Malate synthase: Difference between revisions

Latest revision as of 12:03, 11 January 2023

Function

Malate synthase (MS) catalyzes the reversible conversion of acetyl-CoA, glyoxylate and water to (S)-malate and CoA. MS participates in pyruvate, glyoxylate and dicarboxylate metabolism. There are 2 isozymes of MS. MS G is formed during growth on glycolate^[1] and MS A which metabolizes glyoxylate formed in the dissimilation of acetate.

Structural highlights

. The ternary complex contains malate, acetyl-CoA and Mg+2 ion^[2].

. Water molecules are shown as red spheres.

.

3d structures of malate synthase

Malate synthase 3D structures

Structure of malate synthase G complex with CoA, malate, Hepes and Mg+2 ion (green) (PDB entry 2gq3)

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Anstrom DM, Kallio K, Remington SJ. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution. Protein Sci. 2003 Sep;12(9):1822-32. PMID:12930982
↑ Anstrom DM, Remington SJ. The product complex of M. tuberculosis malate synthase revisited. Protein Sci. 2006 Aug;15(8):2002-7. PMID:16877713 doi:15/8/2002

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

Michal Harel, Alexander Berchansky, Joel L. Sussman, Karsten Theis

[1] Anstrom DM, Kallio K, Remington SJ. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution. Protein Sci. 2003 Sep;12(9):1822-32. PMID:12930982

[2] Anstrom DM, Remington SJ. The product complex of M. tuberculosis malate synthase revisited. Protein Sci. 2006 Aug;15(8):2002-7. PMID:16877713 doi:15/8/2002

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+<StructureSection load='' size='350' side='right' caption='Structure of malate synthase G complex with CoA, malate, Hepes and Mg+2 ion (green) (PDB entry [[2gq3]])' scene='57/573146/Cv/1'>
+== Function ==
+'''Malate synthase''' (MS) catalyzes the reversible conversion of acetyl-CoA, glyoxylate and water to [[R/S nomenclature|(S)]]-malate and CoA.  MS participates in pyruvate, glyoxylate and dicarboxylate metabolism.  There are 2 isozymes of MS.  '''MS G''' is formed during growth on glycolate<ref>PMID:12930982</ref> and '''MS A''' which metabolizes glyoxylate formed in the dissimilation of acetate.
-<StructureSection load='1n8w' size='350' side='right' caption='Structure of malate synthase complex with CoA, glyoxylate and Mg+2 ion (PDB entry [[1n8w]])' scene=''>
+See also: [[Glyoxylate cycle]]
-'''Malate synthase''' (MS) catalyzes the reversible conversion of acetyl-CoA, glyoxylate and water to (S)-malate and CoA.  MS participates in pyruvate, glyoxylate and dicarboxylate metabolism.  There are 2 isozymes of MS.  '''MS G''' is formed during growth on glycolate and '''MS A''' which metabolizes glyoxylate formed in the dissimilation of acetate.
-==3d structures of malate synthase==
+== Structural highlights ==
+<scene name='57/573146/Cv/8'>MS active site pocket is situated between the TIM barrel and the C-terminal</scene>.  The ternary complex contains malate, acetyl-CoA and Mg+2 ion<ref>PMID:16877713</ref>.
-===Malate synthase G===
+<scene name='57/573146/Cv/9'>Malate/Mg+2 ion binding site</scene>. Water molecules  are shown as red spheres.
-[[1y8b]], [[2jqx]] – EcMS (mutant) – ''Escherichia coli'' - NMR<br />
+<scene name='57/573146/Cv/10'>Acetyl-CoA binding site</scene>.
-[[4ex4]] – MS + Mg – ''Mycobacterium leprae''<br />
-===Malate synthase G binary complex===
+==3d structures of malate synthase==
+[[Malate synthase 3D structures]]
-[[1d8c]] – EcMS (mutant) + glyoxylate + Mg <br />
-[[1n8i]] – MtMS + glyoxylate + Mg – ''Mycobacterium tuberculosis''<br />
-[[3s9i]], [[3s9z]], [[3sad]], [[3saz]], [[3sb0]] – MtMS (mutant) + inhibitor + Mg <br />
-===Malate synthase G ternary complex===
+</StructureSection>
-[[1p7t]] – EcMS (mutant) + pyruvate + Mg + acetyl-CoA<br />
+== References ==
-[[1n8w]] – MtMS + glyoxylate + Mg + CoA<br />
+<references/>
-[[2gq3]] – MtMS + malate + Mg + CoA<br />
+[[Category:Topic Page]]