Malate synthase
From Proteopedia
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(New page: <StructureSection load='1n8w' size='350' side='right' caption='Structure of malate synthase complex with CoA, glyoxylate and Mg+2 ion (PDB entry 1n8w)' scene=''> '''Malate syntha...) |
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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. | ||
- | + | See also: [[Glyoxylate cycle]] | |
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- | == | + | == 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>. | ||
- | = | + | <scene name='57/573146/Cv/9'>Malate/Mg+2 ion binding site</scene>. Water molecules are shown as red spheres. |
- | + | <scene name='57/573146/Cv/10'>Acetyl-CoA binding site</scene>. | |
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- | == | + | ==3d structures of malate synthase== |
- | + | [[Malate synthase 3D structures]] | |
- | [[ | + | |
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- | + | </StructureSection> | |
- | + | == References == | |
- | + | <references/> | |
- | [[ | + | [[Category:Topic Page]] |
Current revision
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References
- ↑ 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
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