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Kdo-8-phosphate synthase
From Proteopedia
(Difference between revisions)
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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). KPS is a metal-requiring enzyme. | '''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<ref>PMID: | + | Kdo-8-P is found in cell walls of higher plants and some green algae<ref>PMID:11904225</ref>. |
| + | == Structural highlights == | ||
| + | The active site of the metallo KPS contains a divalent cation and the PEP substrate<ref>PMID:19447118</ref>. | ||
<ref>PMID:8528769</ref>. | <ref>PMID:8528769</ref>. | ||
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*Metallo Kdo8P | *Metallo Kdo8P | ||
| - | **[[1fxp]] - AaKPS + Cd – Aquifex aeolicus<br /> | + | **[[1fxp]] - AaKPS + Cd – ''Aquifex aeolicus''<br /> |
**[[1lrn]], [[1t99]] - AaKPS (mutant) + Cd<br /> | **[[1lrn]], [[1t99]] - AaKPS (mutant) + Cd<br /> | ||
| - | **[[2qkf]] – NmKPS + Na – Neisseria meningitides<br /> | + | **[[2qkf]] – NmKPS + Na – ''Neisseria meningitides''<br /> |
**[[3fyo]] - NmKPS (mutant) + Mn<br /> | **[[3fyo]] - NmKPS (mutant) + Mn<br /> | ||
**[[3qpy]], [[3qpz]], [[3qq0]], [[3stc]], [[3ste]], [[3stf]], [[4jte]], [[4jtf]], [[4jtg]], [[4jth]], [[4jti]], [[4jtj]], [[4jtk]], [[4jtl]] - NmKPS (mutant) + Na<br /> | **[[3qpy]], [[3qpz]], [[3qq0]], [[3stc]], [[3ste]], [[3stf]], [[4jte]], [[4jtf]], [[4jtg]], [[4jth]], [[4jti]], [[4jtj]], [[4jtk]], [[4jtl]] - NmKPS (mutant) + Na<br /> | ||
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**[[1pck]] - AaKPS + PEP derivative + Cd<br /> | **[[1pck]] - AaKPS + PEP derivative + Cd<br /> | ||
**[[1pe1]] - AaKPS + phosphoglyceric acid + Cd<br /> | **[[1pe1]] - AaKPS + phosphoglyceric acid + Cd<br /> | ||
| - | **[[2a21]] - EcKPS + PEP + Zn - Escherichia coli<br /> | + | **[[2a21]] - EcKPS + PEP + Zn - ''Escherichia coli''<br /> |
**[[1jcx]], [[1pcw]] - AaKPS + inhibitor + Cd<br /> | **[[1jcx]], [[1pcw]] - AaKPS + inhibitor + Cd<br /> | ||
**[[1fy6]] - AaKPS + A5P + Cd<br /> | **[[1fy6]] - AaKPS + A5P + Cd<br /> | ||
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**[[1fx6]] - AaKPS <br /> | **[[1fx6]] - AaKPS <br /> | ||
**[[2nws]], [[2nx3]] - AaKPS (mutant) <br /> | **[[2nws]], [[2nx3]] - AaKPS (mutant) <br /> | ||
| - | **[[1o60]] - KPS – Haemophilus influenza<br /> | + | **[[1o60]] - KPS – ''Haemophilus influenza''<br /> |
| - | **[[3e9a]] - KPS – Vibrio | + | **[[3e9a]] - KPS – ''Vibrio cholerae''<br /> |
| - | **[[3fs2]] - KPS – Brucella melitensis<br /> | + | **[[3fs2]] - KPS – ''Brucella melitensis''<br /> |
**[[3qq1]], [[3stg]] - NmKPS (mutant) <br /> | **[[3qq1]], [[3stg]] - NmKPS (mutant) <br /> | ||
| - | **[[3t4c]], [[3tml]] - KPS – Burkholderia ambifaria | + | **[[3t4c]], [[3tml]] - KPS – ''Burkholderia ambifaria'' |
*''Non-metallo Kdo8P binary complex'' | *''Non-metallo Kdo8P binary complex'' | ||
Revision as of 09:38, 5 April 2016
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
- ↑ 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
- ↑ 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
