Serine palmitoyltransferase

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== Function ==
== Function ==
'''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 (PLP) 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<ref>PMID:12782147</ref>.
'''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 (PLP) 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<ref>PMID:12782147</ref>.
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== Structural highlights ==
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The active site of SPT contains a serene residue covalently bound to the cofactor PLP<ref>PMID:19564159</ref>.
==3D structures of serine palmitoyltransferase==
==3D structures of serine palmitoyltransferase==

Revision as of 07:53, 25 August 2016

Template:STRUCTURE 3a2b

Contents

Function

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 (PLP) 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[1].

Structural highlights

The active site of SPT contains a serene residue covalently bound to the cofactor PLP[2].

3D structures of serine palmitoyltransferase

Updated on 25-August-2016

2jg2 – PpSPT + aldimine – Pseudomonas paucimobilis
2jgt – PpSPT
2w8j - SpSPT + aldimine – Sphingomonas paucimobilis
2w8t, 2w8u, 2w8v, 2w8w - SpSPT (mutant) + aldimine
4bmk - SpSPT (mutant) + myriocin + PLP
2xbn – SpSPT + pyridoxamine phosphate
3a2b – SPT + pyridoxal phosphate + serine – Sphingobacterium multivorum
2x8u - SwSPT + pyridoxal derivative – Sphingomonas wittichii

References

  1. Hanada K. Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism. Biochim Biophys Acta. 2003 Jun 10;1632(1-3):16-30. PMID:12782147
  2. Ikushiro H, Islam MM, Okamoto A, Hoseki J, Murakawa T, Fujii S, Miyahara I, Hayashi H. Structural insights into the enzymatic mechanism of serine palmitoyltransferase from Sphingobacterium multivorum. J Biochem. 2009 Oct;146(4):549-62. Epub 2009 Jun 29. PMID:19564159 doi:10.1093/jb/mvp100

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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