Serine palmitoyltransferase
From Proteopedia
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| - | {{STRUCTURE_3a2b| PDB=3a2b | SIZE=400| SCENE= |right|CAPTION= | + | {{STRUCTURE_3a2b| PDB=3a2b | SIZE=400| SCENE= |right|CAPTION=Monomer of the dimeric prokaryotic serine palmitoyltransferase complex with serine and cofactor pyridoxal phosphate [[3a2b]] }} |
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Revision as of 09:46, 15 November 2012
Template:STRUCTURE 3a2b Serine palmitoyltransferase (SPT) catalyzes the conversion of palmitoyl-CoA and serine to CoA and dehydro-sphinganine. This reaction is part of sphingosine biosynthesis. Pyridoxal phosphate is a cofactor in the reaction. The prokaryotic SPT is a soluble homodimer while the eukaryotic one is heterodimeric and is anchored in the endoplasmic reticulum.
3D structures of serine palmitoyltransferase
2jg2 – PpSPT + aldimine – Pseudomonas paucimobilis
2jgt – PpSPT
2w8j - SpSPT + aldimine – Sphingomonas paucimobilis
2w8t, 2w8u, 2w8v, 2w8w - SpSPT (mutant) + aldimine
2xbn – SpSPT + pyridoxamine phosphate
3a2b – SPT + pyridoxal phosphate + serine – Sphingobacterium multivorum
