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Information on EC 2.3.1.50 - serine C-palmitoyltransferase and Organism(s) Sphingomonas paucimobilis and UniProt Accession Q93UV0
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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: Sphingomonas paucimobilis
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, serine c-palmitoyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
serine palmitoyltransferase
-
3-oxosphinganine synthetase
-
-
-
-
acyl-CoA:serine C-2 acyltransferase decarboxylating
-
-
-
-
palmitoyltransferase, serine
-
-
-
-
serine palmitoyltransferase
serine-palmitoyltransferase
-
-
-
-
SPT
additional information
-
SPT belongs to the fold type I family of the pyridoxal 5'-phosphate-dependent enzymes, and the alpha-oxamine synthase subfamily enzymes
serine palmitoyltransferase
-
-
-
-
SPT
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 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
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 several intermediate states, the pyridoxal 5'-phosphate cofactor binds to an active site lysine residue as an internal aldimine/Schiffs 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
ordered bi-bi mechanism
-
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 Dunathans 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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
Acyl group transfer
-
-
-
-
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 + palmitoyl-CoA
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
lauroyl-CoA + L-serine
CoA + 2-amino-1-hydroxytetradecan-3-one + CO2
18% activity compared to palmitoyl-CoA
-
-
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
second best substrate
-
-
?
arachidoyl-CoA + L-serine
CoA + 2-amino-1-hydroxydocosan-3-one + CO2
-
37% activity compared to that with palmitoyl-CoA
-
-
?
elaidoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-trans-11-eicosen-3-one + CO2
-
39% activity compared to that with palmitoyl-CoA
-
-
?
lauroyl-CoA + L-serine
CoA + 2-amino-1-hydroxytetradecan-3-one + CO2
-
18% activity compared to that with palmitoyl-CoA
-
-
?
myristoleoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-cis-11-hexadecen-3-one + CO2
-
46% activity compared to that with palmitoyl-CoA
-
-
?
myristoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
75% activity compared to that with palmitoyl-CoA
-
-
?
n-heptadecanoyl-CoA + L-serine
CoA + 2-amino-1-hydroxynonadecan-3-one + CO2
-
75% activity compared to that with palmitoyl-CoA
-
-
?
oleoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-11-cis-eicosen-3-one + CO2
-
57% activity compared to that with palmitoyl-CoA
-
-
?
palmitoleoyl-CoA + L-serine
CoA + 2-amino-1-hydroxy-cis-11-octadecen-3-one + CO2
-
80% activity compared to that with palmitoyl-CoA
-
-
?
stearoyl-CoA + L-serine
CoA + 2-amino-1-hydroxyeicosan-3-one + CO2
-
51% activity compared to that with palmitoyl-CoA
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
100% activity
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
rate-limiting enzyme in synthesis of sphingolipids
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
interaction between the hydroxyl group of the L-serine substrate and the 5'-phosphate group of pyridoxal 5'-phosphate. This interaction is important for substrate specificity and optimal catalytic efficiency
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
palmitoyl-CoA is the preferred substrate
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
no other amino acids can substitute for serine
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
His159 is the anchoring site for L-serine and regulates the alpha-deprotonation of L-serine by fixing the conformation of the pyridoxal 5'-phosphate-L-serine aldimine to prevent unwanted side reactions
-
-
?
additional information
?
-
no activity with L-phosphoserine
-
-
?
additional information
?
-
no activity with octanoyl-CoA
-
-
-
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
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
-
-
-
-
?
palmitoyl-CoA + L-serine
CoA + 3-dehydro-D-sphinganine + CO2
rate-limiting enzyme in synthesis of sphingolipids
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on, bound at the active site at the dimer interface
pyridoxal 5'-phosphate
dependent on, bound by lysine 265 residue, interaction between the hydroxyl group of the L-serine substrate and the 5'-phosphate group of pyridoxal 5'-phosphate. This interaction is important for substrate specificity and optimal catalytic efficiency
pyridoxal 5'-phosphate
-
bound to epsilon-amino group of a lysine residue in the active site
pyridoxal 5'-phosphate
-
dependent on, the re face of SPT of the pyridoxal 5'-phosphate-Lys aldimine is occupied by a His159 residue instead of an aromatic amino acid residue as in the other type I enzymes
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-amino-3-isoxazolidone
D-cycloserine and L-cycloserine are inhibitors, L-cycloserine is 14-fold more effective than D-cycloserine
myriocin
i.e. (2S,3R,4R,6E)-2-amino-3,4-dihydroxy-2-(hydroxymethyl)-14-oxo-6-eicosenoic acid, or thermozymocidin and ISP-1, is a fungal natural product, kinetics and molecular mechanism of enzyme inhibition, overview. Myriocin is a potent SPT enzyme inhibitor. It initially forms an external aldimine with pyridoxal 5'-phosphate at the active site, the structure of the resulting co-complex explains its nanomolar affinity for the enzyme. The cofactor-inhibitor co-complex, PLP-myriocin aldimine, catalytically degrades via an unexpected retro-aldol-like cleavage mechanism to a C18 aldehyde which in turn acts as a suicide inhibitor of the enzyme by covalent modification of the essential catalytic lysine. This dual mechanism of inhibition rationalizes the extraordinary potency and longevity of myriocin inhibition. Incubations of enzyme SPT with myriocin is consistent with the formation of an initial enzyme-inhibitor complex which is noncovalent in nature and reversible, albeit with a very slow off rate (koff), the PLP-myriocin aldimine as the initial competitive inhibitory species. In contrast, for the enzyme preincubated with myriocin for 16 h, no detectable regain in activity is observed after dialysis either at 3 or 24 h, the second formed covalent adduct acts as an irreversible inhibitor of enzyme SPT
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
L-serine
recombinant wild-type enzyme, pH 7.5, 25°C
5.6
L-serine
mutant enzyme R378K, with palmitoyl-CoA as cosubstrate, at pH 7.5 and 25°C
7.2
L-serine
wild type enzyme, with palmitoyl-CoA as cosubstrate, at pH 7.5 and 25°C
0.035
palmitoyl-CoA
pH 7.5, 37°C, recombinant wild-type enzyme
0.0356
palmitoyl-CoA
recombinant wild-type enzyme, pH 7.5, 25°C
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzyme
-
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics.The regenerated enzyme displays similar Km and kcat values to the purified enzyme, with only a small increase in the Km for L-serine
-
additional information
additional information
-
kinetics analysis, detailed overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.14
palmitoyl-CoA
recombinant wild-type enzyme, pH 7.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
L-serine
mutant enzyme R378K, with myristoyl-CoA as cosubstrate, at pH 7.5 and 25°C
1.4
L-serine
wild type enzyme, with myristoyl-CoA as cosubstrate, at pH 7.5 and 25°C
32.02
palmitoyl-CoA
recombinant wild-type enzyme, pH 7.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.441
-
with [1,2,3-13C,2-15N] L-serine as cosubstrate, at pH 8.1 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the PLP-superfamily and a member of the alpha-oxoamine synthase family (AOS, fold type I)
metabolism
physiological function
the enzyme is required for de novo sphingolipid biosynthesis
metabolism
-
SPT catalyzes the first and rate-limiting step of the sphingolipid biosynthetic pathway
additional information
metabolism
sphingolipids are essential components of cellular membranes formed from the condensation of L-serine and a long-chain acyl thioester. This first step is catalyzed by the pyridoxal 5'-phosphate-dependent enzyme serine palmitoyltransferase
metabolism
the enzyme catalyses the first step of de novo sphingolipid biosynthesis
additional information
key active site residues are His159, Asp231, His234, and Lys265
additional information
the interaction between the hydroxyl group of the L-serine substrate and the 5'-phosphate group of pyridoxal 5'-phosphate is important for substrate specificity and optimal catalytic efficiency. Structure of the PLP-L-serine external aldimine intermediate of the enzyme, PDB ID 2W8J, 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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90000
90000
about, recombinant wild-type enzyme and mutants V246M and G385F, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
the membrane-bound heterodimer composed of two subunits hLCB1 and hLCB2a/b
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
determination of the crystal structure of enzyme mutant K265A that diffract to 1.6 A resolution and contain a canonical dimer in the asymmetric unit. Crystallization of the wild-type SPT:PLP-myriocin aldimine complex is not possible, most likely due to aldimine degradation
purified His-tagged recombinant wild-type and mutant enzymes in complex with cofactor and substrates, wild-type enzyme from 10 mM Tris, pH 7.5, 150 mM NaCl, and 0.025 mM or 0.250 mM pyridoxal 5'-phosphate, different conditions for the mutants, overview. Mass spectroscopic structure analysis, overview
crystal structure of the holo-form of SPT is determined to 1.3 A resolution. Enzyme is a symmetrical homodimer with two active sites and a monomeric tertiary structure consisting of three domains. PLP cofactor is bound covalently to Lys265 as an internal aldimine/Schiff base and the active site is composed of residues from both subunits, located at the bottom of a deep cleft
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
H159A
-
site-directed mutagenesis, the mutant shows reduced activity and still forms the pyridoxal 5'-phosphate-L-serine-aldimine reaction intermediate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, Tris-HCl 20 mM, in sterile capped vials, 2 months without loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+), gel filtration
native and recombinant from E. coli, LCB1 and LCB2 co-immunoprecipitate
recombinant His-tagged wild-type and enzyme and mutants V246M and G385F from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli BL21 (DE3) pLysS, DNA sequence determination
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
overexpression in Escherichia coli BL21 (DE3) pLysS, DNA sequence determination
-
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
useful as a model to elucidate the reaction mechanism
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ikushiro, H.; Hayashi, H.; Kagamiyama, H.
A water-soluble homodimeric serine palmitoyltransferase from Sphingomonas paucimobilis EY2395T strain: purification, characterization, cloning, and overproduction
J. Biol. Chem.
276
18249-18256
2001
Sphingomonas paucimobilis, Sphingomonas paucimobilis EY2395
Ikushiro, H.; Hayashi, H.; Kagamiyama, H.
Bacterial serine palmitoyltransferase: a water-soluble homodimeric prototype of the eukaryotic enzyme
Biochim. Biophys. Acta
1647
116-120
2003
Sphingomonas paucimobilis (Q93UV0), Sphingomonas paucimobilis
Ikushiro, H.; Hayashi, H.; Kagamiyama, H.
Reactions of serine palmitoyltransferase with serine and molecular mechanisms of the actions of serine derivatives as inhibitors
Biochemistry
43
1082-1092
2004
Sphingomonas paucimobilis, Sphingomonas paucimobilis EY2395
Ikushiro, H.; Fujii, S.; Shiraiwa, Y.; Hayashi, H.
Acceleration of the substrate Calpha deprotonation by an analogue of the second substrate palmitoyl-CoA in Serine Palmitoyltransferase
J. Biol. Chem.
283
7542-7553
2008
Sphingomonas paucimobilis (Q93UV0)
Yard, B.A.; Carter, L.G.; Johnson, K.A.; Overton, I.M.; Dorward, M.; Liu, H.; McMahon, S.A.; Oke, M.; Puech, D.; Barton, G.J.; Naismith, J.H.; Campopiano, D.J.
The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis
J. Mol. Biol.
370
870-886
2007
Sphingomonas paucimobilis
Shiraiwa, Y.; Ikushiro, H.; Hayashi, H.
Multifunctional role of His159in the catalytic reaction of serine palmitoyltransferase
J. Biol. Chem.
284
15487-15495
2009
Sphingomonas paucimobilis
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)
Lowther, J.; Yard, B.A.; Johnson, K.A.; Carter, L.G.; Bhat, V.T.; Raman, M.C.; Clarke, D.J.; Ramakers, B.; McMahon, S.A.; Naismith, J.H.; Campopiano, D.J.
Inhibition of the PLP-dependent enzyme serine palmitoyltransferase by cycloserine: evidence for a novel decarboxylative mechanism of inactivation
Mol. Biosyst.
6
1682-1693
2010
Sphingomonas paucimobilis (Q93UV0), Sphingomonas paucimobilis
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
Beattie, A.E.; Clarke, D.J.; Wadsworth, J.M.; Lowther, J.; Sin, H.L.; Campopiano, D.J.
Reconstitution of the pyridoxal 5-phosphate (PLP) dependent enzyme serine palmitoyltransferase (SPT) with pyridoxal reveals a crucial role for the phosphate during catalysis
Chem. Commun. (Camb. )
49
7058-7060
2013
Sphingomonas paucimobilis (Q93UV0)
Wadsworth, J.M.; Clarke, D.J.; McMahon, S.A.; Lowther, J.P.; Beattie, A.E.; Langridge-Smith, P.R.; Broughton, H.B.; Dunn, T.M.; Naismith, J.H.; Campopiano, D.J.
The chemical basis of serine palmitoyltransferase inhibition by myriocin
J. Am. Chem. Soc.
135
14276-14285
2013
Sphingomonas paucimobilis (Q93UV0)
Choe, H.; Cha, M.; Stewart, J.
Semi-rational approach to expand the acyl-CoA chain length tolerance of Sphingomonas paucimobilis serine palmitoyltransferase
Enzyme Microb. Technol.
137
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