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palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2

mechanism
-
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
mechanism
-
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
mechanism
-
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
ordered bi-bi mechanism
-
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
formation of the external aldimine intermediate
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
using 1HNMR the exchange of the alpha-proton of L-serine with the solvent in the presence and absence of S-(2- oxoheptadecyl)-CoA, the structural analogue of palmitoyl-CoA is investagated. Results demonstrate the presence of substrate synergism, in which the alpha-proton of L-serine is activated by the binding of the second substrate palmitoyl-CoA
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the enzyme forms a pyridoxal 5'-phosphate-L-serine-aldimine intermediate during the reaction, His159 plays multiple roles in the reaction mechanism by exploiting the stereochemistry of DunathanĆ¢ĀĀs conjecture. His159 promotes both the Claisen-type condensation as an acid catalyst and the protonation at Calpha of the second quinonoid to form the pyridoxal 5'-phosphate-KDS aldimine, spectral analysis, overview
-
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the enzyme forms an external aldimine intermediate, as well as dunathan and quinoid intermediates, and followed by external beta-keto acid intermediate, and finally product quinoid and product external aldimine intermediates, reaction cycle, overview
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the enzyme forms an external aldimine intermediate, as well as dunathan and quinoid intermediates, followed by external beta-keto acid intermediate, and finally product quinoid and product external aldimine intermediates, reaction cycle, overview
-
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
via reaction intermediate pyridoxal 5'-phosphate-L-serine aldimine, His138 changes its hydrogen bond partner from the carboxyl group of L-serine to the carbonyl group of palmitoyl-CoA upon the binding of palmitoyl-CoA, making the L-serine CaĆ¢ĀĀH bond perpendicular to the pyridoxal 5'-phosphate-Schiff base plane, reaction mechanism with substrate synergism in the SPT reaction, overview. Modelling of reaction intermediates
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
pyridoxal 5'-phosphate dependent reaction mechanism, key active site residues are His159, Asp231, His234, and Lys265
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the reaction proceeds via a key carbanion/quinonoid species and an internal aldimine/PLP-bound form of the enzyme
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the reaction proceeds via a key carbanion/quinonoid species and an internal aldimine/PLP-bound form of the enzyme
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the reaction proceeds via several intermediate states, the pyridoxal 5'-phosphate cofactor binds to an active site lysine residue as an internal aldimine/SchiffĆ¢ĀĀs base (I). The L-serine displaces the lysine residue (Lys265) to form the PLP-L-serine external aldimine (II). Deprotonation of II gives a carbanion/quinonoid species (III) which condenses in a Claisen-like manner with the acyl-CoA thioester substrate to form a PLP-beta-keto acid, which then decarboxylates to generate the PLP-KDS product quinonoid (IV). This then reprotonates to form PLP-KDS aldimine (V) which is finally displaced by Lys265. The step releasing CoA and CO2 and producing the quinonoid intermediate species is irreversible. Interaction between the hydroxyl group of the L-serine substrate and the 5'-phosphate group of pyridoxal 5'-phosphate occurs in the formation of the external aldimine II, overview
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
via reaction intermediate pyridoxal 5'-phosphate-L-serine aldimine, His138 changes its hydrogen bond partner from the carboxyl group of L-serine to the carbonyl group of palmitoyl-CoA upon the binding of palmitoyl-CoA, making the L-serine CaĆ¢ĀĀH bond perpendicular to the pyridoxal 5'-phosphate-Schiff base plane, reaction mechanism with substrate synergism in the SPT reaction, overview. Modelling of reaction intermediates
-
-
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
ordered bi-bi mechanism
-
-
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the enzyme forms an external aldimine intermediate, as well as dunathan and quinoid intermediates, and followed by external beta-keto acid intermediate, and finally product quinoid and product external aldimine intermediates, reaction cycle, overview
-
-
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
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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-hydroxy-cis-11-hexadecen-3-one + CO2
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
-
-
-
-
?
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
-
-
-
-
?
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-hydroxy-cis-11-hexadecen-3-one + CO2
-
SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis
-
-
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-cis-11-hexadecen-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
-
-
-
?
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-hydroxy-cis-11-hexadecen-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
-
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S,3R)-2-amino-12-hydroxy-2-hydroxymethyl-3-sulfooxy-octadecanoic acid
-
IC50: 5.4 nM
(2S,3R)-2-amino-12-[(Z)-hydroxyimino]-2-hydroxymethyl-3-sulfooxy-octadecanoic acid
-
IC50: 30 nM
(2S,3R)-2-amino-3,12-dihydroxy-2-hydroxymethyl-octadecanoic acid
-
IC50: 3.2 nM
(2S,3R)-2-amino-3-hydroxy-2-hydroxymethyl-12-oxo-octadecanoic acid
-
IC50: 3.5 nM
(2S,3R)-2-amino-3-hydroxy-2-hydroxymethyl-12-oxo-octadecanoic acid methyl ester
-
IC50: 17 nM
2-chloro-N-[(7S)-4-(3,4-dimethoxybenzoyl)-1-(propan-2-yl)-4,5,6,7-tetrahydro-1H-pyrazolo[4,3-b]pyridin-7-yl]benzamide
-
3-hydroxypropionate
-
competitive to L-serine
4-amino-3-isoxazolidone
D-cycloserine and L-cycloserine are inhibitors, L-cycloserine is 14-fold more effective than D-cycloserine
alpha-methyl-DL-serine
-
competitive to L-serine
ceramide 1-phosphate
-
from bovine brain, inhibits the enzyme and blocks apoptosis in alveolar macrophages, overview
cis-4-methylsphingosine
-
time- and concentration-dependent, causes drastic morphological changes of the cells in vivo
cis-5-methylsphingosine
-
weak inhibition
cis-sphingosine
-
weak inhibition
cysteine
-
competitive to L-serine
L-alanine
-
inhibition of serine utilization
mycotoxin fumonisin B1
-
enzyme sensitivity to the inhibitor is increased by small subunit ssSPTa overexpression
N-[(7S)-4-(5,6-dimethoxypyridine-3-carbonyl)-1-(propan-2-yl)-4,5,6,7-tetrahydro-1H-pyrazolo[4,3-b]pyridin-7-yl]-2-(trifluoromethoxy)benzamide
-
O-phosphoserine
-
competitive to L-serine
palmitoyl CoA
enzyme shows remarkable substrate inhibition at palmitoyl-CoA concentrations higher than 0.1 nM
serine methylester
-
competitive to L-serine
sulfamisterin
-
antibiotic derived from Pycnidiella sp., IC50: 3 nM
thermozymocidin
-
i.e. ISP-1; strong inhibition, reversible by sphingosine
threonine
-
competitive to L-serine
trans-4-methylsphingosine
-
-
trans-5-methylsphingosine
-
weak inhibition
[N-[(7S)-4-(3,4-dimethoxybenzoyl)-1-[5-(3-[2-[(3,5-dimethyl-1H-pyrrol-2-yl-kappaN)methylidene]-2H-pyrrol-5-yl-kappaN]propanamido)pentyl]-4,5,6,7-tetrahydro-1H-pyrazolo[4,3-b]pyridin-7-yl]-2-(trifluoromethoxy)benzamidato](difluorido)boron
-
beta-chloro-L-alanine

-
in vivo, time dependent
beta-chloro-L-alanine
-
cytotoxic, irreversible
beta-chloro-L-alanine
-
mechanism-based inhibition
beta-chloro-L-alanine
-
-
beta-chloro-L-alanine
-
-
beta-chloro-L-alanine
-
rapid, irreversible and time dependent inhibition at the active site; stereospecific, no inhibition by beta-chloro-D-alanine; suicide substrate
beta-chloro-L-alanine
-
-
beta-chloro-L-alanine
-
irreversible
L-Cycloserine

-
cytotoxic, irreversible
L-Cycloserine
-
mechanism-based inhibition
L-Cycloserine
-
irreversible
lipoxamycin

-
-
myriocin

a potent inhibitor of SPT, that has no effect on Bax-induced programmed cell death
myriocin
-
i.e. sphingofungin B; strong inhibition, reversible by sphingosine
myriocin
-
in vivo intraperitoneal application to apolipoprotein E knockout mice leads to inhibition of atherosclerosis while feeding a high fat diet to the mice, and is associated with reduced plasma glycosphingolipid concentration and reduction of lesions in aorta regions, overview
myriocin
-
the inhibition of SPT in hyperlipidemic apolipoprotein E knockout mice lowers plasma sphingolipids and atherogenic plasma lipids leading to the regression of pre-existing atherosclerotic lesions and to the formation of a stable plaque phenotype
myriocin
inhibits the enzyme and inhibits defense response against a nonhost pathogen; inhibits the enzyme and inhibits defense response against a nonhost pathogen
myriocin
-
an SPT inhibitor
myriocin
-
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
myriocin
i.e. (2S,3R,4R,6E)-2-amino-3,4-dihydroxy-2-(hydroxymethyl)-14-oxo-6-eicosenoic acid, or thermozymocidin and ISP-1, is a fungal natural product, kinetics and molecular mechanism of enzyme inhibition, overview. Myriocin is a potent SPT enzyme inhibitor. It initially forms an external aldimine with pyridoxal 5'-phosphate at the active site, the structure of the resulting co-complex explains its nanomolar affinity for the enzyme. The cofactor-inhibitor co-complex, PLP-myriocin aldimine, catalytically degrades via an unexpected retro-aldol-like cleavage mechanism to a C18 aldehyde which in turn acts as a suicide inhibitor of the enzyme by covalent modification of the essential catalytic lysine. This dual mechanism of inhibition rationalizes the extraordinary potency and longevity of myriocin inhibition. Incubations of enzyme SPT with myriocin is consistent with the formation of an initial enzyme-inhibitor complex which is noncovalent in nature and reversible, albeit with a very slow off rate (koff), the PLP-myriocin aldimine as the initial competitive inhibitory species. In contrast, for the enzyme preincubated with myriocin for 16 h, no detectable regain in activity is observed after dialysis either at 3 or 24 h, the second formed covalent adduct acts as an irreversible inhibitor of enzyme SPT
palmitoyl-CoA

-
causes substrate inhibition at higher concentrations
palmitoyl-CoA
-
0.5-1.0 mM, substrate inhibition
palmitoyl-CoA
-
no inhibition at concentrations up to 10 mM
additional information

-
orosomucoid proteins ORM1 and ORM2 inhibit the function of the small subunit ssSP and thus negatively regulate enzyme activity
-
additional information
-
recombinant expression of C133W mutant SPTLC1 in cell cultures dominantly inhibits the endogenous SPT activity
-
additional information
-
time-dependent degradation of enzyme mRNA by etoposide, activation of enzyme activity on protein level, time-dependent; time-dependent degradation of enzyme mRNA by etoposide, activation of enzyme activity on protein level, time-dependent
-
additional information
time-dependent degradation of enzyme mRNA by etoposide, activation of enzyme activity on protein level, time-dependent; time-dependent degradation of enzyme mRNA by etoposide, activation of enzyme activity on protein level, time-dependent
-
additional information
time-dependent degradation of enzyme mRNA by etoposide, activation of enzyme activity on protein level, time-dependent; time-dependent degradation of enzyme mRNA by etoposide, activation of enzyme activity on protein level, time-dependent
-
additional information
-
no inhibition by sucrose monolaurate
-
additional information
-
the enzyme activity and expression in the heart is not affected by high-fat feeding
-
additional information
-
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
-
additional information
-
not inhibited by halide ions
-
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9.6
L-alanine
-
C133W mutant protein, pH not specified in the publication, temperature not specified in the publication
0.03 - 0.097
myristoyl-CoA
0.019 - 1.2
palmitoyl-CoA
0.0129
stearoyl-CoA
-
pH not specified in the publication, temperature not specified in the publication
1.79
[1,2,3-13C,2-15N] L-serine
-
at pH 8.1 and 37ưC
4.09
[2,3,3-D] L-serine
-
at pH 8.1 and 37ưC
3.64
[2-13C] L-serine
-
at pH 8.1 and 37ưC
2.72
[3,3-D] L-serine
-
at pH 8.1 and 37ưC
additional information
L-alanine
0.68
caproyl-CoA

wild type enzyme, at pH 7.5 and 25ưC
0.9
caproyl-CoA
mutant enzyme R378K, at pH 7.5 and 25ưC
0.1 - 1
L-serine

-
-
0.75
L-serine
-
wild type protein, pH not specified in the publication, temperature not specified in the publication
0.78
L-serine
-
pH not specified in the publication, temperature not specified in the publication
1.2
L-serine
-
pH 8.0, 37ưC, microsomes
1.4
L-serine
pH 7.5, 37ưC, recombinant wild-type enzyme
1.4
L-serine
-
C133W mutant protein, pH not specified in the publication, temperature not specified in the publication
1.56
L-serine
-
at pH 8.1 and 37ưC
1.6
L-serine
recombinant wild-type enzyme, pH 7.5, 25ưC
1.6
L-serine
pH 7.5, 37ưC, recombinant mutant N100W
2.4
L-serine
pH 7.5, 37ưC, recombinant mutant R378N
2.5
L-serine
pH 7.5, 37ưC, recombinant mutant N100Y
2.5
L-serine
recombinant mutant V246M, pH 7.5, 25ưC
3
L-serine
recombinant mutant G385F, pH 7.5, 25ưC
3.5
L-serine
mutant DELTA2-9SPT
3.8
L-serine
pH 7.5, 37ưC, recombinant mutant R378A
4.2
L-serine
-
native enzyme
5.6
L-serine
mutant enzyme R378K, with palmitoyl-CoA as cosubstrate, at pH 7.5 and 25ưC
7
L-serine
pH 7.5, 37ưC, recombinant mutant N100C
7.2
L-serine
wild type enzyme, with palmitoyl-CoA as cosubstrate, at pH 7.5 and 25ưC
10.6
L-serine
-
recombinant enzyme
0.25
lauroyl-CoA

wild type enzyme, at pH 7.5 and 25ưC
0.56
lauroyl-CoA
mutant enzyme R378K, at pH 7.5 and 25ưC
0.03
myristoyl-CoA

-
pH 8.0, 37ưC, recombinant SPTLC3
0.08
myristoyl-CoA
wild type enzyme, at pH 7.5 and 25ưC
0.097
myristoyl-CoA
mutant enzyme R378K, at pH 7.5 and 25ưC
0.019
palmitoyl-CoA

pH 7.5, 37ưC, recombinant mutant N100W
0.0234
palmitoyl-CoA
-
pH not specified in the publication, temperature not specified in the publication
0.024
palmitoyl-CoA
mutant enzyme R378K, at pH 7.5 and 25ưC
0.031
palmitoyl-CoA
pH 7.5, 37ưC, recombinant mutant N100Y
0.031
palmitoyl-CoA
pH 7.5, 37ưC, recombinant mutant R378N
0.035
palmitoyl-CoA
pH 7.5, 37ưC, recombinant wild-type enzyme
0.0356
palmitoyl-CoA
recombinant wild-type enzyme, pH 7.5, 25ưC
0.039
palmitoyl-CoA
pH 7.5, 37ưC, recombinant mutant R378A
0.04
palmitoyl-CoA
-
pH 8.0, 37ưC, recombinant SPTLC3
0.041
palmitoyl-CoA
wild type enzyme, at pH 7.5 and 25ưC
0.0522
palmitoyl-CoA
recombinant mutant G385F, pH 7.5, 25ưC
0.06
palmitoyl-CoA
pH 7.5, 37ưC, recombinant mutant N100C
0.128
palmitoyl-CoA
recombinant mutant V246M, pH 7.5, 25ưC
0.87
palmitoyl-CoA
-
native and recombinant enzyme
1
palmitoyl-CoA
wild-type
1.2
palmitoyl-CoA
mutant DELTA2-9SPT
additional information
L-alanine

-
wild-type enzyme does not utilize alanine efficiently
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetics analysis, detailed overview
-
additional information
additional information
-
kinetics of the recombinant SPTLC3 subunit in HEK-293 cells, overview
-
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzyme
-
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics.The regenerated enzyme displays similar Km and kcat values to the purified enzyme, with only a small increase in the Km for L-serine
-
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