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>. | |||
== 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>. | |||
== 3D Structures of homocitrate synthase == | == 3D Structures of homocitrate synthase == | ||
Line 10: | Line 11: | ||
[[3ivs]] – fyHS Lys4 – fission yeast<br /> | [[3ivs]] – fyHS Lys4 – fission yeast<br /> | ||
[[3ivt]], [[3ivu]] - fyHS Lys4 + 2- | [[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 /> | ||
Line 16: | Line 17: | ||
[[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
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
- ↑ Strassman M, Ceci LN. Enzymatic formation of homocitric acid, an intermediate in lysine biosynthesis. Biochem Biophys Res Commun. 1964;14:262-7. PMID:5836514
- ↑ 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