Homocitrate synthase: Difference between revisions

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{{STRUCTURE_3ivt|  PDB=3ivt  | SIZE=400| SCENE= |right|CAPTION=Fission yeast homocitrate synthase Lys4 dimer complex with 2-oxoglutarate, Na+ (purple) and Zn+2 (grey) ions [[3ivt]] }}
{{STRUCTURE_3ivt|  PDB=3ivt  | SIZE=400| SCENE= |right|CAPTION=Fission yeast homocitrate synthase Lys4 dimer complex with 2-oxoglutarate, Na+ (purple) and Zn+2 (grey) ions [[3ivt]] }}
== Function ==
'''Homocitrate synthase''' (HS) participates in lysine biosynthesis and pyruvate metabolism.  HS catalyzes the conversion of acetyl-CoA + H2O + 2-oxoglutarate to 2-hydroxybutane-1,2,4-tricarboxylate + CoA<ref>PMID:5836514</ref>.


'''Homocitrate synthase''' (HS) participates in lysine biosynthesis and pyruvate metabolism.  HS catalyzes the conversion of acetyl-CoA + H2O + 2-oxoglutarate to 2-hydroxybutane-1,2,4-tricarboxylate + CoA.
== Structural highlights ==
 
The HS active site is located in the interior of the N-terminal TIM-barrel domain.  The metal ion is octahedrally coordinated to the protein and to the 2-oxoglutarate<ref>PMID:19776021</ref>.  
{{TOC limit|limit=2}}


== 3D Structures of homocitrate synthase ==
== 3D Structures of homocitrate synthase ==
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[[3ivs]] – fyHS Lys4 – fission yeast<br />
[[3ivs]] – fyHS Lys4 – fission yeast<br />
[[3ivt]], [[3ivu]] - fyHS Lys4 + 2-oxoglutaric acid<br />
[[3ivt]], [[3ivu]] - fyHS Lys4 + 2-oxoglutarate<br />
[[3mi3]] - fyHS Lys4 + lysine<br />
[[3mi3]] - fyHS Lys4 + lysine<br />
[[2ztj]] – TtHS + α-ketoglutarate – ''Thermus thermophilus''<br />
[[2ztj]] – TtHS + α-ketoglutarate – ''Thermus thermophilus''<br />
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[[2ztk]] – TtHS + homocitrate<br />
[[2ztk]] – TtHS + homocitrate<br />
[[3a9i]] – TtHS + lysine
[[3a9i]] – TtHS + lysine
 
== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 13:42, 24 March 2016

Template:STRUCTURE 3ivt

FunctionFunction

Homocitrate synthase (HS) participates in lysine biosynthesis and pyruvate metabolism. HS catalyzes the conversion of acetyl-CoA + H2O + 2-oxoglutarate to 2-hydroxybutane-1,2,4-tricarboxylate + CoA[1].

Structural highlightsStructural highlights

The HS active site is located in the interior of the N-terminal TIM-barrel domain. The metal ion is octahedrally coordinated to the protein and to the 2-oxoglutarate[2].

3D Structures of homocitrate synthase3D Structures of homocitrate synthase

Updated on 24-March-2016

3ivs – fyHS Lys4 – fission yeast
3ivt, 3ivu - fyHS Lys4 + 2-oxoglutarate
3mi3 - fyHS Lys4 + lysine
2ztj – TtHS + α-ketoglutarate – Thermus thermophilus
2zyf - TtHS + α-ketoglutarate + Mg
2ztk – TtHS + homocitrate
3a9i – TtHS + lysine

ReferencesReferences

  1. Strassman M, Ceci LN. Enzymatic formation of homocitric acid, an intermediate in lysine biosynthesis. Biochem Biophys Res Commun. 1964;14:262-7. PMID:5836514
  2. Bulfer SL, Scott EM, Couture JF, Pillus L, Trievel RC. Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis. J Biol Chem. 2009 Dec 18;284(51):35769-80. Epub . PMID:19776021 doi:10.1074/jbc.M109.046821

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

Michal Harel, Alexander Berchansky