Kdo-8-phosphate synthase
From Proteopedia
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== Function == | == 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 == | == Structural highlights == | ||
Revision as of 08:21, 11 October 2021
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3D structures of Kdo-8-phosphate synthase
Updated on 11-October-2021
References
- ↑ 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
