Homocitrate synthase: Difference between revisions

Revision as of 15:54, 16 May 2019

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^[1].

Structural highlights

The HS . . The ^[2]. Water molecules shown as red spheres.

Fission yeast homocitrate synthase Lys4 dimer complex with 2-oxoglutarate, Na+ (purple) and Zn+2 (grey) ions 3ivt

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3D Structures of homocitrate synthase3D Structures of homocitrate synthase

Updated on 16-May-2019

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

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

Michal Harel, Alexander Berchansky

[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

[1]

[2]

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 == Structural highlights ==
-The HS <scene name='46/465446/Cv/6'>active site is located in the interior of the N-terminal TIM-barrel domain</scene>. <scene name='46/465446/Cv/3'>Whole active site</scene>. The <scene name='46/465446/Cv/5'>metal ion is octahedrally coordinated to the protein and to the 2-oxoglutarate</scene><ref>PMID:19776021</ref>. Water molecules shown as red spheres.
+The HS <scene name='46/465446/Cv/7'>active site is located in the interior of the N-terminal TIM-barrel domain</scene>. <scene name='46/465446/Cv/8'>Active site</scene>. The <scene name='46/465446/Cv/9'>metal ion is octahedrally coordinated to the protein and to the 2-oxoglutarate</scene><ref>PMID:19776021</ref>. Water molecules shown as red spheres.
 </StructureSection>
 == 3D Structures of homocitrate synthase ==