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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

Reaction

palmitoyl-CoA
+
L-serine
=
CoA
 +
3-dehydro-D-sphinganine
 +
CO2

Synonyms

3-oxosphinganine synthetase, acyl-CoA:serine C-2 acyltransferase decarboxylating, LCB1, LCB2, LCB2a, LCB2b, More, palmitoyltransferase, serine, serine palmitoyl transferase, serine palmitoyltransferase, serine palmitoyltransferase 1, serine palmitoyltransferase a, serine-palmitoyl transferase, serine-palmitoyltransferase, SPT, SPT1, SPT2, SPT3, SPTase, SPTLC1, SPTLC2, ssSPT, ssSPTa, Tsc3

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.50 serine C-palmitoyltransferase

Crystallization

Crystallization on EC 2.3.1.50 - serine C-palmitoyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pH 7.5, 30% PEG monomethylether 2000
Rhizorhabdus wittichii
-
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
after incubation with L-cycloserine
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
-
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