Kdo-8-phosphate synthase: Difference between revisions

Revision as of 11:21, 11 October 2021

Function

Kdo-8-phosphate synthase or 2-dehydro-3-deoxyphosphooctonate aldolase (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 biological assembly of Metallo Kdo-8-phosphate synthase from Neisseria meningitidis is . The ^[2]. Water molecules shown as red spheres.

Metallo Kdo-8-phosphate synthase tetramer complex with phosphoenolpyruvate, glycerol, Cl- (green), Na+ (large purple) and Mn+2 (small purple) ion, 3fyp

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3D structures of Kdo-8-phosphate synthase3D structures of Kdo-8-phosphate synthase

Updated on 11-October-2021

ReferencesReferences

↑ 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
↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

[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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 == 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<ref>PMID:11904225</ref>.
+'''Kdo-8-phosphate synthase''' or '''2-dehydro-3-deoxyphosphooctonate aldolase''' (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 ==