Adenylosuccinate lyase

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<StructureSection load='2j91' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load='2x75' size='340' side='right' caption='Adenylsuccinate lyase complex with AMP, oxalate, PEG 400 and Cl- ion (green) (PDB code [[2x75]])' scene=''>
== Function ==
== Function ==
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'''Adenylosuccinate lyase''' (ADSL) is a bifunctional enzyme acting in purine synthesis and purine nucleotide recycling<ref>PMID:10888601</ref>. ADSL caalyzes two reactions: the cleavage of adenylsuccinate to AMP and fumarate and the cleavage of phosphoribosylaminoimidazolesuccinocarboxamide (SAICAR) into 5-aminoimidazole-4-carboxamide (AICAR) and fumarate.
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'''Adenylosuccinate lyase''' (ASL) is a bifunctional enzyme acting in purine synthesis and purine nucleotide recycling<ref>PMID:10888601</ref>. ASL caalyzes two reactions: the cleavage of adenylsuccinate to AMP and fumarate and the cleavage of phosphoribosylaminoimidazolesuccinocarboxamide (SAICAR) into 5-aminoimidazole-4-carboxamide (AICAR) and fumarate.
== Disease ==
== Disease ==
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Mutations in ADSL cause autosomal recessive disorder which manifests itself by encephalopathy with epilepsy and marked psychomotor retardation<ref>PMID:20054783</ref>.
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Mutations in ASL cause autosomal recessive disorder which manifests itself by encephalopathy with epilepsy and marked psychomotor retardation<ref>PMID:20054783</ref>.
== Structural highlights ==
== Structural highlights ==
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The ASL can be divided into 3 domains. The active site is situated between the 3 domains and contains the product AMP and and oxalate<ref>PMID:20693687</ref>.
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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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</StructureSection>
</StructureSection>

Revision as of 09:10, 2 February 2017

Adenylsuccinate lyase complex with AMP, oxalate, PEG 400 and Cl- ion (green) (PDB code 2x75)

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3D structures of adenylosuccinate lyase

Updated on 02-February-2017

References

  1. ↑ Kmoch S, Hartmannova H, Stiburkova B, Krijt J, Zikanova M, Sebesta I. Human adenylosuccinate lyase (ADSL), cloning and characterization of full-length cDNA and its isoform, gene structure and molecular basis for ADSL deficiency in six patients. Hum Mol Genet. 2000 Jun 12;9(10):1501-13. PMID:10888601
  2. ↑ Mierzewska H, Schmidt-Sidor B, Jurkiewicz E, Bogdanska A, Kusmierska K, Stepien T. Severe encephalopathy with brain atrophy and hypomyelination due to adenylosuccinate lyase deficiency--MRI, clinical, biochemical and neuropathological findings of Polish patients. Folia Neuropathol. 2009;47(4):314-20. PMID:20054783
  3. ↑ Fyfe PK, Dawson A, Hutchison MT, Cameron S, Hunter WN. Structure of Staphylococcus aureus adenylosuccinate lyase (PurB) and assessment of its potential as a target for structure-based inhibitor discovery. Acta Crystallogr D Biol Crystallogr. 2010 Aug;66(Pt 8):881-8. Epub 2010, Jul 9. PMID:20693687 doi:10.1107/S0907444910020081

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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