BRENDA - Enzyme Database show
show all sequences of 1.1.1.102

Sphingolipids in the root play an important role in regulating the leaf ionome in Arabidopsis thaliana

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.; Plant Cell 23, 1061-1081 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
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
Arabidopsis thaliana
Engineering
Amino acid exchange
Commentary
Organism
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
Arabidopsis thaliana
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum membrane
-
Arabidopsis thaliana
5789
-
additional information
the plant isozymes contain an N-terminal membrane-spanning domain, subcellular localization study, overview
Arabidopsis thaliana
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-oxosphinganine + NADPH + H+
Arabidopsis thaliana
-
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
-
genes At3g06060/TSC10A and At5g19200/TSC10B, i.e. tsc10A and tsc10B
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
-
Arabidopsis thaliana
-
additional information
the 3-KDS reductase genes are functionally redundant and ubiquitously expressed in Arabidopsis thaliana
Arabidopsis thaliana
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-oxosphinganine + NADPH + H+
-
723408
Arabidopsis thaliana
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
-
-
-
?
additional information
TSC10A lacks stereospecificity
723408
Arabidopsis thaliana
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Arabidopsis thaliana
Cloned(Commentary) (protein specific)
Commentary
Organism
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
Arabidopsis thaliana
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Arabidopsis thaliana
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
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
Arabidopsis thaliana
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum membrane
-
Arabidopsis thaliana
5789
-
additional information
the plant isozymes contain an N-terminal membrane-spanning domain, subcellular localization study, overview
Arabidopsis thaliana
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-oxosphinganine + NADPH + H+
Arabidopsis thaliana
-
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
-
Arabidopsis thaliana
-
additional information
the 3-KDS reductase genes are functionally redundant and ubiquitously expressed in Arabidopsis thaliana
Arabidopsis thaliana
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-oxosphinganine + NADPH + H+
-
723408
Arabidopsis thaliana
D-erythro-dihydrosphingosine + L-threo-dihydrosphingosine + NADP+
-
-
-
?
additional information
TSC10A lacks stereospecificity
723408
Arabidopsis thaliana
?
-
-
-
-
General Information
General Information
Commentary
Organism
malfunction
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
Arabidopsis thaliana
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
Arabidopsis thaliana
General Information (protein specific)
General Information
Commentary
Organism
malfunction
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
Arabidopsis thaliana
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
Arabidopsis thaliana
Other publictions for EC 1.1.1.102
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
721947
Timmins-Schiffman
Characterization of genes invo ...
Crassostrea gigas
BMC Res. Notes
5
502
2012
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721891
Kim
-
Effects of expression of lcb1/ ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae KCCM 50515
Biotechnol. Bioprocess Eng.
16
1-6
2011
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723408
Chao
Sphingolipids in the root play ...
Arabidopsis thaliana
Plant Cell
23
1061-1081
2011
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699413
Gupta
Tsc10p and FVT1: Topologically ...
Homo sapiens, Saccharomyces cerevisiae
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50
1630-1640
2009
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2
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689780
Krebs
A missense mutation in the 3-k ...
Bos taurus
Proc. Natl. Acad. Sci. USA
104
6746-6751
2007
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667831
Fornarotto
Sphingolipid biosynthesis in p ...
Aspergillus fumigatus, Candida albicans, Saccharomyces cerevisiae
Biochim. Biophys. Acta
1761
52-63
2006
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FVT-1 is a mammalian 3-ketodih ...
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Beeler
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Subcellular localization and m ...
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11144-11148
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285699
Stoffel
Stereospecificity of the NADPH ...
Bos taurus, Rattus norvegicus
Hoppe-Seyler's Z. Physiol. Chem.
349
1637-1644
1968
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285700
Stoffel
Biosynthesis of dihydrosphingo ...
Pichia ciferrii, Rattus norvegicus
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349
664-670
1968
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