Role of a conserved arginine residue during catalysis in serine palmitoyltransferase

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書誌事項

公開日
2011-04-18
資源種別
journal article
権利情報
  • http://doi.wiley.com/10.1002/tdm_license_1
DOI
  • 10.1016/j.febslet.2011.04.013
公開者
Wiley

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説明

All sphingolipid-producing organisms require the pyridoxal 5'-phosphate (PLP)-dependent serine palmitoyltransferase (SPT) to catalyse the first reaction on the de novo sphingolipid biosynthetic pathway. SPT is a member of the alpha oxoamine synthase (AOS) family that catalyses a Claisen-like condensation of palmitoyl-CoA and L-serine to form 3-ketodihydrosphingosine (KDS). Protein sequence alignment across various species reveals an arginine residue, not involved in PLP binding, to be strictly conserved in all prokaryotic SPTs, the lcb2 subunits of eukaryotic SPTs and all members of the AOS family. Here we use UV-vis spectroscopy and site-directed mutagenesis, in combination with a substrate analogue, to show that the equivalent residue (R370) in the SPT from Sphingomonas wittichii is required to form the key PLP:L-serine quinonoid intermediate that condenses with palmitoyl-CoA and thus plays an essential role enzyme catalysis.

収録刊行物

  • FEBS Letters

    FEBS Letters 585 (12), 1729-1734, 2011-04-18

    Wiley

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