SAICAR synthetase: Difference between revisions
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<StructureSection load='4fe2' size=' | <StructureSection load='4fe2' size='450' side='right' caption='SAICAR synthetase complex with aminoimidazole-ribonucleotide, ADP, TRIS, aspartate, acetate, Mg+2 and Cl- ions (PDB code [[4fe2]]) ' scene='74/749400/Cv/1'> | ||
== Function == | == Function == |
Revision as of 15:49, 27 December 2016
FunctionSAICAR synthetase (SAI) or phosphoribosylaminoimidazole-succinocarboxamide synthetase is part of the purine biosynthesis. SAI catalyzes ATP-dependent ligation of carboxyaminoimidazole ribotide (AICAR) with aspartate[1]. Structural highlightsSAI structure shows two domains. The active site is located in a hydrophilic tunnel between the 2 domains and contains ADP, aspartic acid and aminoimidazole-ribonucleotide (AIR)[2].
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3D structures of SAICAR synthetase3D structures of SAICAR synthetase
Updated on 27-December-2016
ReferencesReferences
- ↑ Manjunath K, Jeyakanthan J, Sekar K. Catalytic pathway, substrate binding and stability in SAICAR synthetase: A structure and molecular dynamics study. J Struct Biol. 2015 Jul;191(1):22-31. doi: 10.1016/j.jsb.2015.06.006. Epub 2015, Jun 10. PMID:26072057 doi:http://dx.doi.org/10.1016/j.jsb.2015.06.006
- ↑ Wolf NM, Abad-Zapatero C, Johnson ME, Fung LW. Structures of SAICAR synthetase (PurC) from Streptococcus pneumoniae with ADP, Mg(2+), AIR and Asp. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):841-50. doi:, 10.1107/S139900471303366X. Epub 2014 Feb 22. PMID:24598753 doi:http://dx.doi.org/10.1107/S139900471303366X