Homocitrate synthase: Difference between revisions

Latest revision as of 11:43, 27 September 2021

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 27-September-2021

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
6ktq - HS + -ketoglutarate + CoA – Sulfolobus acidocaldarius

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]

@@ Line 1: / Line 1: @@
-<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]]'>
+<StructureSection load='3ivt' size='400' side='right' scene='46/465446/Cv/1' caption='Fission yeast homocitrate synthase Lys4 dimer complex with 2-oxoglutarate, Na+ (purple) and Zn+2 (grey) ions [[3ivt]]'>
 == Function ==
@@ Line 5: / Line 5: @@
 == 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 <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 ==
@@ Line 17: / Line 19: @@
 [[2zyf]] - TtHS + α-ketoglutarate + Mg<br />
 [[2ztk]] – TtHS + homocitrate<br />
-[[3a9i]] – TtHS + lysine
+[[3a9i]] – TtHS + lysine<br />
+[[6ktq]] - HS + -ketoglutarate + CoA – ''Sulfolobus acidocaldarius''<br />
 == References ==
 <references/>
 [[Category:Topic Page]]