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
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2.3.1.50
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sphingolipids
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ceramide
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myriocin
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sphingomyelin
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sphingosine
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sphingomyelinase
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neuropathy
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sphingoid
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cholesterol
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fumonisin
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glucosylceramide
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sphingosine-1-phosphate
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3-ketodihydrosphingosine
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corneum
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glycosphingolipids
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dihydroceramide
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dihydrosphingosine
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plp-dependent
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l-cycloserine
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ormdl3
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molecular biology
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sphingomonas
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paucimobilis
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transepidermal
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charcot-marie-tooth
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analysis
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ceramide-induced
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phytosphingosine
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medicine
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asmase
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aldimine
- 2.3.1.50
- sphingolipids
- ceramide
- myriocin
- sphingomyelin
- sphingosine
- sphingomyelinase
- neuropathy
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sphingoid
- cholesterol
- fumonisin
- glucosylceramide
- sphingosine-1-phosphate
- 3-ketodihydrosphingosine
- corneum
- glycosphingolipids
- dihydroceramide
- dihydrosphingosine
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plp-dependent
- l-cycloserine
-
ormdl3
- molecular biology
- sphingomonas
- paucimobilis
-
transepidermal
-
charcot-marie-tooth
- analysis
-
ceramide-induced
- phytosphingosine
- medicine
- asmase
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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
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Crystallization
Crystallization on EC 2.3.1.50 - serine C-palmitoyltransferase
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purified recombinant enzyme complexed with L-serine, sitting drop vapor diffusion method, 0.002 ml of protein solution containing 20 mg/ml SPT, 20 mM potasium phosphate, pH 7.7, and 10 mM pyridoxal 5'-phosphate, is mixed with 0.004 ml of reservoir solution containing 100 mM Tris-HCl; pH 8.5, 200 mM sodium acetate, 21.6% w/v PEG 4000, equilibration against 0.5 ml reservoir solution at 20°C, 2 weeks, Schiff base formation between L-serine and pyridoxal 5'-phosphate in the crystal, X-ray diffraction structure determination and analysis at 2.3 A resolution, structural modelling
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
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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