Literature summary for 2.3.1.50 extracted from

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 (2007), J. Mol. Biol., 370, 870-886.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Sphingomonas paucimobilis

Organism

Organism	UniProt	Comment	Textmining
Sphingomonas paucimobilis	-	-	-

Subunits

Subunits	Comment	Organism
homodimer	crystal structure	Sphingomonas paucimobilis

Synonyms

Synonyms	Comment	Organism
serine palmitoyltransferase	-	Sphingomonas paucimobilis
SPT	-	Sphingomonas paucimobilis

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Sphingomonas paucimobilis

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Release 2023.1 (January 2023)