brenda
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-
brenda
high expression
brenda
low level of expression
brenda
low level of expression
brenda
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brenda
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brenda
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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C-terminus of FVT1
brenda
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N- and C-terminus of Tsc10p
brenda
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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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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
of endoplasmic reticulum
brenda
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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
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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TSC10_ASHGO
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
307
1
32760
Swiss-Prot
TSC10_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
310
1
34926
Swiss-Prot
TSC10_CANGA
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
363
1
40410
Swiss-Prot
TSC10_CRYNB
Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
335
2
36504
Swiss-Prot
TSC10_CRYNJ
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565)
335
2
36490
Swiss-Prot
TSC10_DEBHA
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968)
328
1
36663
Swiss-Prot
TSC10_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
369
2
40461
Swiss-Prot
TSC10_KLULA
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
313
1
34859
Swiss-Prot
TSC10_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
362
3
39647
Swiss-Prot
TSC10_YARLI
Yarrowia lipolytica (strain CLIB 122 / E 150)
372
3
40734
Swiss-Prot
TSC10_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
320
1
35973
Swiss-Prot
TC10A_ARATH
326
1
34980
Swiss-Prot
TC10B_ARATH
331
2
35835
Swiss-Prot
KDSR_BOVIN
331
1
36020
Swiss-Prot
KDSR_DICDI
334
1
36470
Swiss-Prot
KDSR_HUMAN
332
1
36187
Swiss-Prot
KDSR_MOUSE
332
1
35956
Swiss-Prot
A0A2P6PRB5_ROSCH
293
2
32272
TrEMBL
A0A2I0A9D0_9ASPA
330
1
35795
TrEMBL
A0A2G9HIV9_9LAMI
327
1
35465
TrEMBL
A0A125YH44_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
503
2
54563
TrEMBL
A0A0F8AY10_CERFI
350
2
38466
TrEMBL
A0A0A1UEN1_ENTIV
337
3
37633
TrEMBL
A0A074TMZ3_HAMHA
505
3
54736
TrEMBL
A0A2P6PRD4_ROSCH
329
3
35587
TrEMBL
D7FNF8_ECTSI
195
1
20668
TrEMBL
A0A086Q5V8_TOXGO
263
0
28847
TrEMBL
A0A086K203_TOXGO
385
0
41953
TrEMBL
A0A2H3FPS1_9HELO
369
1
39983
TrEMBL
A0A0E0UA57_SINMB
Sinorhizobium meliloti (strain BL225C)
267
2
28821
TrEMBL
A0A1Z5K4C2_FISSO
353
1
38105
TrEMBL
G4V6G1_SCHMA
479
4
52820
TrEMBL
A0A086PJS4_TOXGO
263
2
28863
TrEMBL
A0A088S2B4_9TRYP
339
1
36170
TrEMBL
A0A3G2RYU5_9BASI
315
2
34736
TrEMBL
A0A396IX11_MEDTR
204
0
22517
TrEMBL
A0A086PJR5_TOXGO
240
2
25768
TrEMBL
A0A086Q5Y3_TOXGO
240
2
25734
TrEMBL
A0A1W2TI28_ROSNE
325
1
35518
TrEMBL
M2W815_GALSU
290
2
31618
TrEMBL
A0A086LQT6_TOXGO
79
1
8953
TrEMBL
A0A2G9HNL5_9LAMI
265
0
28475
TrEMBL
A0A2P6PRB6_ROSCH
274
0
29563
TrEMBL
A0A2P6PRE4_ROSCH
323
2
35021
TrEMBL
A0A2G9HG94_9LAMI
324
1
35391
TrEMBL
B9WMD9_CANDC
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841)
310
1
34914
TrEMBL
F0VEP8_NEOCL
Neospora caninum (strain Liverpool)
470
3
50750
TrEMBL
A0A396GVR5_MEDTR
86
2
9208
TrEMBL
B9RTW7_RICCO
456
1
50142
TrEMBL
A0A2H3ER15_9HELO
346
3
37145
TrEMBL
A0A086JPM1_TOXGO
503
2
54579
TrEMBL
B8LVQ6_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
359
1
38896
TrEMBL
A0A1G4IF34_TRYEQ
348
1
38046
TrEMBL
B7PLM8_IXOSC
288
2
31099
TrEMBL
B0E6T3_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
337
2
37868
TrEMBL
S7W9P9_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
503
2
54563
TrEMBL
A0A396JBD3_MEDTR
327
1
35669
TrEMBL
A0A0S1X8P3_9EURY
234
0
26114
TrEMBL
K0KMR8_WICCF
Wickerhamomyces ciferrii (strain F-60-10 / ATCC 14091 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031)
304
2
33851
TrEMBL
A0A2P6QX36_ROSCH
326
2
34878
TrEMBL
A0A2G9HL43_9LAMI
264
0
28577
TrEMBL
E9AEL0_LEIMA
338
1
35787
TrEMBL
A0A396H9J5_MEDTR
88
2
9917
TrEMBL
A0A1U9WWI9_PLAAG
270
1
29904
TrEMBL
K9Q0D7_9CYAN
267
1
28914
TrEMBL
W6VVG4_9RHIZ
260
2
27555
TrEMBL
A0A2G8Y4R6_TOXGO
503
2
54621
TrEMBL
A0A086LQT9_TOXGO
183
0
19871
TrEMBL
A0A2P6RNA7_ROSCH
257
0
27792
TrEMBL
A0A2P6PRC1_ROSCH
323
3
34839
TrEMBL
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150000
-
gel filtration1
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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
tetramer
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gel filtration
tetramer
-
gel filtration
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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
A175T
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mutation is deleterious to the human enzyme
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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recombinant Myc-His-tagged enzyme, Ni-NTA agarose
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Triton X-100, ammonium sulfate, calcium apatite, density gradient
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expressed in Escherichia coli, Myc-His-tagged enzyme
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expression in yeast cells
FVT1 expressed in CHO cells or yeast
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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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TSC10p expressed in CHO cells or yeast
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expression in yeast cells
expression in yeast cells
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the enzyme is upregulated showing increased expression during the bacterial challenge
S4SCP5
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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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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