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Information on EC 2.3.1.50 - serine C-palmitoyltransferase and Organism(s) Homo sapiens
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2.3.1.50 serine C-palmitoyltransferaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 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
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
serine palmitoyltransferase, sptlc1, sptlc2, serine palmitoyl transferase, ssspta, serine-palmitoyltransferase, serine-palmitoyl transferase, serine palmitoyltransferase a, ssspt, lcb2a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-oxosphinganine synthetase
-
-
-
-
acyl-CoA:serine C-2 acyltransferase decarboxylating
-
-
-
-
palmitoyltransferase, serine
-
-
-
-
serine palmitoyltransferase
serine-palmitoyltransferase
SPT
serine palmitoyltransferase
-
-
-
-
serine palmitoyltransferase
-
-
serine-palmitoyltransferase
-
-
-
-
SPT
-
-
-
-
SPT
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
the reaction proceeds via a key carbanion/quinonoid species and an internal aldimine/PLP-bound form of the enzyme
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
palmitoyl-CoA:L-serine C-palmitoyltransferase (decarboxylating)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
62213-50-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-serine + stearoyl-CoA
CoA + (2S)-2-amino-1-hydroxyicosan-3-one + CO2
-
-
-
-
?
stearoyl-CoA + L-serine
CoA + (2S)-2-amino-1-hydroxyicosan-3-one + CO2
-
-
-
-
?
L-serine + palmitoyl-CoA
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
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-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
-
-
-
?
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 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
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
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
-
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
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
all subunits contain a pyridoxal 5'-phosphate consensus motif sequence
pyridoxal 5'-phosphate
dependent on, bound by lysine 265 residue on subunit LCB2a
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
-
[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
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
small activating subunit of serine palmitoyltransferase
-
ssSPT, the small subunits of human serine palmitoyltransferase (hssSPTs) are glycoproteins and activate the catalytic hLCB1/hLCB2 heterodimer. Two isoforms exist, ssSPTa and ssSPTb, a single amino acid, residue 25, difference between ssSPTa and ssSPTb is responsible for the acyl-CoA preference of heterotrimers containing each isoform. the role of the small activating subunits of serine palmitoyltransferase, ssSPTs, is to increase SPT activity without compromising substrate specificity. Activity and acyl-CoA selectivity of the ssSPTs reside in the conserved core. 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. The region responsible for the acyl-CoA selectivity of ssSPTa lays between residues Ser11 and Glu27, the acyl-CoA selectivity does not lie in the C-terminal region of ssSPTb, overview
-
small subunits of serine palmitoyltransferase
small subunits of SPT, ssSPTa and ssSPTb, increase human SPT activity by 50-100fold when coexpressed with enzyme subunits hLCB1 and hLCBa
-
additional information
-
enzyme activity is enhanced under stress and in apoptosis, e.g. in pancreatic cells in a model for diabetes, in case of angiotensin II type receptor occupancy
-
etoposide
-
enhanced activity due to chemotherapy with epotoside as therapeutic agent in Molt-4 leukemic cells
etoposide
activates enzyme activity, but decreases mRNA level, time-dependent
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.6
L-alanine
-
C133W mutant protein, pH not specified in the publication, temperature not specified in the publication
0.75
L-serine
-
wild type protein, pH not specified in the publication, temperature not specified in the publication
1.4
L-serine
-
C133W mutant protein, pH not specified in the publication, temperature not specified in the publication
additional information
L-alanine
-
wild-type enzyme does not utilize alanine efficiently
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 enzymes
-
additional information
additional information
-
Michaelis-Menten kinetics of wild-type and mutant enzymes
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
L-alanine
-
wild type protein, substrate serine, pH and temperature not specified in the publication
5
L-alanine
-
C133W mutant protein, substrate serine, pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000008 - 0.0000041
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
0.00000076 - 0.0000016
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
0.00000024 - 0.0000008
[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
0.0000008
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
Homo sapiens
subunit SPT2, at pH 8.0 and 25°C
0.0000041
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
Homo sapiens
subunit SPT3, at pH 8.0 and 25°C
0.00000076
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
Homo sapiens
subunit SPT2, at pH 8.0 and 25°C
0.0000016
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
Homo sapiens
subunit SPT3, at pH 8.0 and 25°C
0.00000024
[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
Homo sapiens
subunit SPT2, at pH 8.0 and 25°C
0.0000008
[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
Homo sapiens
subunit SPT3, at pH 8.0 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00011
-
substrate alanine, C133W mutant protein, pH not specified in the publication, temperature not specified in the publication
0.000275
-
substrate serine, C133W mutant protein, pH not specified in the publication, temperature not specified in the publication
0.00135
-
substrate serine, wild type protein, pH not specified in the publication, temperature not specified in the publication
0.0104
with [2,3,3-D] L-serine as cosubstrate, at pH 8.1 and 37°C
0.0113
with[2-13C] L-serine as cosubstrate, at pH 8.1 and 37°C
0.0122
with [3,3-D] L-serine as cosubstrate, at pH 8.1 and 37°C
0.0129
with [1,2,3-13C,2-15N] L-serine as cosubstrate, at pH 8.1 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
subunits SPTLC1 (O15269) and SPTLC2(O15270); subunits SPTLC1 and SPTLC2
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
protein expression of SPT in both psoriatic epidermis and non-lesional epidermis is investigated. Expression of SPT in psoriatic epidermis is significantly less than that of the non-lesional epidermis, which is inversely correlated with PASI score
-
elevation of ceramide in serum lipoproteins during acute phase response to inflammation is accompanied by activation of serine-palmitoyl transferase in liver
mucosal from colon, lung, prostate, stomach, thyroid, uterus, vascular tissue
additional information
additional information
not in neuronal cells like astrocytes, microglia, and oligodendritic cells, not in skin and heart
additional information
not in neuronal cells like astrocytes, microglia, and oligodendritic cells, not in skin and heart
additional information
-
not in neuronal cells like astrocytes, microglia, and oligodendritic cells, not in skin and heart
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
SPT subunit 1 is present in the endoplasmic reticulum
-
the enzyme is a transmembrane protein
-
the N-termini of the small activating subunit of serine palmitoyltransferase isoforms are locatedin the cytosol, their C-termini in the lumen, and they contain a single transmembrane domain
additional information
in addition to its localization in the endoplasmic reticulum for de novo sphingolipid biosynthesis, subunit SPT1 is present in other cellular compartments, including focal adhesions where it is associated with cell morphology, immunofluorescent subcellular localization study, overview
-
additional information
SPT subunit 1, it binds to the focal adhesion protein vinculin
-
additional information
ABL-mediated phosphorylation of enzyme SPTLC1 affects its endoplasmic reticulum localization
-
additional information
-
ABL-mediated phosphorylation of enzyme SPTLC1 affects its endoplasmic reticulum localization
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
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
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
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
the S384D but not the S384E mutation is associated with increased 1-deoxysphingolipids formation
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 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
-
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 long chain-1 (SPTLC1) is the first enzyme of sphingolipid biosynthesis
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
the enzyme catalyses the first step of de novo sphingolipid biosynthesis
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
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
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
specificity of wild-type SPT might by dynamically regulated by a phosphorylation at position S384
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
additional information
wild-type and mutant enzyme structure homology modeling and structure-function analyses, overview
additional information
-
wild-type and mutant enzyme structure homology modeling and structure-function analyses, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SPTC1_HUMAN
473
2
52744
Swiss-Prot
Secretory Pathway (Reliability: 4)
SPTC2_HUMAN
562
0
62924
Swiss-Prot
other Location (Reliability: 4)
SPTC3_HUMAN
552
0
62049
Swiss-Prot
other Location (Reliability: 2)
SPTSA_HUMAN
71
0
8466
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
480000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
heterotrimer
-
SPT is a heterodimer of 2 highly-related subunits, LCB1 and LCB2, existing in two isozyme forms LCB2a and LCB2b, associated with a third small activating subunit, either protein ssSPTa and protein ssSPTb, the proteins have a conserved hydrophobic central domain, reside in the membrane and interact with both hLCB1 and hLCB2 subunits, overview,protein ssSPTa and protein ssSPTb are required for maximal enzyme activity. SPT subunit interaction analysis, overview
octamer
-
results show that functional SPT is not a dimer, but a higher organized complex, composed of three distinct subunits (SPTLC1, SPTLC2 and SPTLC3) with a molecular mass of 480 kDa (gel filtration). The stoichiometry of SPTLC2 and SPTLC3 in this complex is not to be fixed and is changed dynamically in dependence of the tissue specific SPTLC2 and SPTLC3 expression levels. A model of an octameric SPT structure is proposed. By Blue-native-PAGE experiments it is shown that all three SPT subunits (SPTLC1-3) are co-localized within a single SPT complex
oligomer
additional information
heterodimer
-
structure comparison with the SPT from Sphingomonas paucimobilis, overview
heterodimer
the membrane-bound heterodimer composed of two subunits hLCB1 and hLCB2a/b. The hLCB1 and hLCB2 subunits display relatively high sequence homology to each other, but only the hLCB2a subunit contains key catalytic residues including the lysine that binds pyridoxal 5'-phosphate. Subunit hLCB1 lacks these residues but contains other residues involved in catalysis,the hLCB1/hLCB2a heterodimer has a single active site
heterodimer
the membrane-bound heterodimer composed of two subunits SPTLC1 and SPTLC2
oligomer
-
the enzyme is composed of three different types of subunits SPTLC1, SPTLC2, and SPTLC3
oligomer
-
the enzyme is composed of three different types of subunits, the stoichiometry of SPTLC2 and SPTLC3 in this complex seems not to be fixed and is probably changed dynamically in dependence of the tissue specific SPTLC2 and SPTLC3 expression levels, overview
additional information
-
reconstitution of the holoenzyme from subunits SPTLC1 and SPLC2, isolated from placenta extract, and recombinant subunit SPTLC3 forming a single multisubunit SPT complex, overview
additional information
-
the small activating subunits of serine palmitoyltransferase, ssSPTs, are glycoproteins and are part of the enzyme complex
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
the small activating subunits of serine palmitoyltransferase, ssSPTs, are glycoproteins and are part of the enzyme complex
phosphoprotein
phosphoprotein
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. ABL-mediated phosphorylation of SPTLC1 affects its endoplasmic reticulum localization
phosphoprotein
the enzyme is phosphorylated at S284 regulating its substrate specificity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in yeast and mammalian cells, a triple fusion protein of the three subunits expressed in yeast and mammalian cells
-
expression of wild-type and mutant enzymes in HEK-293 cells. The overexpression of wild-type subunit SPTLC1 does not increase SPT enzyme activity compared with controls (empty vector), whereas overexpressing subunit SPTLC2 results in a 2fold increase in enzyme activity
expression of wild-type and mutant smalll subunits isoforms of serine palmitoyltransferase in yeast microsomes
-
individual overexpression of subunits SPTLC1, SPTLC2, and SPTLC3, fused to a C-terminal V5-his tag, in HEK-293 cells
-
overexpression of SPTLC3 in HEK-293 cells leads to the formation of two new sphingoid base metabolites, namely C16-sphinganine and C16-sphingosine. SPTLC3-expressing cells have higher in vitro SPT activities with lauryl- and myristoyl-CoA than SPTLC2-expressing cells, and SPTLC3 mRNA expression levels correlate closely with the C16-sphinganine synthesis rates in various human and murine cell lines. Quantitative reverse transcription--PCR analysis
-
overexpression of subunit SPTLC3 in HEK-293 cells, leading to an 2-3fold increased SPT activity, expression of subunit SPTLC3 in Hep-G2 cells and human trophoblast cells, quantitative expression analysis of SPTLC3
-
recombinant expression of ssSPTa, tagged with EGFP at its N-terminus, in HEK-293 cells
recombinant expression of subunit LCB2a mutants in HEK293 cells, recombinant His-tagged enzyme expression in Escherichia coli strain BL21(DE3). Recombinant expression of wild-type hLCB1/hLCB2a subunits in Saccharomyces cerevisiae microsomes in the absence of either small subunit, the enzyme shows very low activity. 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
recombinant stable expression of mutant and wild-type SPTLC2 subunit in HEK293 cells
ssSPTa and ssSPTb, DNA and amino acid sequence determination and analysis. Transient functional overexpression of ssSPTb-containing isozymes in CHO LyB cells increasing C20-long-chain bases. Expression of the human enzyme subunits in the lcb1DELTAlcb2DELTA double mutant Saccharomyces cerevisiae cells in various combinations constituting enzyme activity, overview. Expression in CHO LyB cells lacking endogenous SPT activity
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
lithospermic acid and two derivative esters, 9''-methyl lithospermate and 9'-methyl lithospermate,isolated from roots of Lithospermum erythrorhizon, significantly increase SPT expression in the relative quantity of SPT1 mRNA as well as SPT2 mRNA, by 21-59%, overview
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of the holoenzyme from subunits SPTLC1 and SPLC2, isolated from placenta extract, and recombinant subunit SPTLC3 forming a single multisubunit SPT complex, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
decreased expression of SPT protein is one of the important causative factors for decreased ceramide levels in psoriasis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Holleran, W.M.; Williams, M.L.; Gao, W.N.; Elias, P.M.
Serine-palmitoyl transferase activity in cultured human keratinocytes
J. Lipid Res.
31
1655-1661
1990
Homo sapiens
Weiss, B.; Stoffel, W.
Human and murine serine-palmitoyl-CoA transferase. Cloning, expression and characterization of the key enzyme in sphingolipid synthesis
Eur. J. Biochem.
249
239-247
1997
Homo sapiens, Mus musculus
Perry, D.K.; Carton, J.; Shah, A.K.; Meredith, F.; Uhlinger, D.J.; Hannun, Y.A.
Serine palmitoyltransferase regulates de novo ceramide generation during etoposide-induced apoptosis
J. Biol. Chem.
275
9078-9084
2000
Homo sapiens, Homo sapiens (O15269), Homo sapiens (O15270)
Perry, D.K.
Serine palmitoyltransferase: role in apoptotic de novo ceramide synthesis and other stress responses
Biochim. Biophys. Acta
1585
146-152
2002
Saccharomyces cerevisiae, Homo sapiens, Mus musculus
Batheja, A.D.; Uhlinger, D.J.; Carton, J.M.; Ho, G.; D'Andrea, M.R.
Characterization of serine palmitoyltransferase in normal human tissues
J. Histochem. Cytochem.
51
687-696
2003
Homo sapiens (O15269), Homo sapiens (O15270), Homo sapiens
Lightle, S.; Tosheva, R.; Lee, A.; Queen-Baker, J.; Boyanovsky, B.; Shedlofsky, S.; Nikolova-Karakashian, M.
Elevation of ceramide in serum lipoproteins during acute phase response in humans and mice: role of serine-palmitoyl transferase
Arch. Biochem. Biophys.
419
120-128
2003
Homo sapiens, Mus musculus
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
1688
168-175
2004
Homo sapiens
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.
51
715-726
2003
Homo sapiens
Hornemann, T.; Wei, Y.; von Eckardstein, A.
Is the mammalian serine-palmitoyltransferase a high molecular weight complex?
Biochem. J.
405
157-164
2007
Homo sapiens
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
3507-3521
2005
Cricetulus griseus, Homo sapiens
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.
281
37275-37281
2006
Homo sapiens
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
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)
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
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)
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
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
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
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
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
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
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
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)
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
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
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
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
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
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
Sphingomonas paucimobilis, Homo sapiens (O15269 AND O15270 AND Q969W0), Homo sapiens
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