Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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 DunathanĀs 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 CaĀH 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/SchiffĀs 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 CaĀH 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
-
-
-
-
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.
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.
acyl-CoA + L-serine
CoA + ?
-
Substrates: -
Products: -
?
arachidoyl-CoA + L-serine
CoA + 2-amino-1-hydroxydocosan-3-one + CO2
-
Substrates: 37% activity compared to that with palmitoyl-CoA
Products: -
?
caproyl-CoA + L-serine
?
Substrates: very low activity
Products: -
?
elaidoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-trans-11-eicosen-3-one + CO2
-
Substrates: 39% activity compared to that with palmitoyl-CoA
Products: -
?
heptadecanoyl-CoA + L-serine
?
L-alanine + palmitoyl-CoA
CoA + (2S)-2-aminooctadecan-3-one + CO2
-
Substrates: -
Products: -
?
L-alanine + stearoyl-CoA
CoA + (2S)-2-aminoicosan-3-one + CO2
-
Substrates: -
Products: -
?
L-serine + palmitoyl-CoA
CoA + 3-dehydro-D-sphinganine + CO2
L-serine + stearoyl-CoA
CoA + (2S)-2-amino-1-hydroxyicosan-3-one + CO2
-
Substrates: -
Products: -
?
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
-
Substrates: 46% activity compared to that with palmitoyl-CoA
Products: -
?
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
-
Substrates: 57% activity compared to that with palmitoyl-CoA
Products: -
?
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
-
Substrates: -
Products: -
?
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
-
Substrates: -
Products: -
?
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
-
Substrates: 51% activity compared to that with palmitoyl-CoA
Products: -
?
additional information
?
-
heptadecanoyl-CoA + L-serine
?
-
Substrates: -
Products: -
?
heptadecanoyl-CoA + L-serine
?
-
Substrates: -
Products: -
?
heptadecanoyl-CoA + L-serine
?
-
Substrates: less than 50% activity compared to palmitoyl-CoA
Products: -
?
heptadecanoyl-CoA + L-serine
?
-
Substrates: less than 50% activity compared to palmitoyl-CoA
Products: -
?
L-serine + palmitoyl-CoA
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
L-serine + palmitoyl-CoA
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
L-serine + palmitoyl-CoA
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
lauroyl-CoA + L-serine
CoA + 2-amino-1-hydroxytetradecan-3-one + CO2
-
Substrates: 18% activity compared to that with palmitoyl-CoA
Products: -
?
lauroyl-CoA + L-serine
CoA + 2-amino-1-hydroxytetradecan-3-one + CO2
Substrates: 18% activity compared to palmitoyl-CoA
Products: -
?
myristoyl-CoA + L-serine
?
-
Substrates: -
Products: -
?
myristoyl-CoA + L-serine
?
-
Substrates: -
Products: -
?
myristoyl-CoA + L-serine
?
-
Substrates: less than 50% activity compared to palmitoyl-CoA
Products: -
?
myristoyl-CoA + L-serine
?
-
Substrates: less than 50% activity compared to palmitoyl-CoA
Products: -
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
Substrates: SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis
Products: -
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
Substrates: the viral enzyme exhibits preference for myristoyl-CoA rather than palmitoyl-CoA
Products: -
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
Substrates: -
Products: -
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
Substrates: second best substrate
Products: -
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
Substrates: 75% activity compared to that with palmitoyl-CoA
Products: -
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
Substrates: 75% activity compared to that with palmitoyl-CoA
Products: -
?
myristoyl-CoA + L-serine
CoA + ? + CO2
-
Substrates: -
Products: -
?
myristoyl-CoA + L-serine
CoA + ? + CO2
-
Substrates: recombinant SPTLC3 subunit in HEK-293 cells
Products: -
?
n-heptadecanoyl-CoA + L-serine
CoA + 2-amino-1-hydroxynonadecan-3-one + CO2
-
Substrates: 75% activity compared to that with palmitoyl-CoA
Products: -
?
n-heptadecanoyl-CoA + L-serine
CoA + 2-amino-1-hydroxynonadecan-3-one + CO2
-
Substrates: 75% activity compared to that with palmitoyl-CoA
Products: -
?
palmitoleoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-cis-11-octadecen-3-one + CO2
-
Substrates: 80% activity compared to that with palmitoyl-CoA
Products: -
?
palmitoleoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-cis-11-octadecen-3-one + CO2
-
Substrates: 80% activity compared to that with palmitoyl-CoA
Products: -
?
palmitoyl-CoA + L-alanine
CoA + (2S)-2-aminooctadecan-3-one + CO2
Substrates: wild-type enzyme can metabolize L-alanine under certain conditions
Products: -
?
palmitoyl-CoA + L-alanine
CoA + (2S)-2-aminooctadecan-3-one + CO2
Substrates: low activity with the wild-type enzyme, but increased activity with some mutants of the enzyme, overview
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: step in the sphingolipid biosynthetic pathway, overview
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
E2RKV3
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: the viral enzyme exhibits preference for myristoyl-CoA rather than palmitoyl-CoA
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: first step of biosynthesis of sphingolipid bases
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: key enzyme of sphingolipid metabolism
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: palmitoyl-CoA is the preferred substrate
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: optimal palmitoyl-CoA concentration is 0.2 mM
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: palmitoyl-CoA is used in preference to other saturated or unsaturated acyl-CoA substrates
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: 100% activity
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: 100% activity
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: palmitoyl-CoA is used in preference to other saturated or unsaturated acyl-CoA substrates
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: involved in cellular stress response
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: first step of biosynthesis of sphingolipid bases
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: first step of biosynthesis of sphingolipid bases
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: first step of biosynthesis of sphingolipid bases
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: rate-limiting enzyme in synthesis of sphingolipids
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: rate-limiting enzyme in synthesis of sphingolipids
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: rate-limiting enzyme in synthesis of sphingolipids
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: initial step of de novo ceramide biosynthesis
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: initial step of de novo ceramide biosynthesis
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: 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
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: 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
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: first and rate-limiting step in the de novo synthesis of sphingolipids
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: first step of biosynthesis of sphingolipid bases
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: key enzyme in ceramide synthesis, overview
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: initial step of de novo ceramide biosynthesis
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: i.e. 2-amino-1-hydroxyoctadecane-3-one, i.e. 3-oxo-dihydroxysphingosine
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: palmitoyl-CoA is the preferred substrate
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: palmitoyl-CoA is the preferred substrate
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: 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
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: no other amino acids can substitute for serine
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: first step of biosynthesis of sphingolipid bases
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: first step of biosynthesis of sphingolipid bases
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: initial step of de novo ceramide biosynthesis
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: the enzyme catalyses the first step in the ceramide biosynthesis pathway
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: the enzyme is involved in the ceramide metabolism, overview
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: involved in cellular stress response
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: first step of biosynthesis of sphingolipid bases
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: rate-limiting enzyme in synthesis of sphingolipids
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: initial step of de novo ceramide biosynthesis
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: initial step of de novo ceramide biosynthesis
Products: -
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
Substrates: -
Products: -
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
show
top
