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| Class:Id | Summation:6793620 |
|---|---|
| _displayName | Mitochondrial lipoyl synthase (LIAS) mediates the radical-me... |
| _timestamp | 2024-01-09 09:31:03 |
| created | [InstanceEdit:6793626] Jassal, Bijay, 2015-09-02 |
| modified | [InstanceEdit:9857777] Stephan, Ralf, 2024-01-09 |
| text | Mitochondrial lipoyl synthase (LIAS) mediates the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to glycine cleavage system H protein (GCSH), transforming the octanoyl moiety to a lipoyl moiety. LIAS requires two 4Fe-4S clusters as cofactors, which act as the sulfur donors in the reaction. It also requires ferredoxin FDX1 as a cofactor. Moreover, LIAS is in complex with iron-sulfur cluster scaffold NFU1, which restores the auxiliary cluster of LIAS during turnover (Morikawa et al., 2001; Warui et al., 2022; Dreishpoon et al., 2023; Joshi et al., 2023). Defects in LIAS can cause neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation (HGCLAS, MIM:614462; Mayr et al., 2011; reviewed by Cronan, 2020). |
| (summation) | [Reaction:6793591] LIAS synthesizes lipoyl-GCSH [Homo sapiens] |
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