Adenylosuccinate lyase

From Proteopedia

spinqualitylabelsall models Adenylsuccinate lyase complex with AMP, oxalate, PEG 400 and Cl- ion (green) (PDB code 2x75) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Structural highlights 4 3D structures of adenylosuccinate lyase Function Adenylosuccinate lyase (ASL) is a bifunctional enzyme acting in purine synthesis and purine nucleotide recycling[1]. 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 Mutations in ASL cause autosomal recessive disorder which manifests itself by encephalopathy with epilepsy and marked psychomotor retardation[2]. Structural highlights The ASL can be divided into 3 domains. The is situated between the 3 domains and contains the product AMP and and oxalate[3]. Water molecules are shown as red spheres. . 3D structures of adenylosuccinate lyase Adenylosuccinate lyase 3D structures

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