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Information on EC 2.3.1.50 - serine C-palmitoyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q3B7D2
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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: Rattus norvegicus
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
-
-
-
-
SPT
-
-
-
-
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
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
-
-
?
stearoyl-CoA + L-serine
CoA + (2S)-2-amino-1-hydroxyicosan-3-one + 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
-
-
i.e. 2-amino-1-hydroxyoctadecane-3-one, i.e. 3-oxo-dihydroxysphingosine
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
palmitoyl-CoA is the preferred substrate
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
palmitoyl-CoA is the preferred substrate
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
activities are greatest with palmitoyl-CoA and palmitelaidoyl-CoA, followed by fully saturated homologs, activity considerably diminishes as the alkyl-chain length increases or decreases, or with the presence of a cis-double bond
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
no other amino acids can substitute for serine
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
initial step of de novo ceramide biosynthesis
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme catalyses the first step in the ceramide biosynthesis pathway
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme is involved in the ceramide metabolism, overview
-
-
?
additional information
?
-
-
the enzyme activity and expression in the heart is not affected by high-fat feeding
-
-
?
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
additional information
?
-
-
the enzyme activity and expression in the heart is not affected by high-fat feeding
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
first step of biosynthesis of sphingolipid bases
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
initial step of de novo ceramide biosynthesis
-
ir
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme catalyses the first step in the ceramide biosynthesis pathway
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
the enzyme is involved in the ceramide metabolism, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate can be resolved from the enzyme by dialysis
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
NaCl, LiCl, MgCl2, MnCl2 have no effect on activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-chloro-L-alanine
-
rapid, irreversible and time dependent inhibition at the active site; stereospecific, no inhibition by beta-chloro-D-alanine; suicide substrate
ceramide 1-phosphate
-
from bovine brain, inhibits the enzyme and blocks apoptosis in alveolar macrophages, overview
myriocin
-
both short and prolonged time of inhibition of the enzyme by myriocin is sufficient to prevent ceramide accumulation and simultaneously reverse palmitate induced inhibition of insulin-stimulated glucose transport
additional information
-
the enzyme activity and expression in the heart is not affected by high-fat feeding
-
additional information
-
short-term inhibition of SPT ameliorates palmitate/ceramide-induced insulin resistance, sustained loss/reduction in SPT expression/activity promotes greater partitioning of palmitate towards diacylglycerol synthesis, which impacts negatively upon IRS1-directed insulin signalling
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pioglitazone
-
increases the enzyme activity in vitro and in vivo independent of standard or high-fat diet
additional information
-
increased SPT enzyme activity in reactive astrocytes of the hippocampus at 2 weeks post-kainate injection
-
additional information
-
the enzyme activity and expression in the heart is not affected by high-fat feeding
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
increased enzymatic activity of SPT in reactive astrocytes of the hippocampus after kainate injections is shown
additional information
-
enzyme activity and ceramide synthesis in macrophages, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.3
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
increased SPT enzyme activity in reactive astrocytes of the hippocampus at 2 weeks post-kainate injection
-
increased SPT enzyme activity in reactive astrocytes of the hippocampus at 2 weeks post-kainate injection
-
increased expression of SPT in reactive astrocytes of the hippocampus after kainate injections is shown
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
IRS1 serine phosphorylation and PKCtheta recruitment to the plasma membrane are increased in cells with reduced SPT expression and activity. Short-term inhibition of SPT ameliorates palmitate/ceramide-induced insulin resistance, sustained loss/reduction in SPT expression/activity promotes greater partitioning of palmitate towards diacylglycerol synthesis, which impacts negatively upon IRS1-directed insulin signalling
malfunction
-
both short and prolonged time of inhibition of the enzyme by myriocin is sufficient to prevent ceramide accumulation and simultaneously reverse palmitate induced inhibition of insulin-stimulated glucose transport
malfunction
-
inhibiting the enzyme in the astrocytes decreases the levels of both TNFalpha and interleukin-1beta in the conditioned media, which in turn reduced the neural and acidic sphingomyelinase activities and BACE1 level in primary neurons, overview
metabolism
-
SPT is the key regulator enzyme in the ceramide de novo biosynthesis pathway
metabolism
-
the first and rate-limiting step of de novo synthesis is the condensation of a fatty acyl-CoA, usually palmitoyl-CoA, with serine, which is catalyzed by the enzyme serine palmitoyltransferase to form 3-dehydrosphinganin
physiological function
-
SPT plays a crucial role in lipid-induced insulin resistance in skeletal muscle cells by desensitizing muscle cells to insulin in response to incubation with palmitate, overview. The effect is antagonized by inhibition of protein kinase C
physiological function
-
the enzyme is required for ceramide synthesis as key regulatory enzyme of this pathway, major mechanism for ceramide generation in NR8383 macrophages is stimulation of their de novo synthesis
physiological function
-
serine palmitoyltransferase in the astrocytes increases ceramide levels, which enhances the release of cytokines that mediate the activation of neural and acidic sphingomyelinase (N-SMase and A-SMase) in the neurons, to propagate the deleterious effects of palmitate, i.e. BACE1 upregulation and amyloidogenesis in primary rat neurons, overview
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_RAT
473
2
52549
Swiss-Prot
Secretory Pathway (Reliability: 4)
SPTC2_RAT
560
0
62962
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
carrier lipid during extraction required for activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
short-term Mg deficiency results in an upregulation of major subunit 1 and 2 in cardiovascular tissues
-
the levels of subunits SPTLC1 and 2 progressively increase at both the protein and mRNA levels in oligodendrocytes as the cells differentiate from immature oligodendrocyte progenitors (day 2) into mature myelinating oligodendrocytes (day 16)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
results suggest that SPT activity might contribute to neuronal injury after kainate excitotoxicity in the rat hippocampus
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stoffel, W.; LeKim, D.; Sticht, G.
Biosynthesis of dihydrosphingosine in vitro
Hoppe-Seyler's Z. Physiol. Chem.
349
664-670
1968
Wickerhamomyces ciferrii, Rattus norvegicus
Merrill, A.H.; Wang, E.
Enzymes of ceramide biosynthesis
Methods Enzymol.
209
427-437
1992
Prevotella melaninogenica, Saccharomyces cerevisiae, Rattus norvegicus
Merrill, A.H.; Williams, R.D.
Utilization of different fatty acyl-CoA thioesters by serine palmitoyltransferase from rat brain
J. Lipid Res.
25
185-188
1984
Rattus norvegicus
Williams, R.D.; Wang, E.; Merrill, A.H.
Enzymology of long-chain base synthesis by liver: characterization of serine palmitoyltransferase in rat liver microsomes
Arch. Biochem. Biophys.
228
282-291
1984
Rattus norvegicus
Medlock, K.A.; Merrill, A.H.
Inhibition of serine palmitoyltransferase in vitro and long-chain base biosynthesis in intact Chinese hamster ovary cells by beta-chloroalanine
Biochemistry
27
7079-7084
1988
Cricetulus griseus, Rattus norvegicus
He, X.; Guan, X.L.; Ong, W.Y.; Farooqui, A.A.; Wenk, M.R.
Expression, activity, and role of serine palmitoyltransferase in the rat hippocampus after kainate injury
J. Neurosci. Res.
85
423-432
2007
Rattus norvegicus
Baranowski, M.; Blachnio, A.; Zabielski, P.; Gorski, J.
Pioglitazone induces de novo ceramide synthesis in the rat heart
Prostaglandins Other Lipid Mediat.
83
99-111
2007
Rattus norvegicus
Watson, M.L.; Coghlan, M.; Hundal, H.S.
Modulating serine palmitoyl transferase (SPT) expression and activity unveils a crucial role in lipid-induced insulin resistance in rat skeletal muscle cells
Biochem. J.
417
791-801
2009
Rattus norvegicus
Granado, M.H.; Gangoiti, P.; Ouro, A.; Arana, L.; Gomez-Munoz, A.
Ceramide 1-phosphate inhibits serine palmitoyltransferase and blocks apoptosis in alveolar macrophages
Biochim. Biophys. Acta
1791
263-272
2009
Rattus norvegicus
Altura, B.M.; Shah, N.C.; Li, Z.; Jiang, X.C.; Perez-Albela, J.L.; Altura, B.T.
Magnesium deficiency upregulates serine palmitoyl transferase (SPT 1 and SPT 2) in cardiovascular tissues: relationship to serum ionized Mg and cytochrome c
Am. J. Physiol. Heart Circ. Physiol.
299
H932-H938
2010
Rattus norvegicus
Liu, L.; Martin, R.; Chan, C.
Palmitate-activated astrocytes via serine palmitoyltransferase increase BACE1 in primary neurons by sphingomyelinases
Neurobiol. Aging
34
540-550
2013
Rattus norvegicus, Rattus norvegicus Sprague Dawley
Miklosz, A.; Lukaszuk, B.; Baranowski, M.; Gorski, J.; Chabowski, A.
Effects of inhibition of serine palmitoyltransferase (SPT) and sphingosine kinase 1 (SphK1) on palmitate induced insulin resistance in L6 myotubes
PLoS ONE
8
e85547
2013
Rattus norvegicus
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