Kdo-8-phosphate synthase

From Proteopedia

proteopedia linkproteopedia link

Template:STRUCTURE 3fyp

Contents 1 Function 2 Structural highlights 3 3D structures of Kdo-8-phosphate synthase 4 References

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