2.3.1.50: serine C-palmitoyltransferase
This is an abbreviated version!
For detailed information about serine C-palmitoyltransferase, go to the full flat file.
Word Map on EC 2.3.1.50
-
2.3.1.50
-
sphingolipids
-
ceramide
-
myriocin
-
sphingomyelin
-
sphingosine
-
sphingomyelinase
-
neuropathy
-
sphingoid
-
cholesterol
-
fumonisin
-
glucosylceramide
-
sphingosine-1-phosphate
-
3-ketodihydrosphingosine
-
corneum
-
glycosphingolipids
-
dihydroceramide
-
dihydrosphingosine
-
plp-dependent
-
l-cycloserine
-
ormdl3
-
molecular biology
-
sphingomonas
-
paucimobilis
-
transepidermal
-
charcot-marie-tooth
-
analysis
-
ceramide-induced
-
phytosphingosine
-
medicine
-
asmase
-
aldimine
- 2.3.1.50
- sphingolipids
- ceramide
- myriocin
- sphingomyelin
- sphingosine
- sphingomyelinase
- neuropathy
-
sphingoid
- cholesterol
- fumonisin
- glucosylceramide
- sphingosine-1-phosphate
- 3-ketodihydrosphingosine
- corneum
- glycosphingolipids
- dihydroceramide
- dihydrosphingosine
-
plp-dependent
- l-cycloserine
-
ormdl3
- molecular biology
- sphingomonas
- paucimobilis
-
transepidermal
-
charcot-marie-tooth
- analysis
-
ceramide-induced
- phytosphingosine
- medicine
- asmase
-
aldimine
Reaction
Synonyms
3-oxosphinganine synthetase, acyl-CoA:serine C-2 acyltransferase decarboxylating, LCB1, LCB2, LCB2a, LCB2b, More, palmitoyltransferase, serine, serine palmitoyl transferase, serine palmitoyltransferase, serine palmitoyltransferase 1, serine palmitoyltransferase a, serine-palmitoyl transferase, serine-palmitoyltransferase, SPT, SPT1, SPT2, SPT3, SPTase, SPTLC1, SPTLC2, ssSPT, ssSPTa, Tsc3
ECTree
2.3.1.50 serine C-palmitoyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.3.1.50 - serine C-palmitoyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K311E
construction of mutant BcLCB2DELTAK311E that shows reduced activity compared to the wild-type enzyme
C133W
-
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
C133W
C133Y
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
G382V
I504F
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
S331F
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
S384F
V359M
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
H159F
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
R378N
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
-
additional information
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
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
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
