Kdo-8-phosphate synthase

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{{STRUCTURE_3fyp| PDB=3fyp | SIZE=400| SCENE= |right|CAPTION=Metallo Kdo-8-phosphate synthase tetramer complex with phosphoenolpyruvate, glycerol, Cl- (green), Na+ (large purple) and Mn+2 (small purple) ion, [[3fyp]] }}
{{STRUCTURE_3fyp| PDB=3fyp | SIZE=400| SCENE= |right|CAPTION=Metallo Kdo-8-phosphate synthase tetramer complex with phosphoenolpyruvate, glycerol, Cl- (green), Na+ (large purple) and Mn+2 (small purple) ion, [[3fyp]] }}
== Function ==
== Function ==
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'''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). Some bacteria like 'Aquifex aeolicus'' have '''Metallo KPS''' which is a metal-requiring enzyme while others like ''E.coli'' have a '''Non-metallo KPS''' which does not require a divalent cation for its activity. Kdo-8-P is found in cell walls of higher plants and some green algae<ref>PMID:11904225</ref>.
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'''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). Some bacteria like ''Aquifex aeolicus'' have '''Metallo KPS''' which is a metal-requiring enzyme while others like ''E.coli'' have a '''Non-metallo KPS''' which does not require a divalent cation for its activity. Kdo-8-P is found in cell walls of higher plants and some green algae<ref>PMID:11904225</ref>.
== Structural highlights ==
== Structural highlights ==

Revision as of 10:22, 6 April 2016

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). Some bacteria like Aquifex aeolicus have Metallo KPS which is a metal-requiring enzyme while others like E.coli have a Non-metallo KPS which does not require a divalent cation for its activity. 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].

3D structures of Kdo-8-phosphate synthase

Updated on 06-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

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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