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Kdo-8-phosphate synthase

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Template:STRUCTURE 3fyp

Contents

Function

Kdo-8-phosphate synthase (KPS) catalyzes the formation of the phosphorylated rare sugar Kdo-8-phosphate (Kdo-8-P) from phosphoenolpyruvate (PEP) and D-arabinose-5-phosphate (A5P). KPS is a metal-requiring enzyme. Kdo-8-P is found in cell walls of higher plants and some green algae[1].

Structural highlights

The active site of the metallo KPS contains a divalent cation and the PEP substrate[2].

[3].

3D structures of Kdo-8-phosphate synthase

Updated on 05-April-2016

References

  1. Krosky DJ, Alm R, Berg M, Carmel G, Tummino PJ, Xu B, Yang W. Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase is a zinc-metalloenzyme. Biochim Biophys Acta. 2002 Feb 11;1594(2):297-306. PMID:11904225
  2. Cochrane FC, Cookson TV, Jameson GB, Parker EJ. Reversing evolution: re-establishing obligate metal ion dependence in a metal-independent KDO8P synthase. J Mol Biol. 2009 Jul 24;390(4):646-61. Epub 2009 May 15. PMID:19447118 doi:10.1016/j.jmb.2009.05.014
  3. White SH, Wimley WC, Selsted ME. Structure, function, and membrane integration of defensins. Curr Opin Struct Biol. 1995 Aug;5(4):521-7. PMID:8528769

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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