Glyoxylate cycle

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(New page: <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'>...)
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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'>
<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'>
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This is a default text for your page '''Glyoxylate cycle'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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The glyoxylate cycle, a variation of the [[tricarboxylic acid cycle]], is an anabolic pathway occurring in plants, bacteria, protists, and fungi. The glyoxylate cycle centers on the conversion of acetyl-CoA to succinate for the synthesis of carbohydrates.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Function ==
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The glyoxylate cycle uses six of the eight enzymes associated with the tricarboxylic acid cycle: citrate synthase, aconitase, succinate dehydrogenase, fumarase, and malate dehydrogenase.
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== Disease ==
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[[Citrate Synthase]]
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== Relevance ==
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4C <scene name='43/430893/Cv/3'>oxaloacetate</scene> to a 6C molecule <scene name='43/430893/Cv/4'>citrate</scene>
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== Structural highlights ==
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[[Aconitase]]
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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6C Citrate => 6C <scene name='43/430893/Cv/5'>cis-Aconitate</scene>
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6C ''cis''-Aconitate => 6C <scene name='43/430893/Cv/6'>Isocitrate</scene>
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[[Succinate Dehydrogenase]]
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<scene name='43/430893/Cv/10'>Succinate</scene> => <scene name='43/430893/Cv/11'>Fumarate</scene>
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[[Fumarase]]
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Fumarate => <scene name='43/430893/Cv/12'>L-Malate</scene>
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[[Malate dehydrogenase]]
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L-Malate => <scene name='43/430893/Cv/3'>oxaloacetate</scene>
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The two cycles differ in that in the glyoxylate cycle, <scene name='43/430893/Cv/6'>isocitrate</scene> is converted into <scene name='93/939250/Cv/1'>glyoxylate</scene> and <scene name='43/430893/Cv/10'>succinate</scene> by isocitrate lyase (ICL) instead of into α-ketoglutarate. This bypasses the decarboxylation steps that take place in the citric acid cycle, allowing simple carbon compounds to be used in the later synthesis of macromolecules, including glucose. Glyoxylate is subsequently combined with acetyl-CoA to produce malate, catalyzed by malate synthase. Malate is also formed in parallel from succinate by the action of succinate dehydrogenase and fumarase.
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*[[Malate synthase]]
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<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>.
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Current revision

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

References

  1. ↑ 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?)

Alexander Berchansky

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