This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Homocitrate synthase
From Proteopedia
Contents |
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 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 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
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
