Homocitrate synthase
From Proteopedia
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- | + | <StructureSection load='3ivt' size='400' side='right' scene='' caption='Fission yeast homocitrate synthase Lys4 dimer complex with 2-oxoglutarate, Na+ (purple) and Zn+2 (grey) ions [[3ivt]]'> | |
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== Function == | == 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<ref>PMID:5836514</ref>. | ||
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== Structural highlights == | == 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>. | 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>. | ||
- | + | </StructureSection> | |
== 3D Structures of homocitrate synthase == | == 3D Structures of homocitrate synthase == | ||
Revision as of 11:02, 3 April 2016
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3D Structures of homocitrate synthase
Updated on 03-April-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
References
- ↑ 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