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Kdo-8-phosphate synthase
From Proteopedia
(Difference between revisions)
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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 == | ||
| - | '''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). '''Metallo KPS''' is a metal-requiring enzyme while '''Non-metallo KPS''' does not require a divalent cation for its activity. | + | '''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-P is found in cell walls of higher plants and some green algae<ref>PMID:11904225</ref>. | + | |
== Structural highlights == | == Structural highlights == | ||
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**[[1fxp]] - AaKPS + Cd – ''Aquifex aeolicus''<br /> | **[[1fxp]] - AaKPS + Cd – ''Aquifex aeolicus''<br /> | ||
**[[1lrn]], [[1t99]] - AaKPS (mutant) + Cd<br /> | **[[1lrn]], [[1t99]] - AaKPS (mutant) + Cd<br /> | ||
| + | **[[1fx6]] - AaKPS <br /> | ||
| + | **[[2nws]], [[2nx3]] - AaKPS (mutant) <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 /> | ||
| + | **[[3qq1]], [[3stg]] - NmKPS (mutant) <br /> | ||
**[[3sz8]] – BpKPS-2 – ''Burkholderia pseudomallei''<br /> | **[[3sz8]] – BpKPS-2 – ''Burkholderia pseudomallei''<br /> | ||
**[[4lu0]] – KPS – ''Pseudomonas aeruginosa''<br /> | **[[4lu0]] – KPS – ''Pseudomonas aeruginosa''<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]] - | + | **[[2a21]] - AaKPS + PEP + Zn <br /> |
**[[1jcx]], [[1pcw]] - AaKPS + inhibitor + Cd<br /> | **[[1jcx]], [[1pcw]] - AaKPS + inhibitor + Cd<br /> | ||
**[[1fy6]] - AaKPS + A5P + Cd<br /> | **[[1fy6]] - AaKPS + A5P + Cd<br /> | ||
**[[3e12]] - AaKPS + Kdo-8-P + Cu<br /> | **[[3e12]] - AaKPS + Kdo-8-P + Cu<br /> | ||
| + | **[[2nxi]], [[1fwn]] - AaKPS + PEP<br /> | ||
| + | **[[2nwr]], [[2nxh]] - AaKPS (mutant) + PEP<br /> | ||
**[[3fyp]] - NmKPS (mutant) + PEP + Mn<br /> | **[[3fyp]] - NmKPS (mutant) + PEP + Mn<br /> | ||
**[[3tmq]] - BpKPS + arabinose-5-phosphate<br /> | **[[3tmq]] - BpKPS + arabinose-5-phosphate<br /> | ||
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**[[2a2i]] - AaKPS + A5P + PEP + Zn<br /> | **[[2a2i]] - AaKPS + A5P + PEP + Zn<br /> | ||
**[[1lrq]], [[1t8x]] - AaKPS (mutant) + A5P + PEP + Cd<br /> | **[[1lrq]], [[1t8x]] - AaKPS (mutant) + A5P + PEP + Cd<br /> | ||
| + | **[[1fxq]] - AaKPS + A5P + PEP<br /> | ||
| + | **[[2nx1]], [[2ef9]] - AaKPS (mutant) + A5P + PEP<br /> | ||
| + | **[[2nxg]] - AaKPS (mutant) + octanoic acid derivative + A5P + PEP<br /> | ||
**[[3und]] - BpKPS + arabinose-5-phosphate + PEP<br /> | **[[3und]] - BpKPS + arabinose-5-phosphate + PEP<br /> | ||
*Non-metallo Kdo8P | *Non-metallo Kdo8P | ||
| - | **[[1d9e]], [[1gg0]], [[1x8f]] – EcKPS | + | **[[1d9e]], [[1gg0]], [[1x8f]] – EcKPS - ''Escherichia coli''<br /> |
| - | + | ||
| - | + | ||
**[[1o60]] - KPS – ''Haemophilus influenza''<br /> | **[[1o60]] - KPS – ''Haemophilus influenza''<br /> | ||
**[[3e9a]] - KPS – ''Vibrio cholerae''<br /> | **[[3e9a]] - KPS – ''Vibrio cholerae''<br /> | ||
**[[3fs2]] - KPS – ''Brucella melitensis''<br /> | **[[3fs2]] - KPS – ''Brucella melitensis''<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'' | ||
| - | **[[2nxi]], [[1fwn]] - AaKPS + PEP<br /> | ||
| - | **[[2nwr]], [[2nxh]] - AaKPS (mutant) + PEP<br /> | ||
**[[1g7u]], [[1q3n]] - EcKPS + PEP<br /> | **[[1g7u]], [[1q3n]] - EcKPS + PEP<br /> | ||
**[[1phq]], [[1pl9]] - EcKPS + PEP derivative<br /> | **[[1phq]], [[1pl9]] - EcKPS + PEP derivative<br /> | ||
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**[[1x6u]] - EcKPS + Kdo-8-P | **[[1x6u]] - EcKPS + Kdo-8-P | ||
| - | *''Non-metallo Kdo8P ternary complex'' | ||
| - | |||
| - | **[[1fxq]] - AaKPS + A5P + PEP<br /> | ||
| - | **[[2nx1]], [[2ef9]] - AaKPS (mutant) + A5P + PEP<br /> | ||
| - | **[[2nxg]] - AaKPS (mutant) + octanoic acid derivative + A5P + PEP<br /> | ||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 10:21, 6 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). 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
- ↑ 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
