Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions.
Pathway
Metabolism; Metabolism of vitamins and cofactors; Metabolism of water-soluble vitamins and cofactors; Molybdenum cofactor biosynthesis; Sulfur relay system; molybdenum cofactor biosynthesis;
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Citations
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Huang, JS; Mukerjee, S; et al. Molybdenum - Iron sulfide-bridged double cubanes. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 119:8662-8674(1997).
Lim, BS; Donahue, JP; et al. Synthesis and structures of bis(dithiolene)molybdenum complexes related to the active sites of the DMSO reductase enzyme family. INORGANIC CHEMISTRY 39:263-273(2000).
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