BRENDA - Enzyme Database
show all sequences of 1.14.18.5

Synthesis of 4-hydroxysphinganine and characterization of sphinganine hydroxylase activity in corn

Wright, B.S.; Snow, J.W.; OBrien, T.C.; Lynch, D.V.; Arch. Biochem. Biophys. 415, 184-192 (2003)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.033
-
NADPH
pH 6.5, 30C
Zea mays
0.058
-
NADH
pH 6.5, 30C
Zea mays
0.06
-
D-erythro-sphinganine
pH 6.5, 30C
Zea mays
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum
associated with endoplasmic reticulum
Zea mays
5783
-
Organism
Organism
UniProt
Commentary
Textmining
Zea mays
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
shoot
-
Zea mays
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
D-erythro-eicosasphinganine + NADH + H+ + O2
-
733207
Zea mays
4-hydroxyeicosasphinganine + NAD+ + H2O
-
-
-
?
D-erythro-sphinganine + NADH + H+ + O2
-
733207
Zea mays
4-hydroxysphinganine + NAD+ + H2O
free 4-hydroxysphinganine is produced in excised corn shoots by the direct hydroxylation of sphinganine and not from the breakdown of complex sphingolipids
-
-
?
D-erythro-sphinganine + NADPH + H+ + O2
-
733207
Zea mays
4-hydroxysphinganine + NADP+ + H2O
-
-
-
?
additional information
DL-threo-sphinganine is not an effective substrate. Individual ceramide species having 2-, 6-,8-, or 24-carbon fatty acyl chains amide-linked to sphinganine are hydroxylated with similar efficiency as free sphinganine
733207
Zea mays
?
-
-
-
-
N-acetylsphinganine + NADPH + H+ + O2
-
733207
Zea mays
N-acetyl-4-hydroxysphinganine + NADP+ + H2O
-
-
-
?
N-hexanoylsphinganine + NADPH + H+ + O2
-
733207
Zea mays
N-hexanoyl-4-hydroxysphinganine + NADP+ + H2O
-
-
-
?
N-octanoylsphinganine + NADPH + H+ + O2
-
733207
Zea mays
N-octanoyl-4-hydroxysphinganine + NADP+ + H2O
-
-
-
?
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.033
-
NADPH
pH 6.5, 30C
Zea mays
0.058
-
NADH
pH 6.5, 30C
Zea mays
0.06
-
D-erythro-sphinganine
pH 6.5, 30C
Zea mays
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum
associated with endoplasmic reticulum
Zea mays
5783
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
shoot
-
Zea mays
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
D-erythro-eicosasphinganine + NADH + H+ + O2
-
733207
Zea mays
4-hydroxyeicosasphinganine + NAD+ + H2O
-
-
-
?
D-erythro-sphinganine + NADH + H+ + O2
-
733207
Zea mays
4-hydroxysphinganine + NAD+ + H2O
free 4-hydroxysphinganine is produced in excised corn shoots by the direct hydroxylation of sphinganine and not from the breakdown of complex sphingolipids
-
-
?
D-erythro-sphinganine + NADPH + H+ + O2
-
733207
Zea mays
4-hydroxysphinganine + NADP+ + H2O
-
-
-
?
additional information
DL-threo-sphinganine is not an effective substrate. Individual ceramide species having 2-, 6-,8-, or 24-carbon fatty acyl chains amide-linked to sphinganine are hydroxylated with similar efficiency as free sphinganine
733207
Zea mays
?
-
-
-
-
N-acetylsphinganine + NADPH + H+ + O2
-
733207
Zea mays
N-acetyl-4-hydroxysphinganine + NADP+ + H2O
-
-
-
?
N-hexanoylsphinganine + NADPH + H+ + O2
-
733207
Zea mays
N-hexanoyl-4-hydroxysphinganine + NADP+ + H2O
-
-
-
?
N-octanoylsphinganine + NADPH + H+ + O2
-
733207
Zea mays
N-octanoyl-4-hydroxysphinganine + NADP+ + H2O
-
-
-
?
Expression
Organism
Commentary
Expression
Zea mays
sphinganine hydroxylase activity in microsomes isolated from corn shoots treated with fumonisin B1 increases more than 3fold compared to controls
up
Expression (protein specific)
Organism
Commentary
Expression
Zea mays
sphinganine hydroxylase activity in microsomes isolated from corn shoots treated with fumonisin B1 increases more than 3fold compared to controls
up
Other publictions for EC 1.14.18.5
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
Synonyms
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)
734653
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720322
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1
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1
1
1
1
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719486
Idkowiak-Baldys
Sphingolipid C4 hydroxylation ...
Saccharomyces cerevisiae
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1
1
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721116
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Cloning and functional charact ...
Wickerhamomyces ciferrii
Yeast
21
437-443
2004
-
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1
-
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4
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1
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1
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1
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733207
Wright
Synthesis of 4-hydroxysphingan ...
Zea mays
Arch. Biochem. Biophys.
415
184-192
2003
-
-
-
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3
1
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1
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1
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7
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3
1
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1
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7
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1
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1
-
-
733375
Idkowiak-Baldys
Structure-function studies of ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1618
17-24
2003
-
-
-
-
19
-
-
-
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2
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1
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2
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19
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1
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1
1
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734141
Ternes
Identification and characteriz ...
Mus musculus
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277
25512-25518
2002
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1
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1
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719481
Sperling
Functional characterization of ...
Arabidopsis thaliana
FEBS Lett.
494
90-94
2001
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1
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4
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719795
Grilley
Syringomycin action gene SYR2 ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303C
J. Biol. Chem.
273
11062-11068
1998
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1
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4
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2
2
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719792
Haak
Hydroxylation of Saccharomyces ...
Saccharomyces cerevisiae
J. Biol. Chem.
272
29704-29710
1997
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2
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