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Information on EC 1.1.1.102 - 3-dehydrosphinganine reductase and Organism(s) Homo sapiens and UniProt Accession Q06136

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Homo sapiens
UNIPROT: Q06136 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
tsc10, tsc10p, fvt-1, 3-ketosphinganine reductase, 3-ketodihydrosphingosine reductase, kds reductase, 3-kds reductase, tsc10a, 3-dehydrosphinganine reductase, ksr1p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-ketodihydrosphingosine reductase
-
KDS reductase
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3-oxosphinganine reductase
-
-
-
-
3-oxosphinganine:NADPH oxidoreductase
-
-
-
-
D-3-dehydrosphinganine reductase
-
-
-
-
D-3-oxosphinganine reductase
-
-
-
-
D-3-oxosphinganine:B-NADPH oxidoreductase
-
-
-
-
DSR
-
-
-
-
Fvt1
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
D-erythro-dihydrosphingosine:NADP+ 3-oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37250-36-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-ketodihydrosphingosine + NADPH
dihydrosphingosine + NADP+
show the reaction diagram
-
-
-
?
3-dehydrosphinganine + NADPH + H+
sphinganine + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
FVT1 can replace Tsc10p in yeast
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
siRNA
-
reduces expression of transfected FVT1 mRNA and protein by at least 70%
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
3-ketodihydrosphingosine
pH 7.5, 37°C
0.028
NADPH
pH 7.5, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
low expression
Manually annotated by BRENDA team
high expression
Manually annotated by BRENDA team
pheripheral blood, low expression
Manually annotated by BRENDA team
high expression
Manually annotated by BRENDA team
low expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
of endoplasmic reticulum, the large hydrophilic domain, which contains putative active site residues, faces the cytosol
Manually annotated by BRENDA team
-
C-terminus of FVT1
Manually annotated by BRENDA team
-
N-terminal membrane-spanning domain in FVT1 orients to place it in the endoplasmic reticulum lumen
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KDSR_HUMAN
332
1
36187
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
-
gel filtration1
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
gel filtration
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A175T
-
mutation is deleterious to the human enzyme
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in yeast cells
FVT1 expressed in CHO cells or yeast
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Homo sapiens, Saccharomyces cerevisiae
Manually annotated by BRENDA team