7xej

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/SUFS_BACSU SUFS_BACSU] Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40-to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity.<ref>PMID:20097860</ref> <ref>PMID:20822158</ref> <ref>PMID:21744456</ref>
[https://www.uniprot.org/uniprot/SUFS_BACSU SUFS_BACSU] Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40-to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity.<ref>PMID:20097860</ref> <ref>PMID:20822158</ref> <ref>PMID:21744456</ref>
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== Publication Abstract from PubMed ==
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The reactivity of pyridoxal-5'-phosphate (PLP) with cysteine and its derivatives has been of increasing interest because the corresponding product, a thiazolidine PLP-cysteine adduct, can be formed via PLP-dependent enzymatic and non-enzymatic reactions. Here, we report biochemical and X-ray crystallographic snapshots of thiazolidine formation in reaction of D-cysteine with PLP in SufS, a PLP-dependent L-cysteine desulfurase. By comparing L- and D-penicillamine-bound SufS showing no thiazolidine formation in the crystals with D-cysteine SufS, we proposed a thiazolidine formation mechanism with important factors: the polar environments provided by the carbonyl groups of Ala28-Ala29 and Lys224-mediated base catalysis for the nucleophilic thiolate of D-cysteine.
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Visualizing thiazolidine ring formation in the reaction of D-cysteine and pyridoxal-5'-phosphate within L-cysteine desulfurase SufS.,Nakamura R, Fujishiro T Biochem Biophys Res Commun. 2025 Mar 25;754:151497. doi: , 10.1016/j.bbrc.2025.151497. Epub 2025 Feb 19. PMID:40020322<ref>PMID:40020322</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
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Current revision

SufS with D-cysteine for 5 min

PDB ID 7xej

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