Cysteine desulfurase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Cysteine desulfurase''' ( | + | '''Cysteine desulfurase''' (Suf) catalyzes the conversion of L-cysteine to L-alanine and sulfane sulfur. Suf has a role in the biosynthesis of Fe-S custers, thiamine, thionucleosides, biotin, lipoic acid, molybdopterin and NAD<ref>PMID:12382038</ref>. Suf is a PLP-dependent enzyme. |
== Structural highlights == | == Structural highlights == | ||
| - | The structure of | + | The structure of SufS contains the <scene name='80/800705/Cv/2'>cofactor PLP bound to Lys224</scene>. |
*<scene name='80/800705/Cv/4'>All interactions of PLP</scene>. | *<scene name='80/800705/Cv/4'>All interactions of PLP</scene>. | ||
<scene name='80/800705/Cv/5'>Cys361 is the nucleophilic catalytic residue</scene>. The reaction product <scene name='80/800705/Cv/6'>alanine is bound near the Cys361-persulfide</scene><ref>PMID:27382962</ref>. | <scene name='80/800705/Cv/5'>Cys361 is the nucleophilic catalytic residue</scene>. The reaction product <scene name='80/800705/Cv/6'>alanine is bound near the Cys361-persulfide</scene><ref>PMID:27382962</ref>. | ||
Revision as of 09:52, 23 February 2025
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References
- ↑ Mihara H, Esaki N. Bacterial cysteine desulfurases: their function and mechanisms. Appl Microbiol Biotechnol. 2002 Oct;60(1-2):12-23. doi:, 10.1007/s00253-002-1107-4. Epub 2002 Sep 4. PMID:12382038 doi:http://dx.doi.org/10.1007/s00253-002-1107-4
- ↑ Blauenburg B, Mielcarek A, Altegoer F, Fage CD, Linne U, Bange G, Marahiel MA. Crystal Structure of Bacillus subtilis Cysteine Desulfurase SufS and Its Dynamic Interaction with Frataxin and Scaffold Protein SufU. PLoS One. 2016 Jul 6;11(7):e0158749. doi: 10.1371/journal.pone.0158749., eCollection 2016. PMID:27382962 doi:http://dx.doi.org/10.1371/journal.pone.0158749
