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acyl-CoA + L-serine
CoA + ?
-
-
-
-
?
arachidoyl-CoA + L-serine
CoA + 2-amino-1-hydroxydocosan-3-one + CO2
-
37% activity compared to that with palmitoyl-CoA
-
-
?
caproyl-CoA + L-serine
?
very low activity
-
-
?
elaidoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-trans-11-eicosen-3-one + CO2
-
39% activity compared to that with palmitoyl-CoA
-
-
?
heptadecanoyl-CoA + L-serine
?
L-alanine + palmitoyl-CoA
CoA + (2S)-2-aminooctadecan-3-one + CO2
-
-
-
-
?
L-alanine + stearoyl-CoA
CoA + (2S)-2-aminoicosan-3-one + CO2
-
-
-
-
?
L-serine + palmitoyl-CoA
CoA + 3-dehydro-D-sphinganine + CO2
L-serine + stearoyl-CoA
CoA + (2S)-2-amino-1-hydroxyicosan-3-one + CO2
-
-
-
-
?
lauroyl-CoA + L-serine
CoA + 2-amino-1-hydroxytetradecan-3-one + CO2
myristoleoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-cis-11-hexadecen-3-one + CO2
-
46% activity compared to that with palmitoyl-CoA
-
-
?
myristoyl-CoA + L-serine
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
myristoyl-CoA + L-serine
CoA + ? + CO2
n-heptadecanoyl-CoA + L-serine
CoA + 2-amino-1-hydroxynonadecan-3-one + CO2
oleoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-11-cis-eicosen-3-one + CO2
-
57% activity compared to that with palmitoyl-CoA
-
-
?
palmitoleoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-cis-11-octadecen-3-one + CO2
palmitoyl-CoA + L-alanine
CoA + (2S)-2-aminooctadecan-3-one + CO2
palmitoyl-CoA + L-serine
3-dehydrosphinganine + CoA + CO2
Rhizorhabdus wittichii
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
palmitoyl-CoA + [1,2,3-13C,2-15N] L-serine
?
palmitoyl-CoA + [2,3,3-D] L-serine
?
palmitoyl-CoA + [2-13C] L-serine
?
palmitoyl-CoA + [3,3-D] L-serine
?
pentadecanoyl-CoA + L-serine
?
S-(2-oxoheptadecyl)-CoA + L-serine
CoA + ?
stearoyl-CoA + L-serine
(2S)-2-amino-1-hydroxyicosan-3-one + CoA + CO2
Rhizorhabdus wittichii
-
-
-
-
?
stearoyl-CoA + L-serine
CoA + (2S)-2-amino-1-hydroxyicosan-3-one + CO2
stearoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyeicosan-3-one + CO2
-
51% activity compared to that with palmitoyl-CoA
-
-
?
additional information
?
-
heptadecanoyl-CoA + L-serine
?
-
-
-
-
?
heptadecanoyl-CoA + L-serine
?
-
-
-
-
?
heptadecanoyl-CoA + L-serine
?
-
less than 50% activity compared to palmitoyl-CoA
-
-
?
heptadecanoyl-CoA + L-serine
?
-
less than 50% activity compared to palmitoyl-CoA
-
-
?
L-serine + palmitoyl-CoA
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
L-serine + palmitoyl-CoA
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
L-serine + palmitoyl-CoA
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
lauroyl-CoA + L-serine
CoA + 2-amino-1-hydroxytetradecan-3-one + CO2
-
18% activity compared to that with palmitoyl-CoA
-
-
?
lauroyl-CoA + L-serine
CoA + 2-amino-1-hydroxytetradecan-3-one + CO2
18% activity compared to palmitoyl-CoA
-
-
?
myristoyl-CoA + L-serine
?
-
-
-
-
?
myristoyl-CoA + L-serine
?
-
-
-
-
?
myristoyl-CoA + L-serine
?
-
less than 50% activity compared to palmitoyl-CoA
-
-
?
myristoyl-CoA + L-serine
?
-
less than 50% activity compared to palmitoyl-CoA
-
-
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis
-
-
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
the viral enzyme exhibits preference for myristoyl-CoA rather than palmitoyl-CoA
-
-
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
-
-
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
second best substrate
-
-
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
75% activity compared to that with palmitoyl-CoA
-
-
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
75% activity compared to that with palmitoyl-CoA
-
-
?
myristoyl-CoA + L-serine
CoA + ? + CO2
-
-
-
-
?
myristoyl-CoA + L-serine
CoA + ? + CO2
-
recombinant SPTLC3 subunit in HEK-293 cells
-
-
?
n-heptadecanoyl-CoA + L-serine
CoA + 2-amino-1-hydroxynonadecan-3-one + CO2
-
75% activity compared to that with palmitoyl-CoA
-
-
?
n-heptadecanoyl-CoA + L-serine
CoA + 2-amino-1-hydroxynonadecan-3-one + CO2
-
75% activity compared to that with palmitoyl-CoA
-
-
?
palmitoleoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-cis-11-octadecen-3-one + CO2
-
80% activity compared to that with palmitoyl-CoA
-
-
?
palmitoleoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-cis-11-octadecen-3-one + CO2
-
80% activity compared to that with palmitoyl-CoA
-
-
?
palmitoyl-CoA + L-alanine
CoA + (2S)-2-aminooctadecan-3-one + CO2
wild-type enzyme can metabolize L-alanine under certain conditions
-
-
?
palmitoyl-CoA + L-alanine
CoA + (2S)-2-aminooctadecan-3-one + CO2
low activity with the wild-type enzyme, but increased activity with some mutants of the enzyme, overview
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
step in the sphingolipid biosynthetic pathway, overview
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
E2RKV3
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the viral enzyme exhibits preference for myristoyl-CoA rather than palmitoyl-CoA
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
key enzyme of sphingolipid metabolism
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
palmitoyl-CoA is the preferred substrate
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
optimal palmitoyl-CoA concentration is 0.2 mM
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
palmitoyl-CoA is used in preference to other saturated or unsaturated acyl-CoA substrates
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
100% activity
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
100% activity
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
palmitoyl-CoA is used in preference to other saturated or unsaturated acyl-CoA substrates
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
involved in cellular stress response
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
rate-limiting enzyme in synthesis of sphingolipids
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
rate-limiting enzyme in synthesis of sphingolipids
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
rate-limiting enzyme in synthesis of sphingolipids
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
initial step of de novo ceramide biosynthesis
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
initial step of de novo ceramide biosynthesis
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme catalyzes the initial and rate-limiting step in de novo sphingolipid synthesis. Potential role for overexpression of SPT in processes of cell metastasis
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids, the dynamic composition of the SPT complex could provide a cellular mechanism to adjust SPT activity to tissue specific requirements in sphingolipid synthesis
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first and rate-limiting step in the de novo synthesis of sphingolipids
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
key enzyme in ceramide synthesis, overview
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
initial step of de novo ceramide biosynthesis
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
i.e. 2-amino-1-hydroxyoctadecane-3-one, i.e. 3-oxo-dihydroxysphingosine
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
palmitoyl-CoA is the preferred substrate
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
palmitoyl-CoA is the preferred substrate
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
activities are greatest with palmitoyl-CoA and palmitelaidoyl-CoA, followed by fully saturated homologs, activity considerably diminishes as the alkyl-chain length increases or decreases, or with the presence of a cis-double bond
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
no other amino acids can substitute for serine
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
initial step of de novo ceramide biosynthesis
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme catalyses the first step in the ceramide biosynthesis pathway
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme is involved in the ceramide metabolism, overview
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
involved in cellular stress response
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
rate-limiting enzyme in synthesis of sphingolipids
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
initial step of de novo ceramide biosynthesis
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
initial step of de novo ceramide biosynthesis
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
100% activity
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
palmitoyl-CoA is the preferred substrate
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
no other amino acids can substitute for serine
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
rate-limiting enzyme in synthesis of sphingolipids
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
His159 is the anchoring site for L-serine and regulates the alpha-deprotonation of L-serine by fixing the conformation of the pyridoxal 5'-phosphate-L-serine aldimine to prevent unwanted side reactions
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
interaction between the hydroxyl group of the L-serine substrate and the 5'-phosphate group of pyridoxal 5'-phosphate. This interaction is important for substrate specificity and optimal catalytic efficiency
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
palmitoyl-CoA is the preferred substrate
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
no other amino acids can substitute for serine
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
i.e. 2-amino-1-hydroxyoctadecane-3-one, i.e. 3-oxo-dihydroxysphingosine
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
ir
palmitoyl-CoA + [1,2,3-13C,2-15N] L-serine
?
-
-
-
?
palmitoyl-CoA + [1,2,3-13C,2-15N] L-serine
?
-
-
-
-
?
palmitoyl-CoA + [2,3,3-D] L-serine
?
-
-
-
?
palmitoyl-CoA + [2,3,3-D] L-serine
?
-
-
-
-
?
palmitoyl-CoA + [2-13C] L-serine
?
-
-
-
?
palmitoyl-CoA + [2-13C] L-serine
?
-
-
-
-
?
palmitoyl-CoA + [3,3-D] L-serine
?
-
-
-
?
palmitoyl-CoA + [3,3-D] L-serine
?
-
-
-
-
?
pentadecanoyl-CoA + L-serine
?
-
-
-
-
?
pentadecanoyl-CoA + L-serine
?
-
-
-
-
?
pentadecanoyl-CoA + L-serine
?
-
less than 50% activity compared to palmitoyl-CoA
-
-
?
pentadecanoyl-CoA + L-serine
?
-
less than 50% activity compared to palmitoyl-CoA
-
-
?
S-(2-oxoheptadecyl)-CoA + L-serine
CoA + ?
-
-
-
?
S-(2-oxoheptadecyl)-CoA + L-serine
CoA + ?
-
-
-
?
stearoyl-CoA + L-serine
CoA + (2S)-2-amino-1-hydroxyicosan-3-one + CO2
-
-
-
-
?
stearoyl-CoA + L-serine
CoA + (2S)-2-amino-1-hydroxyicosan-3-one + CO2
-
-
-
?
additional information
?
-
the LCB2 subunit of the sphingolipid biosynthesis enzyme SPT can function as an attenuator of the hypersensitive response and Bax-induced cell death, overview
-
-
?
additional information
?
-
-
the viral single-chain enzyme might form multiprotein complexes in vivo with functions different from the monomer
-
-
?
additional information
?
-
-
acyl-CoA substrate specificity, overview
-
-
?
additional information
?
-
-
increasing the acyl-CoA chain length above C16 by 1 or 2 carbons is less detrimental to activity than similar decrements in chain length
-
-
?
additional information
?
-
-
44% reduction of SPT activity in patiens with hereditary sensory neuropathy type I with mutation T399G in the SPTLC1 gene. However the decrease in SPT activity has no effect on de novo sphingolipid biosynthesis, cellular sphingolipid content, cell proliferation and death. Despite the inhibition of mutant allele, the activity of nonmutant allele of SPT may be sufficient for adequate sphingolipid biosynthesis and cell viability. The neurodegeneration in HSN1 is likely to be caused by subtler and rather long-term effects of these mutations such as loss of a cell-type selective facet of sphingolipid metabolism and/or function, or perhaps accumulation of toxic species, including abnormal proteins
-
-
?
additional information
?
-
-
elevation of ceramide in serum lipoproteins during acute phase response to inflammation is accompanied by activation of serine-palmitoyl transferase in liver
-
-
?
additional information
?
-
-
mutations in the enzyme subunit SPTLC1 cause hereditary sensory and autonomic neuropathy type I, HSAN1, an adult onset, autosomal dominant neuropathy, HSAN1 patients have reduced SPT activity, link between mutant SPT and neuronal dysfunction
-
-
?
additional information
?
-
-
the expression of two SPT isoforms could be a cellular mechanism to adjust SPT activity to tissue-specific requirements of sphingolipid synthesis
-
-
?
additional information
?
-
-
ability of the ssSPT subunits to modulate the chain lengths of LCBs in mammalian cells
-
-
?
additional information
?
-
-
assay optimization measuring radio-labeled L-serine incorporation into 3-oxodihydrosphingosine in microsomes or crude cell lysate, usage of an nonradioactive HPLC-based detection protocol, overview
-
-
?
additional information
?
-
1-deoxysphingolipids are atypical sphingolipids that are formed by the enzyme serine palmitoyltransferase due to a promiscuous use of L-alanine over its canonical substrate L-serine. Wild-type SPT forms 1-deoxysphingolipids under certain conditions, and elevated levels are found in individuals with the metabolic syndrome and diabetes
-
-
?
additional information
?
-
-
1-deoxysphingolipids are atypical sphingolipids that are formed by the enzyme serine palmitoyltransferase due to a promiscuous use of L-alanine over its canonical substrate L-serine. Wild-type SPT forms 1-deoxysphingolipids under certain conditions, and elevated levels are found in individuals with the metabolic syndrome and diabetes
-
-
?
additional information
?
-
the small subunit of serine palmitoyltransferase a (ssSPTa) as an lysophosphatidylinositol acyltransferase 1 (LPIAT1)-interacting protein
-
-
?
additional information
?
-
-
elevation of ceramide in serum lipoproteins during acute phase response to inflammation is accompanied by activation of serine-palmitoyl transferase in liver
-
-
?
additional information
?
-
-
stearoyl-CoA desaturase-1 deficiency, SCD1 deficiency, reduces ceramide synthesis by downregulating SPT and increasing beta-oxidation in skeletal muscle
-
-
?
additional information
?
-
-
specificity
-
-
?
additional information
?
-
-
specificity
-
-
?
additional information
?
-
-
the enzyme activity and expression in the heart is not affected by high-fat feeding
-
-
?
additional information
?
-
no activity with L-phosphoserine
-
-
?
additional information
?
-
no activity with octanoyl-CoA
-
-
-
additional information
?
-
-
no activity with octanoyl-CoA
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis
-
-
?
myristoyl-CoA + L-serine
CoA + ? + CO2
-
recombinant SPTLC3 subunit in HEK-293 cells
-
-
?
palmitoyl-CoA + L-alanine
CoA + (2S)-2-aminooctadecan-3-one + CO2
wild-type enzyme can metabolize L-alanine under certain conditions
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
pentadecanoyl-CoA + L-serine
?
additional information
?
-
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
step in the sphingolipid biosynthetic pathway, overview
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
E2RKV3
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
key enzyme of sphingolipid metabolism
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
involved in cellular stress response
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
rate-limiting enzyme in synthesis of sphingolipids
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
rate-limiting enzyme in synthesis of sphingolipids
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
rate-limiting enzyme in synthesis of sphingolipids
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
initial step of de novo ceramide biosynthesis
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
initial step of de novo ceramide biosynthesis
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme catalyzes the initial and rate-limiting step in de novo sphingolipid synthesis. Potential role for overexpression of SPT in processes of cell metastasis
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids, the dynamic composition of the SPT complex could provide a cellular mechanism to adjust SPT activity to tissue specific requirements in sphingolipid synthesis
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first and rate-limiting step in the de novo synthesis of sphingolipids
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
key enzyme in ceramide synthesis, overview
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
initial step of de novo ceramide biosynthesis
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
initial step of de novo ceramide biosynthesis
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme catalyses the first step in the ceramide biosynthesis pathway
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme is involved in the ceramide metabolism, overview
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
involved in cellular stress response
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
rate-limiting enzyme in synthesis of sphingolipids
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
initial step of de novo ceramide biosynthesis
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
initial step of de novo ceramide biosynthesis
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
rate-limiting enzyme in synthesis of sphingolipids
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
ir
pentadecanoyl-CoA + L-serine
?
-
-
-
-
?
pentadecanoyl-CoA + L-serine
?
-
-
-
-
?
additional information
?
-
the LCB2 subunit of the sphingolipid biosynthesis enzyme SPT can function as an attenuator of the hypersensitive response and Bax-induced cell death, overview
-
-
?
additional information
?
-
-
the viral single-chain enzyme might form multiprotein complexes in vivo with functions different from the monomer
-
-
?
additional information
?
-
-
44% reduction of SPT activity in patiens with hereditary sensory neuropathy type I with mutation T399G in the SPTLC1 gene. However the decrease in SPT activity has no effect on de novo sphingolipid biosynthesis, cellular sphingolipid content, cell proliferation and death. Despite the inhibition of mutant allele, the activity of nonmutant allele of SPT may be sufficient for adequate sphingolipid biosynthesis and cell viability. The neurodegeneration in HSN1 is likely to be caused by subtler and rather long-term effects of these mutations such as loss of a cell-type selective facet of sphingolipid metabolism and/or function, or perhaps accumulation of toxic species, including abnormal proteins
-
-
?
additional information
?
-
-
elevation of ceramide in serum lipoproteins during acute phase response to inflammation is accompanied by activation of serine-palmitoyl transferase in liver
-
-
?
additional information
?
-
-
mutations in the enzyme subunit SPTLC1 cause hereditary sensory and autonomic neuropathy type I, HSAN1, an adult onset, autosomal dominant neuropathy, HSAN1 patients have reduced SPT activity, link between mutant SPT and neuronal dysfunction
-
-
?
additional information
?
-
-
the expression of two SPT isoforms could be a cellular mechanism to adjust SPT activity to tissue-specific requirements of sphingolipid synthesis
-
-
?
additional information
?
-
1-deoxysphingolipids are atypical sphingolipids that are formed by the enzyme serine palmitoyltransferase due to a promiscuous use of L-alanine over its canonical substrate L-serine. Wild-type SPT forms 1-deoxysphingolipids under certain conditions, and elevated levels are found in individuals with the metabolic syndrome and diabetes
-
-
?
additional information
?
-
-
1-deoxysphingolipids are atypical sphingolipids that are formed by the enzyme serine palmitoyltransferase due to a promiscuous use of L-alanine over its canonical substrate L-serine. Wild-type SPT forms 1-deoxysphingolipids under certain conditions, and elevated levels are found in individuals with the metabolic syndrome and diabetes
-
-
?
additional information
?
-
the small subunit of serine palmitoyltransferase a (ssSPTa) as an lysophosphatidylinositol acyltransferase 1 (LPIAT1)-interacting protein
-
-
?
additional information
?
-
-
elevation of ceramide in serum lipoproteins during acute phase response to inflammation is accompanied by activation of serine-palmitoyl transferase in liver
-
-
?
additional information
?
-
-
stearoyl-CoA desaturase-1 deficiency, SCD1 deficiency, reduces ceramide synthesis by downregulating SPT and increasing beta-oxidation in skeletal muscle
-
-
?
additional information
?
-
-
the enzyme activity and expression in the heart is not affected by high-fat feeding
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
the enzyme belongs to the PLP-superfamily and a member of the alpha-oxoamine synthase family (AOS, fold type I)
malfunction
-
IRS1 serine phosphorylation and PKCtheta recruitment to the plasma membrane are increased in cells with reduced SPT expression and activity. Short-term inhibition of SPT ameliorates palmitate/ceramide-induced insulin resistance, sustained loss/reduction in SPT expression/activity promotes greater partitioning of palmitate towards diacylglycerol synthesis, which impacts negatively upon IRS1-directed insulin signalling
malfunction
-
mutations in human SPT cause hereditary sensory autonomic neuropathy type 1, HSAN1, a disease characterized by loss of feeling in extremities and severe pain
malfunction
mutations in the SPTLC1 subunit associated with hereditary sensory and autonomic neuropathy type I
malfunction
-
both short and prolonged time of inhibition of the enzyme by myriocin is sufficient to prevent ceramide accumulation and simultaneously reverse palmitate induced inhibition of insulin-stimulated glucose transport
malfunction
enzyme inhibition promotes cell survival
malfunction
E2RKV3
enzyme inhibition promotes cell survival
malfunction
hereditary sensory and autonomic neuropathy type 1 (HSAN1) is a rare autosomal dominant inherited peripheral neuropathy caused by mutations in the SPTLC1 and SPTLC2 subunits of serine palmitoyltransferase. The mutations induce a permanent shift in the substrate preference from L-serine to L-alanine, which results in the pathological formation of atypical and neurotoxic 1-deoxy-sphingolipids. Overview of clinical features of HSAN1 patients with SPTLC1 mutations, genotype-phenotype association in HSAN1
malfunction
-
homozygous ssSPTa T-DNA mutants are not recoverable, and 50% nonviable pollen is detected in heterozygous ssSpta mutants. Pollen viability is recovered by expression of wild-type ssSPTa or ssSPTb under control of the ssSPTa promoter, indicating ssSPTa and ssSPTb functional redundancy. SPT activity and sensitivity to the PCD-inducing mycotoxin fumonisin B1 are increased by ssSPTa overexpression. Conversely, SPT activity and mycotoxin fumonisin B1 sensitivity are reduced in ssSPTa RNA interference lines
malfunction
-
inhibiting the enzyme in the astrocytes decreases the levels of both TNFalpha and interleukin-1beta in the conditioned media, which in turn reduced the neural and acidic sphingomyelinase activities and BACE1 level in primary neurons, overview
malfunction
knockdown of small subunit of serine palmitoyltransferase a decreases the an lysophosphatidylinositol acyltransferase 1-dependent incorporation of exogenous aracidonic acid into phosphatidylinositol but does not affect the in vitro enzyme activity of an lysophosphatidylinositol acyltransferase 1 in the microsomal fraction. ssSPTa knockdown decreases the protein level of LPIAT1 in the crude mitochondrial fraction but not in total homogenate or the microsomal fraction
malfunction
mutations in both subunits hLCB1 (e.g., C133W and C133Y) and hLCB2a (e.g., V359M, G382V, and I504F) are identified in patients with hereditary sensory and autonomic neuropathy type I (HSAN1), an inherited disorder that affects sensory and autonomic neurons. These mutations result in substrate promiscuity, leading to formation of neurotoxic deoxysphingolipids found in affected individuals. Structure homology modeling to understand the impact of the hLCB2a mutations on the mechanism of the enzyme using the structure data from the Sphingomonas paucimobilis enzyme
malfunction
myeloid cell-specific serine palmitoyltransferase subunit 2 haploinsufficiency reduces murine atherosclerosis. SPT subunit 2-haploinsufficient (Sptlc2+/-) macrophages have significantly lower SM levels in plasma membrane and lipid rafts. This reduction not only impairs inflammatory responses triggered by TLR4 and its downstream NF-kappaB and MAPK pathways, but also enhances reverse cholesterol transport mediated by ABC transporters. LDL receptor-deficient (Ldlr-/-) mice transplanted with Sptlc2+/- bone marrow cells exhibit significantly fewer atherosclerotic lesions after high-fat and high-cholesterol diet feeding. Additionally, Ldlr-/- mice with myeloid cell-specific Sptlc2 haploinsufficiency exhibit significantly less atherosclerosis than controls. Sptlc2 haploinsufficiency in macrophages leads to significant reductions of SM, glucosylceramide, and GM3 in macrophage plasma membranes and lipid rafts, resulting in altered raft distribution. Detailed phenotype overview
malfunction
the S384D but not the S384E mutation is associated with increased 1-deoxysphingolipids formation
malfunction
-
inhibiting the enzyme in the astrocytes decreases the levels of both TNFalpha and interleukin-1beta in the conditioned media, which in turn reduced the neural and acidic sphingomyelinase activities and BACE1 level in primary neurons, overview
-
metabolism
-
SPT catalyzes the first and rate-limiting step in the de novo synthesis of sphingolipids
metabolism
-
SPT catalyzes the first and rate-limiting step of the sphingolipid biosynthetic pathway
metabolism
-
SPT catalyzes the first and rate-limiting step of the sphingolipid biosynthetic pathway
metabolism
-
SPT catalyzes the first committed step in sphingolipid biosynthesis
metabolism
-
SPT catalyzes the rate-limiting step in the de novo synthesis of sphingolipids, subunit SPTLC3 generates C16-sphingoid bases, and sphingolipids with a C16 backbone constitute a significant proportion of human plasma sphingolipids
metabolism
SPT is a key enzyme of sphingolipid biosynthesis and catalyses the pyridoxal 5'-phosphate-dependent decarboxylative condensation reaction of L-serine with palmitoyl-CoA to generate 3-ketodihydrosphingosine
metabolism
-
SPT is the key regulator enzyme in the ceramide de novo biosynthesis pathway
metabolism
-
eukaryotic serine palmitoyltransferase is an integral endoplasmic reticulum membrane protein that contains a head-to-tail heterodimer of two related but distinct subunits, LCB1 and LCB2, with a single catalytic site. There are additional subunits necessary for maximal activity as well as associated negative regulatory components
metabolism
serine palmitoyltransferase is the first and rate-limiting enzyme of the de novo biosynthetic pathway of sphingomyelin. Both serine palmitoyltransferase and sphingomyelin are implicated in the pathogenesis of atherosclerosis, the development of which is driven by macrophages
metabolism
serine palmitoyltransferase long chain-1 (SPTLC1) is the first enzyme of sphingolipid biosynthesis
metabolism
-
serine palmitoyltransferase, composed of LCB1 and LCB2 subunits, catalyzes the primary regulatory point for sphingolipid synthesis
metabolism
several mutations in SPT are associated with the hereditary sensory and autonomic neuropathy type I, HSAN1. Wild-type SPT forms 1-deoxysphingolipids under certain conditions, and elevated levels are found in individuals with the metabolic syndrome and diabetes
metabolism
sphingolipids are essential components of cellular membranes formed from the condensation of L-serine and a long-chain acyl thioester. This first step is catalyzed by the pyridoxal 5'-phosphate-dependent enzyme serine palmitoyltransferase
metabolism
the enzyme catalyses the first step of de novo sphingolipid biosynthesis
metabolism
the enzyme catalyses the first step of de novo sphingolipid biosynthesis
metabolism
-
the first and rate-limiting step of de novo synthesis is the condensation of a fatty acyl-CoA, usually palmitoyl-CoA, with serine, which is catalyzed by the enzyme serine palmitoyltransferase to form 3-dehydrosphinganin
metabolism
the small subunit of serine palmitoyltransferase a (ssSPTa) as an lysophosphatidylinositol acyltransferase 1 (LPIAT1)-interacting protein and colocalizes with LPIAT1 in cultured mammalian cells
metabolism
-
SPT is a key enzyme of sphingolipid biosynthesis and catalyses the pyridoxal 5'-phosphate-dependent decarboxylative condensation reaction of L-serine with palmitoyl-CoA to generate 3-ketodihydrosphingosine
-
physiological function
in the endoplasmic reticulum subunit SPT1 is responsible for de novo sphingolipid biosynthesis, it is also present in other cellular compartments, including focal adhesions where it is associated with cell morphology
physiological function
-
SPT plays a crucial role in lipid-induced insulin resistance in skeletal muscle cells by desensitizing muscle cells to insulin in response to incubation with palmitate, overview. The effect is antagonized by inhibition of protein kinase C
physiological function
-
the enzyme is required for ceramide synthesis as key regulatory enzyme of this pathway, major mechanism for ceramide generation in NR8383 macrophages is stimulation of their de novo synthesis
physiological function
the enzyme is required for resistance against pathogen Pseudomonas cichorii. The gene for the LCB2 subunit of SPT is a potent inducer of hypersensitive response-like cell death involving pyridoxal 5'-phosphate
physiological function
the LCB2 subunit of the sphingolipid biosynthesis enzyme SPT can function as an attenuator of the hypersensitive response and Bax-induced cell death, not involved in the dominant-negative effect that results from BcLCB2 overexpression, overview
physiological function
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enzyme activators, the small subunits are essential for male gametophytes, are important for mycotoxin fumonisin B1 sensitivity, and limit sphingolipid synthesis in planta
physiological function
phosphorylation of serine palmitoyltransferase long chain-1 (SPTLC1) on tyrosine 164 by the fusion kinase BCR-ABL inhibits the SPTLC1 enzyme activity. Inhibition of BCR-ABL kinase using either imatinib or shRNA-mediated silencing leads to the activation of SPTLC1 and to increased apoptosis in both K562 and LAMA-84 cells, a mechanistic explanation for imatinib-mediated cell death
physiological function
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serine palmitoyltransferase in the astrocytes increases ceramide levels, which enhances the release of cytokines that mediate the activation of neural and acidic sphingomyelinase (N-SMase and A-SMase) in the neurons, to propagate the deleterious effects of palmitate, i.e. BACE1 upregulation and amyloidogenesis in primary rat neurons, overview
physiological function
specificity of wild-type SPT might by dynamically regulated by a phosphorylation at position S384
physiological function
the enzyme is required for de novo sphingolipid biosynthesis
physiological function
-
the role of the small activating subunits of serine palmitoyltransferase, ssSPTs, is to increase SPT activity without compromising substrate specificity
physiological function
the small subunit of serine palmitoyltransferase a (ssSPTa) plays a role in fatty acid remodeling of phosphatidyl inositol, probably by facilitating the MAM localization oflysophosphatidylinositol acyltransferase 1, LPIAT1
physiological function
-
serine palmitoyltransferase in the astrocytes increases ceramide levels, which enhances the release of cytokines that mediate the activation of neural and acidic sphingomyelinase (N-SMase and A-SMase) in the neurons, to propagate the deleterious effects of palmitate, i.e. BACE1 upregulation and amyloidogenesis in primary rat neurons, overview
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additional information
key active site residues are His159, Asp231, His234, and Lys265
additional information
structure modeling
additional information
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structure modeling
additional information
the interaction between the hydroxyl group of the L-serine substrate and the 5'-phosphate group of pyridoxal 5'-phosphate is important for substrate specificity and optimal catalytic efficiency. Structure of the PLP-L-serine external aldimine intermediate of the enzyme, PDB ID 2W8J, overview
additional information
wild-type and mutant enzyme structure homology modeling and structure-function analyses, overview
additional information
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wild-type and mutant enzyme structure homology modeling and structure-function analyses, overview
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K311E
construction of mutant BcLCB2DELTAK311E that shows reduced activity compared to the wild-type enzyme
C133W
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site-directed mutagenesis, mutation of subunit SPTLC1, construction of transgenic mouse lines that ubiquitously overexpress either wild-type SPTLC1WT or mutant SPTLC1C133W in brain and liver microsomes, SPTLC1C133W mice develop age-dependent weight loss and mild sensory and motor impairments, fed SPTLC1C133W mice lose large myelinated axons in the ventral root of the spinal cord and demonstrate myelin thinning, there is also a loss of large myelinated axons in the dorsal roots, although the unmyelinated fibers are preserved, in the dorsal root ganglia, IB4 staining is diminished, whereas expression of the injury-induced transcription factor ATF3 is increased, phenotype, detailed overview
R246G
-
naturally occuring mutation, comparison of de novo sphingolipid biosynthesis in wild-type LY-B cells and in LY-B cells expressing long-chain base subunit 1, LCB1, LC-ESI-MS/MS mass spectrometric analysis, overview
A182P
naturally occuring mutation in subunit LCB1 involved in hereditary sensory and autonomic neuropathy type I disease, and associated with increased synthesis of neurotoxic 1-deoxy-sphingolipids
A352V
subunit 1, naturally occuring mutation, reduced activity in cells expressing mutant protein
G246R
expression of mutant G246R in in LYB cells, which is the same mutation that is present in LYB endogenously, neither restores canonical activity nor results in the formation of 1-deoxy-sphingolipids
I505Y
naturally occuring mutation in subunit LCB2 involved in hereditary sensory and autonomic neuropathy type I disease, and associated with increased synthesis of neurotoxic 1-deoxy-sphingolipids. The mutant shows an increased canonical activity and increased formation of C20 sphingoid base, associated with an exceptionally severe HSAN1 phenotype, where C20 sphingosine levels are also confirmed in plasma of patients
S331Y
naturally occuring mutation in subunit LCB1 involved in hereditary sensory and autonomic neuropathy type I disease, and associated with increased synthesis of neurotoxic 1-deoxy-sphingolipids.The mutant shows an increased canonical activity and increased formation of C20 sphingoid base, associated with an exceptionally severe HSAN1 phenotype, where C20 sphingosine levels are also confirmed in plasma of patients
S384A
a subunit SPTLC2 phosphorylation site mutant, the mutation has no effect n enzyme activity
S384D
a subunit SPTLC2 phosphorylation site mutant, the mutation is associated with increased 1-deoxysphingolipids formation
S384E
a subunit SPTLC2 phosphorylation site mutant, the mutation is not associated with increased 1-deoxysphingolipids formation
Y164F
site-directed mutagenesis, the mutant shows increased serine palmitoyltransferase activity compared to the wild-type enzyme. The Y164F mutation also promotes the remodeling of cellular sphingolipid content, thereby sensitizing K562 cells to apoptosis. the Y164F mutation affects SPTLC1 subcellular localization, induction of apoptosis, and sell sensitivity to imatinib
Y387F
a subunit SPTLC2 phosphorylation site mutant, the mutation has no effect n enzyme activity
Y387F/S384A
a subunit SPTLC2 phosphorylation sites mutant, the mutation has no effect n enzyme activity
R370A
Rhizorhabdus wittichii
-
strictly conserved in all prokaryotic enzymes and the Icb2 subunit of eukaryotic enzymes, no catalytic activity
R370K
Rhizorhabdus wittichii
-
strictly conserved in all prokaryotic enzymes and the Icb2 subunit of eukaryotic enzymes, 3% catalytic activity of wild type enzyme
DELTA2-9SPT
mutant bearing deleted residues from Ala2 to Pro9: Km values are not significantly changed compared to wild-type
G268V
site-directed mutagenesis, the mutation perturbs the pyridoxal 5'-phosphate cofactor binding and reduces the affinity for both substrates, inactive mutant, the protein is expressed in a completely insoluble form, structure homology modeling of the mutant enzyme using the Sp SPT PLP-L-serine external aldimine structure, PDB ID 2W8J
G385F
site-directed mutagenesis, the mutation perturbs the pyridoxal 5'-phosphate cofactor binding, reduces the affinity for both substrates, decreases the enzyme activity, soluble protein
H159A
-
site-directed mutagenesis, the mutant shows reduced activity and still forms the pyridoxal 5'-phosphate-L-serine-aldimine reaction intermediate
H159W
-
site-directed mutagenesis, inactive mutant
H159Y
-
site-directed mutagenesis, inactive mutant
K265A
site-directed mutagenesis, the mutant is unable to bind pyridoxal 5'-phosphate, structure of a SPT K265A:PLP-myriocin external aldimine complex, molecular replacement study
N100C
site-directed mutagenesis, the mutation mimics the wild-type human enzyme and is fully active, crystal structure analysis
N100W
site-directed mutagenesis, the mutation mimics the mutation in the human enzyme causing hereditary sensory autonomic neuropathy type 1, the mutant shows reduced activity compared to the wild-type enzyme. The mutation affects the chemistry of the pyridoxal 5'-phosphate, crystal structure analysis
N100Y
site-directed mutagenesis, N100Y is less able to stabilize a quinonoid intermediate, the mutation mimics the mutation in the human enzyme causing hereditary sensory autonomic neuropathy type 1, the mutant shows reduced activity compared to the wild-type enzyme. The mutation affects the chemistry of the pyridoxal 5'-phosphate. The L-Ser external aldimine structure N100Y reveals significant differences that hinder the movement of a catalytically important Arg378 residue into the active site, crystal structure analysis
R378A
site-directed mutagenesis, crystal structure analysis, the mutant is less able to stabilize a quinonoid intermediate
R378K
the mutant shows lower specific activities for myristoyl-CoA and palmitoyl-CoA but greater efficiencies for caproyl- and lauroyl-CoA compared to the wild type enzyme
V246M
site-directed mutagenesis, the mutation perturbs the pyridoxal 5'-phosphate cofactor binding, reduces the affinity for both substrates, decreases the enzyme activity, soluble protein
N100C
-
site-directed mutagenesis, the mutation mimics the wild-type human enzyme and is fully active, crystal structure analysis
-
N100W
-
site-directed mutagenesis, the mutation mimics the mutation in the human enzyme causing hereditary sensory autonomic neuropathy type 1, the mutant shows reduced activity compared to the wild-type enzyme. The mutation affects the chemistry of the pyridoxal 5'-phosphate, crystal structure analysis
-
N100Y
-
site-directed mutagenesis, N100Y is less able to stabilize a quinonoid intermediate, the mutation mimics the mutation in the human enzyme causing hereditary sensory autonomic neuropathy type 1, the mutant shows reduced activity compared to the wild-type enzyme. The mutation affects the chemistry of the pyridoxal 5'-phosphate. The L-Ser external aldimine structure N100Y reveals significant differences that hinder the movement of a catalytically important Arg378 residue into the active site, crystal structure analysis
-
R378A
-
site-directed mutagenesis, crystal structure analysis, the mutant is less able to stabilize a quinonoid intermediate
-
R378N
-
site-directed mutagenesis, crystal structure analysis
-
C133W
-
subunit 1, naturally occuring mutation, causing sensory neurophaty type 1, forms stable inactive heterodimers with subunit 2, forms heterotrimers with subunit 2 and subunit 3 with 10-20% of wild-type activity, heterotrimers expressed in yeast synthesize also C18-1-deoxyshinganine and expressed in mammalian cells synthesize also C18-1-deoxyshinganine and C20-1-deoxyshinganine, mutant heterotrimeric enzymes are active in yeast and mammalian cells and have an enhanced ability to condense alanine with acyl-CoA
C133W
subunit 1, naturally occuring mutation, reduced activity in cells expressing mutant protein
C133W
naturally occuring mutation in subunit LCB1 involved in hereditary sensory and autonomic neuropathy type I disease, the mutant shows reduced activity compared tot he wild-type enzyme
C133W
naturally occuring mutation in subunit LCB1 involved in hereditary sensory and autonomic neuropathy type I disease, the mutant shows showa a significantly increased canonical activity and is associated with increased synthesis of neurotoxic 1-deoxy-sphingolipids
C133Y
-
reduced activity
C133Y
naturally occuring mutation in subunit LCB1 involved in hereditary sensory and autonomic neuropathy type I disease, the mutant shows reduced activity compared tot he wild-type enzyme
C133Y
naturally occuring mutation in subunit LCB1 involved in hereditary sensory and autonomic neuropathy type I disease, the mutant shows showa a significantly increased canonical activity and is associated with increased synthesis of neurotoxic 1-deoxy-sphingolipids
G382V
subunit 2, activity affected, naturally occuring mutation, hereditary sensory and autonomic neuropathy type I, expression in HEK293 cells increases concentration of neurotoxic 1-deoxysphinganine
G382V
naturally occuring mutation in subunit LCB2 involved in hereditary sensory and autonomic neuropathy type I disease, and associated with increased synthesis of neurotoxic 1-deoxy-sphingolipids
G382V
naturally occuring mutation in subunit LCB2a involved in hereditary sensory and autonomic neuropathy type I disease, the activity of mutant G382V is barely detectable above background
I504F
subunit 2, activity affected, naturally occuring mutation, hereditary sensory and autonomic neuropathy type I, expression in HEK293 cells increases concentration of neurotoxic 1-deoxysphinganine
I504F
naturally occuring mutation in subunit LCB2 involved in hereditary sensory and autonomic neuropathy type I disease, the mutant shows showa a significantly increased canonical activity and is associated with increased synthesis of neurotoxic 1-deoxy-sphingolipids
I504F
naturally occuring mutation in subunit LCB2a involved in hereditary sensory and autonomic neuropathy type I disease, the mutant shows reduced activity compared tot he wild-type enzyme
S331F
subunit 1, naturally occuring mutation, reduced activity in cells expressing mutant protein, accumulation of 1-deoxysphingoid bases in HEK293T cells expressing mutant protein
S331F
naturally occuring mutation in subunit LCB1 involved in hereditary sensory and autonomic neuropathy type I disease, and associated with increased synthesis of neurotoxic 1-deoxy-sphingolipids. The mutant shows an increased canonical activity and increased formation of C20 sphingoid base, associated with an exceptionally severe HSAN1 phenotype, where C20 sphingosine levels are also confirmed in plasma of patients. Expression of the p.S331F mutant in enzyme-deficient LYB cells fully restores canonical activity, and activity is even 9-10fold higher compared with the wild-type subunit
S384F
a subunit SPTLC2 phosphorylation site mutant, naturally occuring in hereditary sensory and autonomic neuropathy type I, HSAN1, families. Affected patients showed elevated plasma 1-deoxysphingolipid levels and expression of the S384F mutant in HEK-293 cells increased 1-deoxysphingolipid formation
S384F
naturally occuring mutation in subunit LCB2 involved in hereditary sensory and autonomic neuropathy type I disease, and associated with increased synthesis of neurotoxic 1-deoxy-sphingolipids
V359M
subunit 2, activity affected, naturally occuring mutation, hereditary sensory and autonomic neuropathy type I, expression in HEK293 cells increases concentration of neurotoxic 1-deoxysphinganine
V359M
naturally occuring mutation in subunit LCB2a involved in hereditary sensory and autonomic neuropathy type I disease, the mutant shows reduced activity compared tot he wild-type enzyme
H159F
mutant enzyme shows no activity
H159F
-
site-directed mutagenesis, inactive mutant
R378N
site-directed mutagenesis, crystal structure analysis
R378N
residue highly mobile, activity 40fold reduced
additional information
homozygous T-DNA insertion mutants for At LCB1 are not recoverable, but viability is restored by complementation with the wild-type At LCB1 gene, T-DNA disruption of AtLCB1 results in embryo lethality, partial RNAi suppression of At LCB1 expression is accompanied by a marked reduction in plant size that resulted primarily from reduced cell expansion, while the sphingolipid content remains unaltered, overview
additional information
-
homozygous T-DNA insertion mutants for At LCB1 are not recoverable, but viability is restored by complementation with the wild-type At LCB1 gene, T-DNA disruption of AtLCB1 results in embryo lethality, partial RNAi suppression of At LCB1 expression is accompanied by a marked reduction in plant size that resulted primarily from reduced cell expansion, while the sphingolipid content remains unaltered, overview
additional information
-
the identification of the fumonisin B1 resistant11-2 (fbr11-2) mutant, an allele of lcb1-1, is reported. The fbr11-2 mutation, is transmitted only through female gametophytes and causes the formation of abortive microspores. During the second pollen mitosis, fbr11-2 initiates apoptotic cell death in binucleated microspores characteristic of nuclear DNA fragmentation, followed by cytoplasm shrinkage and organelle degeneration at the trinucleated stage. A double mutant with T-DNA insertions in two homologous LCB2 genes show a phenotype similar to fbr11-2
additional information
-
T-DNA disruption of ssSPTa results in loss of pollen viability
additional information
construction of an inactive pyridoxal 5'-phosphate binding site deletion mutant BcLCB2DELTA307-314. Overexpression of BcLCB2 in Nicotiana tabacum cv. Xanthi leaves suppresses the hypersensitive cell death initiated by elicitors and PB90-triggered H2O2 accumulation, while NbLCB2 silencing in Nicotiana benthamiana enhances elicitor-triggered hypersensitive cell death. BcLCB2 overexpression suppresses Bax- and oxidant stress-triggered yeast cell death. Reactive oxygen species accumulation induced by Bax is compromised in BcLCB2-overexpressing Saccharomyces cerevisiae strain W303 cells, detailed overview
additional information
-
deficient mutant strain LY-B lacks LCB1 and has reduced content in LCB2, the latter is restored upon recombinant expression of LCB2
additional information
-
mutations in the enzyme subunit SPTLC1 cause hereditary sensory and autonomic neuropathy type I, HSAN1, an adult onset, autosomal dominant neuropathy, HSAN1 patients have reduced SPT activity
additional information
elimination of subunit SPT1 activity using SPTLC1 siRNA in HEK-293 cells causes cell rounding
additional information
an enzyme knockout strain, which completely lacks SPT activity, is not viable unless supplemented with a long chain base or a competent, active SPT complex. Coexpression of each of the three subunit hLCB2a mutants, V359M, G382V, and I504F, along with subunit hLCB1 results in low activity, with G382V barely detectable above background. When small subunit ssSPTb is expressed, heterodimers containing the G382V and I504F mutant hLCB2a subunits are activated to the same extent as wild-type heterodimers, but heterodimers containing the V359Mmutant subunit are less well activated
additional information
-
an enzyme knockout strain, which completely lacks SPT activity, is not viable unless supplemented with a long chain base or a competent, active SPT complex. Coexpression of each of the three subunit hLCB2a mutants, V359M, G382V, and I504F, along with subunit hLCB1 results in low activity, with G382V barely detectable above background. When small subunit ssSPTb is expressed, heterodimers containing the G382V and I504F mutant hLCB2a subunits are activated to the same extent as wild-type heterodimers, but heterodimers containing the V359Mmutant subunit are less well activated
additional information
-
deletion of the N-terminal 10 amino acids of small activating subunit of serine palmitoyltransferase isoforms ssSPTa or ssSPTb has no effect on the ability of the proteins to activate hLCB1/hLCB2a heterodimers sufficiently to complement growth of yeast lacking endogenous serine palmitoyltransferase. A chimera in which residues Glu27 to Pro54 of ssSPTa are replaced with residues Glu27 to Pro54 of ssSPTb or a chimera in which residues Glu27 to Gln68 of ssSPTa are replaced by residues Glu27 to Asn76 of ssSPTb is expressed in yeast, along with hLCB1 and hLCB2a, microsomal SPT assays show that both chimeric heterotrimers prefer palmitoyl-CoA as a substrate
additional information
knockdown of small subunit of serine palmitoyltransferase a, ssSPTa
additional information
mutations associated with the mild form cluster around the active site, whereas mutations associated with the severe form are located on the surface of the enzyme protein. Overview of clinical features of HSAN1 patients with SPTLC1 mutations, genotype-phenotype association in HSAN1
additional information
-
mutations associated with the mild form cluster around the active site, whereas mutations associated with the severe form are located on the surface of the enzyme protein. Overview of clinical features of HSAN1 patients with SPTLC1 mutations, genotype-phenotype association in HSAN1
additional information
reduced sphingolipid synthesis resulting from suppression of NbLCB2 expression interferes with normal leaf morphogenesis. NbLCB2 overexpression causes a cell death phenotype in Nicotiana benthamiana leaves. Downregulation of the genes encoding for the enzyme subunits compromises pathogen resistance against Pseudomonas cichorii
additional information
reduced sphingolipid synthesis resulting from suppression of NbLCB2 expression interferes with normal leaf morphogenesis. NbLCB2 overexpression causes a cell death phenotype in Nicotiana benthamiana leaves. Downregulation of the genes encoding for the enzyme subunits compromises pathogen resistance against Pseudomonas cichorii
additional information
-
reduced sphingolipid synthesis resulting from suppression of NbLCB2 expression interferes with normal leaf morphogenesis. NbLCB2 overexpression causes a cell death phenotype in Nicotiana benthamiana leaves. Downregulation of the genes encoding for the enzyme subunits compromises pathogen resistance against Pseudomonas cichorii
additional information
the phenotype of NbLCB1-silenced plants is almost the same as the control except for a slight downward curling of leaf edges in NbLCB1-silenced plants. Downregulation of the genes encoding for the enzyme subunits compromises pathogen resistance against Pseudomonas cichorii
additional information
the phenotype of NbLCB1-silenced plants is almost the same as the control except for a slight downward curling of leaf edges in NbLCB1-silenced plants. Downregulation of the genes encoding for the enzyme subunits compromises pathogen resistance against Pseudomonas cichorii
additional information
-
the phenotype of NbLCB1-silenced plants is almost the same as the control except for a slight downward curling of leaf edges in NbLCB1-silenced plants. Downregulation of the genes encoding for the enzyme subunits compromises pathogen resistance against Pseudomonas cichorii
additional information
-
SPT subunit LCB1 knockdown in L6 muscle cells by shRNA causes enzyme activity reduction by over 70%, silencing of LCB1 also leads to an attendant reduction in the expression of LCB2
additional information
-
natural mutant strains: SCS1/LCB2 knock-out mutant, scs1-1 mutant shows reduced activity, scs1-2 mutant is temperature-sensitive, but shows normal enzyme activity
additional information
-
tsc3 mutants show reduced enzyme activity, tsc3 is not required for expression, stability and membrane association of Lcb1p and Lcbp2
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Fungal metabolite sulfamisterin suppresses sphingolipid synthesis through inhibition of serine palmitoyltransferase
Biochemistry
44
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2005
Cricetulus griseus
brenda
Dedov, V.N.; Dedova, I.V.; Merrill, A.H., Jr.; Nicholson, G.A.
Activity of partially inhibited serine palmitoyltransferase is sufficient for normal sphingolipid metabolism and viability of HSN1 patient cells
Biochim. Biophys. Acta
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2004
Homo sapiens
brenda
Han, G.; Gable, K.; Yan, L.; Natarajan, M.; Krishnamurthy, J.; Gupta, S.D.; Borovitskaya, A.; Harmon, J.M.; Dunn, T.M.
The topology of the Lcb1p subunit of yeast serine palmitoyltransferase
J. Biol. Chem.
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Saccharomyces cerevisiae
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Carton, J.M.; Uhlinger, D.J.; Batheja, A.D.; Derian, C.; Ho, G.; Argenteri, D.; D'Andrea, M.R.
Enhanced serine palmitoyltransferase expression in proliferating fibroblasts, transformed cell lines, and human tumors
J. Histochem. Cytochem.
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Homo sapiens
brenda
Hanada, K.; Nishijima, M.
Purification of mammalian serine palmitoyltransferase, a hetero-subunit enzyme for sphingolipid biosynthesis, by affinity-peptide chromatography
Methods Mol. Biol.
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Cricetulus griseus
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Dobrzyn, A.; Dobrzyn, P.; Lee, S.; Miyazaki, M.; Cohen, P.; Asilmaz, E.; Hardie, D.G.; Friedman, J.M.; Ntambi, J.M.
Stearoyl-CoA desaturase-1 deficiency reduces ceramide synthesis by downregulating serine palmitoyltransferase and increasing beta-oxidation in skeletal muscle
Am. J. Physiol.
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Mus musculus
brenda
Hornemann, T.; Wei, Y.; von Eckardstein, A.
Is the mammalian serine-palmitoyltransferase a high molecular weight complex?
Biochem. J.
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2007
Homo sapiens
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Glaros, E.N.; Kim, W.S.; Wu, B.J.; Suarna, C.; Quinn, C.M.; Rye, K.A.; Stocker, R.; Jessup, W.; Garner, B.
Inhibition of atherosclerosis by the serine palmitoyl transferase inhibitor myriocin is associated with reduced plasma glycosphingolipid concentration
Biochem. Pharmacol.
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2007
Mus musculus
brenda
McCampbell, A.; Truong, D.; Broom, D.C.; Allchorne, A.; Gable, K.; Cutler, R.G.; Mattson, M.P.; Woolf, C.J.; Frosch, M.P.; Harmon, J.M.; Dunn, T.M.; Brown, R.H.
Mutant SPTLC1 dominantly inhibits serine palmitoyltransferase activity in vivo and confers an age-dependent neuropathy
Hum. Mol. Genet.
14
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2005
Cricetulus griseus, Homo sapiens
brenda
Hornemann, T.; Richard, S.; Ruetti, M.F.; Wei, Y.; von Eckardstein, A.
Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase
J. Biol. Chem.
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Homo sapiens
brenda
Han, G.; Gable, K.; Yan, L.; Allen, M.J.; Wilson, W.H.; Moitra, P.; Harmon, J.M.; Dunn, T.M.
Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera
J. Biol. Chem.
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39935-39942
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Coccolithovirus
brenda
He, X.; Guan, X.L.; Ong, W.Y.; Farooqui, A.A.; Wenk, M.R.
Expression, activity, and role of serine palmitoyltransferase in the rat hippocampus after kainate injury
J. Neurosci. Res.
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423-432
2007
Rattus norvegicus
brenda
Chen, M.; Han, G.; Dietrich, C.R.; Dunn, T.M.; Cahoon, E.B.
The essential nature of sphingolipids in plants as revealed by the functional identification and characterization of the Arabidopsis LCB1 subunit of serine palmitoyltransferase
Plant Cell
18
3576-3593
2006
Arabidopsis thaliana (Q9LSZ9), Arabidopsis thaliana
brenda
Baranowski, M.; Blachnio, A.; Zabielski, P.; Gorski, J.
Pioglitazone induces de novo ceramide synthesis in the rat heart
Prostaglandins Other Lipid Mediat.
83
99-111
2007
Rattus norvegicus
brenda
Ikushiro, H.; Islam, M.M.; Tojo, H.; Hayashi, H.
Molecular characterization of membrane-associated soluble serine palmitoyltransferases from Sphingobacterium multivorum and Bdellovibrio stolpii
J. Bacteriol.
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5749-5761
2007
Bacteriovorax stolpii (A7BFV8), Bacteriovorax stolpii, Sphingobacterium multivorum (A7BFV6), Sphingobacterium multivorum, Sphingobacterium spiritivorum (A7BFV7), Sphingobacterium spiritivorum
brenda
Ikushiro, H.; Fujii, S.; Shiraiwa, Y.; Hayashi, H.
Acceleration of the substrate Calpha deprotonation by an analogue of the second substrate palmitoyl-CoA in Serine Palmitoyltransferase
J. Biol. Chem.
283
7542-7553
2008
Sphingomonas paucimobilis (Q93UV0)
brenda
Hong, K.K.; Cho, H.R.; Ju, W.C.; Cho, Y.; Kim, N.I.
A study on altered expression of serine palmitoyltransferase and ceramidase in psoriatic skin lesion
J. Korean Med. Sci.
22
862-867
2007
Homo sapiens
brenda
Yard, B.A.; Carter, L.G.; Johnson, K.A.; Overton, I.M.; Dorward, M.; Liu, H.; McMahon, S.A.; Oke, M.; Puech, D.; Barton, G.J.; Naismith, J.H.; Campopiano, D.J.
The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis
J. Mol. Biol.
370
870-886
2007
Sphingomonas paucimobilis
brenda
Park, T.S.; Rosebury, W.; Kindt, E.K.; Kowala, M.C.; Panek, R.L.
Serine palmitoyltransferase inhibitor myriocin induces the regression of atherosclerotic plaques in hyperlipidemic ApoE-deficient mice
Pharmacol. Res.
58
45-51
2008
Mus musculus
brenda
Teng, C.; Dong, H.; Shi, L.; Deng, Y.; Mu, J.; Zhang, J.; Yang, X.; Zuo, J.
Serine palmitoyltransferase, a key enzyme for de novo synthesis of sphingolipids, is essential for male gametophyte development in Arabidopsis
Plant Physiol.
146
1322-1332
2008
Arabidopsis thaliana
brenda
Watson, M.L.; Coghlan, M.; Hundal, H.S.
Modulating serine palmitoyl transferase (SPT) expression and activity unveils a crucial role in lipid-induced insulin resistance in rat skeletal muscle cells
Biochem. J.
417
791-801
2009
Rattus norvegicus
brenda
Granado, M.H.; Gangoiti, P.; Ouro, A.; Arana, L.; Gomez-Munoz, A.
Ceramide 1-phosphate inhibits serine palmitoyltransferase and blocks apoptosis in alveolar macrophages
Biochim. Biophys. Acta
1791
263-272
2009
Rattus norvegicus
brenda
Wei, J.; Yerokun, T.; Leipelt, M.; Haynes, C.A.; Radhakrishna, H.; Momin, A.; Kelly, S.; Park, H.; Wang, E.; Carton, J.M.; Uhlinger, D.J.; Merrill, A.H.
Serine palmitoyltransferase subunit 1 is present in the endoplasmic reticulum, nucleus and focal adhesions, and functions in cell morphology
Biochim. Biophys. Acta
1791
746-756
2009
Homo sapiens (O15269)
brenda
Thuong, P.T.; Kang, K.W.; Kim, J.K.; Seo, D.B.; Lee, S.J.; Kim, S.H.; Oh, W.K.
Lithospermic acid derivatives from Lithospermum erythrorhizon increased expression of serine palmitoyltransferase in human HaCaT cells
Bioorg. Med. Chem. Lett.
19
1815-1817
2009
Homo sapiens
brenda
Ikushiro, H.; Islam, M.M.; Okamoto, A.; Hoseki, J.; Murakawa, T.; Fujii, S.; Miyahara, I.; Hayashi, H.
Structural insights into the enzymatic mechanism of serine palmitoyltransferase from Sphingobacterium multivorum
J. Biochem.
146
549-562
2009
Sphingobacterium multivorum (A7BFV6), Sphingobacterium multivorum, Sphingobacterium multivorum GTC97 (A7BFV6), Sphingobacterium multivorum GTC97
brenda
Shiraiwa, Y.; Ikushiro, H.; Hayashi, H.
Multifunctional role of His159in the catalytic reaction of serine palmitoyltransferase
J. Biol. Chem.
284
15487-15495
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Sphingomonas paucimobilis
brenda
Raman, M.C.; Johnson, K.A.; Yard, B.A.; Lowther, J.; Carter, L.G.; Naismith, J.H.; Campopiano, D.J.
The external aldimine form of serine palmitoyltransferase: structural, kinetic, and spectroscopic analysis of the wild-type enzyme and HSAN1 mutant mimics
J. Biol. Chem.
284
17328-17339
2009
Homo sapiens, Sphingomonas paucimobilis (Q93UV0), Sphingomonas paucimobilis, Sphingomonas paucimobilis EY2395 (Q93UV0)
brenda
Hornemann, T.; Penno, A.; Ruetti, M.F.; Ernst, D.; Kivrak-Pfiffner, F.; Rohrer, L.; von Eckardstein, A.
The SPTLC3 subunit of serine palmitoyltransferase generates short chain sphingoid bases
J. Biol. Chem.
284
26322-26330
2009
Homo sapiens
brenda
Ruetti, M.F.; Richard, S.; Penno, A.; von Eckardstein, A.; Hornemann, T.
An improved method to determine serine palmitoyltransferase activity
J. Lipid Res.
50
1237-1244
2009
Homo sapiens
brenda
Momin, A.A.; Park, H.; Allegood, J.C.; Leipelt, M.; Kelly, S.L.; Merrill, A.H.; Hanada, K.
Characterization of mutant serine palmitoyltransferase 1 in LY-B cells
Lipids
44
725-732
2009
Cricetulus griseus
brenda
Takahashi, Y.; Berberich, T.; Kanzaki, H.; Matsumura, H.; Saitoh, H.; Kusano, T.; Terauchi, R.
Serine palmitoyltransferase, the first step enzyme in sphingolipid biosynthesis, is involved in nonhost resistance
Mol. Plant Microbe Interact.
22
31-38
2009
Nicotiana benthamiana (B3Y000), Nicotiana benthamiana (B3Y9H2), Nicotiana benthamiana
brenda
Gan, Y.; Zhang, L.; Zhang, Z.; Dong, S.; Li, J.; Wang, Y.; Zheng, X.
The LCB2 subunit of the sphingolip biosynthesis enzyme serine palmitoyltransferase can function as an attenuator of the hypersensitive response and Bax-induced cell death
New Phytol.
181
127-146
2009
Brassica rapa subsp. oleifera (B5LED9), Arabidopsis thaliana (Q94IB8), Arabidopsis thaliana (Q9LSZ9)
brenda
Han, G.; Gupta, S.D.; Gable, K.; Niranjanakumari, S.; Moitra, P.; Eichler, F.; Brown, R.H.; Harmon, J.M.; Dunn, T.M.
Identification of small subunits of mammalian serine palmitoyltransferase that confer distinct acyl-CoA substrate specificities
Proc. Natl. Acad. Sci. USA
106
8186-8191
2009
Homo sapiens
brenda
Rotthier, A.; Auer-Grumbach, M.; Janssens, K.; Baets, J.; Penno, A.; Almeida-Souza, L.; Van Hoof, K.; Jacobs, A.; De Vriendt, E.; Schlotter-Weigel, B.; Loescher, W.; Vondracek, P.; Seeman, P.; De Jonghe, P.; Van Dijck, P.; Jordanova, A.; Hornemann, T.; Timmerman, V.
Mutations in the SPTLC2 subunit of serine palmitoyltransferase cause hereditary sensory and autonomic neuropathy type I
Am. J. Hum. Genet.
87
513-522
2010
Homo sapiens (O15270 and Q9NUV7), Homo sapiens
brenda
Altura, B.M.; Shah, N.C.; Li, Z.; Jiang, X.C.; Perez-Albela, J.L.; Altura, B.T.
Magnesium deficiency upregulates serine palmitoyl transferase (SPT 1 and SPT 2) in cardiovascular tissues: relationship to serum ionized Mg and cytochrome c
Am. J. Physiol. Heart Circ. Physiol.
299
H932-H938
2010
Rattus norvegicus
brenda
Raman, M.C.; Johnson, K.A.; Clarke, D.J.; Naismith, J.H.; Campopiano, D.J.
The serine palmitoyltransferase from Sphingomonas wittichii RW1: An interesting link to an unusual acyl carrier protein
Biopolymers
93
811-822
2010
Rhizorhabdus wittichii
brenda
Lowther, J.; Charmier, G.; Raman, M.C.; Ikushiro, H.; Hayashi, H.; Campopiano, D.J.
Role of a conserved arginine residue during catalysis in serine palmitoyltransferase
FEBS Lett.
585
1729-1734
2011
Rhizorhabdus wittichii
brenda
Rotthier, A.; Penno, A.; Rautenstrauss, B.; Auer-Grumbach, M.; Stettner, G.M.; Asselbergh, B.; Van Hoof, K.; Sticht, H.; Levy, N.; Timmerman, V.; Hornemann, T.; Janssens, K.
Characterization of two mutations in the SPTLC1 subunit of serine palmitoyltransferase associated with hereditary sensory and autonomic neuropathy type I
Hum. Mutat.
32
E2211-E2225
2011
Homo sapiens (O15269), Homo sapiens
brenda
Gable, K.; Gupta, S.D.; Han, G.; Niranjanakumari, S.; Harmon, J.M.; Dunn, T.M.
A disease-causing mutation in the active site of serine palmitoyltransferase causes catalytic promiscuity
J. Biol. Chem.
285
22846-22852
2010
Homo sapiens
brenda
Lowther, J.; Yard, B.A.; Johnson, K.A.; Carter, L.G.; Bhat, V.T.; Raman, M.C.; Clarke, D.J.; Ramakers, B.; McMahon, S.A.; Naismith, J.H.; Campopiano, D.J.
Inhibition of the PLP-dependent enzyme serine palmitoyltransferase by cycloserine: evidence for a novel decarboxylative mechanism of inactivation
Mol. Biosyst.
6
1682-1693
2010
Sphingomonas paucimobilis (Q93UV0), Sphingomonas paucimobilis
brenda
Beattie, A.E.; Gupta, S.D.; Frankova, L.; Kazlauskaite, A.; Harmon, J.M.; Dunn, T.M.; Campopiano, D.J.
The pyridoxal 5'-phosphate (PLP)-dependent enzyme serine palmitoyltransferase (SPT): effects of the small subunits and insights from bacterial mimics of human hLCB2a HSAN1 mutations
BioMed Res. Int.
2013
194371
2013
Homo sapiens (O15269 and O15270), Homo sapiens, Sphingomonas paucimobilis (Q93UV0), Sphingomonas paucimobilis
brenda
Beattie, A.E.; Clarke, D.J.; Wadsworth, J.M.; Lowther, J.; Sin, H.L.; Campopiano, D.J.
Reconstitution of the pyridoxal 5-phosphate (PLP) dependent enzyme serine palmitoyltransferase (SPT) with pyridoxal reveals a crucial role for the phosphate during catalysis
Chem. Commun. (Camb. )
49
7058-7060
2013
Sphingomonas paucimobilis (Q93UV0)
brenda
Hirata, Y.; Yamamori, N.; Kono, N.; Lee, H.C.; Inoue, T.; Arai, H.
Identification of small subunit of serine palmitoyltransferase a as a lysophosphatidylinositol acyltransferase 1-interacting protein
Genes Cells
18
397-409
2013
Homo sapiens (Q969W0)
brenda
Bode, H.; Bourquin, F.; Suriyanarayanan, S.; Wei, Y.; Alecu, I.; Othman, A.; Von Eckardstein, A.; Hornemann, T.
HSAN1 mutations in serine palmitoyltransferase reveal a close structure-function-phenotype relationship
Hum. Mol. Genet.
25
853-865
2016
Homo sapiens (O15269 and O15270), Homo sapiens
brenda
Wadsworth, J.M.; Clarke, D.J.; McMahon, S.A.; Lowther, J.P.; Beattie, A.E.; Langridge-Smith, P.R.; Broughton, H.B.; Dunn, T.M.; Naismith, J.H.; Campopiano, D.J.
The chemical basis of serine palmitoyltransferase inhibition by myriocin
J. Am. Chem. Soc.
135
14276-14285
2013
Sphingomonas paucimobilis (Q93UV0)
brenda
Harmon, J.M.; Bacikova, D.; Gable, K.; Gupta, S.D.; Han, G.; Sengupta, N.; Somashekarappa, N.; Dunn, T.M.
Topological and functional characterization of the ssSPTs, small activating subunits of serine palmitoyltransferase
J. Biol. Chem.
288
10144-10153
2013
Homo sapiens
brenda
Taouji, S.; Higa, A.; Delom, F.; Palcy, S.; Mahon, F.X.; Pasquet, J.M.; Bosse, R.; Segui, B.; Chevet, E.
Phosphorylation of serine palmitoyltransferase long chain-1 (SPTLC1) on tyrosine 164 inhibits its activity and promotes cell survival
J. Biol. Chem.
288
17190-17201
2013
Canis lupus familiaris (E2RKV3), Canis lupus familiaris, Homo sapiens (O15269), Homo sapiens
brenda
Chakraborty, M.; Lou, C.; Huan, C.; Kuo, M.S.; Park, T.S.; Cao, G.; Jiang, X.C.
Myeloid cell-specific serine palmitoyltransferase subunit 2 haploinsufficiency reduces murine atherosclerosis
J. Clin. Invest.
123
1784-1797
2013
Mus musculus (P97363), Mus musculus
brenda
Liu, L.; Martin, R.; Chan, C.
Palmitate-activated astrocytes via serine palmitoyltransferase increase BACE1 in primary neurons by sphingomyelinases
Neurobiol. Aging
34
540-550
2013
Rattus norvegicus, Rattus norvegicus Sprague Dawley
brenda
Ernst, D.; Murphy, S.M.; Sathiyanadan, K.; Wei, Y.; Othman, A.; Laura, M.; Liu, Y.T.; Penno, A.; Blake, J.; Donaghy, M.; Houlden, H.; Reilly, M.M.; Hornemann, T.
Novel HSAN1 mutation in serine palmitoyltransferase resides at a putative phosphorylation site that is involved in regulating substrate specificity
Neuromolecular Med.
17
47-57
2015
Homo sapiens (O15270), Homo sapiens
brenda
Kimberlin, A.N.; Majumder, S.; Han, G.; Chen, M.; Cahoon, R.E.; Stone, J.M.; Dunn, T.M.; Cahoon, E.B.
Arabidopsis 56-amino acid serine palmitoyltransferase-interacting proteins stimulate sphingolipid synthesis, are essential, and affect mycotoxin sensitivity
Plant Cell
25
4627-4639
2013
Arabidopsis thaliana
brenda
Miklosz, A.; Lukaszuk, B.; Baranowski, M.; Gorski, J.; Chabowski, A.
Effects of inhibition of serine palmitoyltransferase (SPT) and sphingosine kinase 1 (SphK1) on palmitate induced insulin resistance in L6 myotubes
PLoS ONE
8
e85547
2013
Rattus norvegicus
brenda
Adachi, R.; Asano, Y.; Ogawa, K.; Oonishi, M.; Tanaka, Y.; Kawamoto, T.
Pharmacological characterization of synthetic serine palmitoyltransferase inhibitors by biochemical and cellular analyses
Biochem. Biophys. Res. Commun.
497
1171-1176
2018
Homo sapiens (O15269 AND O15270 AND Q9NUV7), Homo sapiens
brenda
Han, G.; Gupta, S.D.; Gable, K.; Bacikova, D.; Sengupta, N.; Somashekarappa, N.; Proia, R.L.; Harmon, J.M.; Dunn, T.M.
The ORMs interact with transmembrane domain 1 of Lcb1 and regulate serine palmitoyltransferase oligomerization, activity and localization
Biochim. Biophys. Acta
1864
245-259
2019
Saccharomyces cerevisiae
brenda
Choe, H.; Cha, M.; Stewart, J.
Semi-rational approach to expand the acyl-CoA chain length tolerance of Sphingomonas paucimobilis serine palmitoyltransferase
Enzyme Microb. Technol.
137
109515
2020
Sphingomonas paucimobilis (Q93UV0), Sphingomonas paucimobilis
brenda
Harrison, P.J.; Gable, K.; Somashekarappa, N.; Kelly, V.; Clarke, D.J.; Naismith, J.H.; Dunn, T.M.; Campopiano, D.J.
Use of isotopically labeled substrates reveals kinetic differences between human and bacterial serine palmitoyltransferase
J. Lipid Res.
60
953-962
2019
Homo sapiens (O15269 AND O15270 AND Q969W0), Homo sapiens, Sphingomonas paucimobilis
brenda
Davis, D.L.; Mahawar, U.; Pope, V.S.; Allegood, J.; Sato-Bigbee, C.; Wattenberg, B.W.
Dynamics of sphingolipids and the serine palmitoyltransferase complex in rat oligodendrocytes during myelination
J. Lipid Res.
61
505-522
2020
Rattus norvegicus (D4A2H2 AND Q3B7D2)
brenda
Li, J.; Yin, J.; Rong, C.; Li, K.E.; Wu, J.X.; Huang, L.Q.; Zeng, H.Y.; Sahu, S.K.; Yao, N.
Orosomucoid proteins interact with the small subunit of serine palmitoyltransferase and contribute to sphingolipid homeostasis and stress responses in Arabidopsis
Plant Cell
28
3038-3051
2016
Arabidopsis thaliana
brenda
Ziv, C.; Malitsky, S.; Othman, A.; Ben-Dor, S.; Wei, Y.; Zheng, S.; Aharoni, A.; Hornemann, T.; Vardi, A.
Viral serine palmitoyltransferase induces metabolic switch in sphingolipid biosynthesis and is required for infection of a marine alga
Proc. Natl. Acad. Sci. USA
113
E1907-E1916
2016
Emiliania huxleyi, Emiliania huxleyi virus sp., Emiliania huxleyi virus sp. 201, Emiliania huxleyi CCMP374
brenda